ID   ANFY1_HUMAN    STANDARD;      PRT;  1169 AA.
AC   Q9P2R3; Q9ULG5;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   18-APR-2006, entry version 34.
DE   Ankyrin repeat and FYVE domain-containing protein 1 (Ankyrin repeats
DE   hooked to a zinc finger motif).
GN   Name=ANKFY1; Synonyms=ANKHZN, KIAA1255;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Fetal brain;
RX   MEDLINE=20400338; PubMed=10940552; DOI=10.1016/S0378-1119(00)00247-X;
RA   Kuriyama H., Asakawa S., Minoshima S., Maruyama H., Ishii N., Ito K.,
RA   Gejyo F., Arakawa M., Shimizu N., Kuwano R.;
RT   "Characterization and chromosomal mapping of a novel human gene,
RT   ANKHZN.";
RL   Gene 253:151-160(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   MEDLINE=20039619; PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA   Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XV.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 6:337-345(1999).
RN   [3]
RP   SEQUENCE REVISION.
RX   MEDLINE=22158633; PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA   Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT   "Construction of expression-ready cDNA clones for KIAA genes: manual
RT   curation of 330 KIAA cDNA clones.";
RL   DNA Res. 9:99-106(2002).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome; endosomal membrane;
CC       peripheral membrane protein. Also associated with endosomal
CC       membranes.
CC   -!- TISSUE SPECIFICITY: High expression in whole adult brain and
CC       intermediate expression in all other tissues and specific brain
CC       regions examined, including fetal brain.
CC   -!- SIMILARITY: Contains 21 ANK repeats.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
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DR   EMBL; AB037360; BAA90300.1; -; mRNA.
DR   EMBL; AB033081; BAA86569.2; ALT_INIT; mRNA.
DR   UniGene; Hs.513875; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSG00000185722; Homo sapiens.
DR   HGNC; HGNC:20763; ANKFY1.
DR   MIM; 607927; gene.
DR   GO; GO:0010008; C:endosome membrane; ISS.
DR   GO; GO:0006897; P:endocytosis; ISS.
DR   InterPro; IPR002110; ANK.
DR   InterPro; IPR000210; BTB.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF00023; Ank; 21.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 16.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00064; FYVE; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 12.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   ANK repeat; Membrane; Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1   1169       Ankyrin repeat and FYVE domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000066890.
FT   DOMAIN       68    130       BTB.
FT   REPEAT      217    247       ANK 1.
FT   REPEAT      255    284       ANK 2.
FT   REPEAT      288    317       ANK 3.
FT   REPEAT      322    362       ANK 4.
FT   REPEAT      366    396       ANK 5.
FT   REPEAT      490    519       ANK 6.
FT   REPEAT      542    572       ANK 7.
FT   REPEAT      588    617       ANK 8.
FT   REPEAT      621    650       ANK 9.
FT   REPEAT      654    683       ANK 10.
FT   REPEAT      687    716       ANK 11.
FT   REPEAT      724    753       ANK 12.
FT   REPEAT      769    798       ANK 13.
FT   REPEAT      802    832       ANK 14.
FT   REPEAT      836    865       ANK 15.
FT   REPEAT      870    899       ANK 16.
FT   REPEAT      905    934       ANK 17.
FT   REPEAT      938    967       ANK 18.
FT   REPEAT      971   1001       ANK 19.
FT   REPEAT     1005   1037       ANK 20.
FT   REPEAT     1043   1072       ANK 21.
FT   ZN_FING    1104   1164       FYVE-type.
FT   CONFLICT      1      4       MAEE -> AGGK (in Ref. 2).
FT   CONFLICT     48     48       E -> K (in Ref. 1).
FT   CONFLICT    115    115       M -> V (in Ref. 1).
FT   CONFLICT    207    207       A -> P (in Ref. 1).
FT   CONFLICT    235    235       F -> S (in Ref. 1).
FT   CONFLICT    270    270       S -> N (in Ref. 1).
FT   CONFLICT    283    291       DMVDKSGWS -> AWWPRVLE (in Ref. 1).
FT   CONFLICT    299    300       RG -> E (in Ref. 1).
FT   CONFLICT    322    322       A -> C (in Ref. 1).
FT   CONFLICT    336    337       KK -> RN (in Ref. 1).
FT   CONFLICT    379    379       N -> D (in Ref. 1).
FT   CONFLICT    385    385       Q -> H (in Ref. 1).
FT   CONFLICT    645    645       Q -> R (in Ref. 1).
FT   CONFLICT    652    654       TQD -> PQA (in Ref. 1).
FT   CONFLICT    687    687       K -> E (in Ref. 1).
FT   CONFLICT    713    713       D -> G (in Ref. 1).
FT   CONFLICT    784    784       Missing (in Ref. 1).
FT   CONFLICT    795    795       N -> D (in Ref. 1).
FT   CONFLICT    798    798       A -> P (in Ref. 1).
FT   CONFLICT    807    807       I -> C (in Ref. 1).
FT   CONFLICT    827    829       DIH -> ISS (in Ref. 1).
FT   CONFLICT    835    835       R -> K (in Ref. 1).
FT   CONFLICT    849    849       N -> D (in Ref. 1).
FT   CONFLICT    860    860       E -> G (in Ref. 1).
FT   CONFLICT    874    874       F -> S (in Ref. 1).
FT   CONFLICT    889    889       F -> S (in Ref. 1).
FT   CONFLICT    901    901       V -> A (in Ref. 1).
FT   CONFLICT    905    905       S -> P (in Ref. 1).
FT   CONFLICT    913    913       A -> V (in Ref. 1).
FT   CONFLICT    916    916       A -> E (in Ref. 1).
FT   CONFLICT    933    933       N -> T (in Ref. 1).
FT   CONFLICT    940    940       Q -> K (in Ref. 1).
FT   CONFLICT    949    949       Q -> E (in Ref. 1).
FT   CONFLICT    962    962       G -> A (in Ref. 1).
FT   CONFLICT   1120   1120       T -> A (in Ref. 1).
FT   CONFLICT   1157   1157       N -> T (in Ref. 1).
SQ   SEQUENCE   1169 AA;  128399 MW;  589297CA4ACDDB56 CRC64;
     MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCALLAAQ ANKESSSESF ISRLLAIVAD
     LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TKELDLSDAN PEVTMTMLRW
     IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
     TLMNYCAEII ASHWDDLRKE DFSSMSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
     MDSQLPGKLN EADHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKSGW SLLHKGIQRG
     DLFAATFLIK NGAFVNAATL GAQETPLHLV ALYSSKKHSA DVMSEMAQIA EALLQAGANP
     NMQDSKGRTP LHVSIMAGNE YVFSQLLQCK QLDLELKDHE GSTALWLAVQ HITVSSDQSV
     NPFEDVPVVN GTSFDENSFA ARLIQRGSHT DAPDTATGNC LLQRAAGAGN EAAALFLATN
     GAHVNHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALPLPKE AASLTSLADS
     VHLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
     MHTIAAQLLG SGAAINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
     LAIRNQLPLV VDAICTRGAD MSVPDEKGNP PLWLALANNL EDIASTLVRH GCDATCWGPG
     PGGCLQTLLH RAIDENNEPT ACFLIRSGCD VNSPRQPGAN GEGEEEARDG QTPLHLAASW
     GLEETVQCLL EFGANVNAQD AEGRTPIHVA ISSQHGVIIQ LLVSHPDIHL NVRDRQGLTP
     FACAMTFKNN KSAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVHANVNSR
     VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
     NGVDFAAVDE NGNNALHLAV MHGRLNNIRV LLTECTVDAE AFNLRGQSPL HILGQYGKEN
     AAAIFDLFLE CMPGYPLDKP DADGSTVLLL AYMKGNANLC RAIVRSGARL GVNNNQGVNI
     FNYQVATKQL LFRLLDMLSK EPPWCDGSYC YECTARFGVT TRKHHCRHCG RLLCHKCSTK
     EIPIIKFDLN KPVRVCNICF DVLTLGGVS
//
ID   ANFY1_MOUSE    STANDARD;      PRT;  1169 AA.
AC   Q810B6; O54807; Q80TG6; Q80UH8;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   30-MAY-2006, entry version 29.
DE   Ankyrin repeat and FYVE domain-containing protein 1 (Ankyrin repeats
DE   hooked to a zinc finger motif).
GN   Name=Ankfy1; Synonyms=Ankhzn, Kiaa1255;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND SUBCELLULAR LOCATION.
RX   MEDLINE=99194578; PubMed=10092534; DOI=10.1006/bbrc.1999.0430;
RA   Ito K., Ishii N., Miyashita A., Tominaga K., Kuriyama H., Maruyama H.,
RA   Shirai M., Naito M., Arakawa M., Kuwano R.;
RT   "Molecular cloning of a novel 130-kDa cytoplasmic protein, Ankhzn,
RT   containing ankyrin repeats hooked to a zinc finger motif.";
RL   Biochem. Biophys. Res. Commun. 257:206-213(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2), AND SEQUENCE REVISION.
RA   Maruyama H., Kuriyama H., Ishii N., Ito K., Odani S., Kuwano R.;
RT   "Genomic organization, alternative splicing, and promoter assay of the
RT   mouse Ankhzn gene.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 994-1169.
RC   TISSUE=Brain;
RX   MEDLINE=22579291; PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   II. The complete nucleotide sequences of 400 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome; endosomal membrane;
CC       peripheral membrane protein. Also associated with endosomal
CC       membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q810B6-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q810B6-2; Sequence=VSP_007917, VSP_007918;
CC   -!- SIMILARITY: Contains 21 ANK repeats.
CC   -!- SIMILARITY: Contains 1 BTB (POZ) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
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DR   EMBL; AB011370; BAA24980.2; -; mRNA.
DR   EMBL; AB098329; BAC67211.1; -; mRNA.
DR   EMBL; AB098157; BAC67389.1; -; Genomic_DNA.
DR   EMBL; AB098157; BAC67388.1; -; Genomic_DNA.
DR   EMBL; AK122479; BAC65761.1; -; mRNA.
DR   UniGene; Mm.10313; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSMUSG00000020790; Mus musculus.
DR   MGI; MGI:1337008; Ankfy1.
DR   GO; GO:0010008; C:endosome membrane; IDA.
DR   GO; GO:0006897; P:endocytosis; NAS.
DR   InterPro; IPR002110; ANK.
DR   InterPro; IPR000210; BTB.
DR   InterPro; IPR013069; BTB_POZ.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF00023; Ank; 21.
DR   Pfam; PF00651; BTB; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 15.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00064; FYVE; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 11.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Alternative splicing; ANK repeat; Membrane; Metal-binding; Repeat;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1169       Ankyrin repeat and FYVE domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000066891.
FT   DOMAIN       68    130       BTB.
FT   REPEAT      217    247       ANK 1.
FT   REPEAT      255    284       ANK 2.
FT   REPEAT      288    317       ANK 3.
FT   REPEAT      322    362       ANK 4.
FT   REPEAT      366    396       ANK 5.
FT   REPEAT      490    519       ANK 6.
FT   REPEAT      542    572       ANK 7.
FT   REPEAT      588    617       ANK 8.
FT   REPEAT      621    650       ANK 9.
FT   REPEAT      654    683       ANK 10.
FT   REPEAT      687    716       ANK 11.
FT   REPEAT      724    753       ANK 12.
FT   REPEAT      769    798       ANK 13.
FT   REPEAT      802    832       ANK 14.
FT   REPEAT      836    865       ANK 15.
FT   REPEAT      870    899       ANK 16.
FT   REPEAT      905    934       ANK 17.
FT   REPEAT      938    967       ANK 18.
FT   REPEAT      971   1001       ANK 19.
FT   REPEAT     1005   1037       ANK 20.
FT   REPEAT     1043   1072       ANK 21.
FT   ZN_FING    1104   1164       FYVE-type.
FT   VAR_SEQ     392    439       LDLELKDHEGSTALWLAVQYITVSSDQSVNPFEDLPVVNGT
FT                                SFDENSL -> YVGRPGEMQSGCEGGIIRFRAERSRRQHCT
FT                                LAGRPVHHCVFRPVCKPL (in isoform 2).
FT                                /FTId=VSP_007917.
FT   VAR_SEQ     440   1169       Missing (in isoform 2).
FT                                /FTId=VSP_007918.
FT   CONFLICT    439    439       L -> F (in Ref. 1; BAC67389).
FT   CONFLICT    448    448       S -> T (in Ref. 1; BAC67389).
FT   CONFLICT    502    502       G -> V (in Ref. 1; BAC67389).
FT   CONFLICT    527    527       L -> V (in Ref. 1; BAC67389).
FT   CONFLICT    840    840       P -> S (in Ref. 1; BAC67389).
SQ   SEQUENCE   1169 AA;  128604 MW;  A78E5406A0AD0165 CRC64;
     MAEEEVAKLE KHLMLLRQEY VKLQKKLAET EKRCTLLAAQ ANKENSNESF ISRLLAIVAG
     LYEQEQYSDL KIKVGDRHIS AHKFVLAARS DSWSLANLSS TEEIDLSDAN PEVTMTIVRW
     IYTDELEFRE DDVFLTELMK LANRFQLQLL RERCEKGVMS LVNVRNCIRF YQTAEELNAS
     TLMNYCAEII ASHWDDLRKE DFSSLSAQLL YKMIKSKTEY PLHKAIKVER EDVVFLYLIE
     MDSQLPGKLN ETDHNGDLAL DLALSRRLES IATTLVSHKA DVDMVDKNGW SLLHKGIQRG
     DLFASTFLIK NGALVNAATA GAQETPLHLV ALYSPKKYSA DVMSEMAQIA EALLQAGANP
     NMQDSKGRTP LHLSIMARND CVFSQLLQCK QLDLELKDHE GSTALWLAVQ YITVSSDQSV
     NPFEDLPVVN GTSFDENSLA ARLIQRGSNT DAPDVMTGNC LLQRAAGAGN EAAALFLATS
     GAHANHRNKW GETPLHTACR HGLANLTAEL LQQGANPNLQ TEEALTLPKE SPVLMSSADS
     IYLQTPLHMA IAYNHPDVVS VILEQKANAL HATNNLQIIP DFSLKDSRDQ TVLGLALWTG
     MHTIAAQLLG SGASINDTMS DGQTLLHMAI QRQDSKSALF LLEHQADINV RTQDGETALQ
     LAIKHQLPLV VDAICTRGAD MSVPDEKGNP PLWLALASNL EDIASTLVRH GCDATCWGPG
     PSGCLQTLLH RAVDENNEST ACFLIRSGCD VNSPRQPGTN GEGEEEARDG QTPLHLAASW
     GLEETVQCLL EFGANVNAQD AEGRTPVHVA ISNQHSVIIQ LLISHPNIEL SVRDRQGLTP
     FACAMTYKNN KAAEAILKRE SGAAEQVDNK GRNFLHVAVQ NSDIESVLFL ISVQANVNSR
     VQDASKLTPL HLAVQAGSEI IVRNLLLAGA KVNELTKHRQ TALHLAAQQD LPTICSVLLE
     NGVDFAAVDE NGNNALHLAV MHGRLNNIRA LLTECTVDAE AFNLRGQSPL HILGQYGKEN
     AAAIFDLFLE CMPEYPLDKP DAEGNTVLLL AYMKGNANLC RAIVRSGVRL GVNNNQGVNI
     FNYQVATKQL LFRLLDMLSK EPPWCDGSNC YECTAKFGVT TRKHHCRHCG RLLCHKCSTK
     EIPIIKFDLN KPVRVCNICF DVLTLGGVS
//
ID   EEA1_HUMAN     STANDARD;      PRT;  1411 AA.
AC   Q15075; Q14221;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-MAY-2006, entry version 45.
DE   Early endosome antigen 1 (Endosome-associated protein p162) (Zinc
DE   finger FYVE domain-containing protein 2).
GN   Name=EEA1; Synonyms=ZFYVE2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   TISSUE=Cervix carcinoma;
RX   MEDLINE=95286647; PubMed=7768953; DOI=10.1074/jbc.270.22.13503;
RA   Mu F.-T., Callaghan J.M., Steele-Mortimer O., Stenmark H.,
RA   Parton R.G., Campbell P.L., McCluskey J., Yeo J.-P., Tock E.P.C.,
RA   Toh B.-H.;
RT   "EEA1, an early endosome-associated protein. EEA1 is a conserved
RT   alpha-helical peripheral membrane protein flanked by cysteine
RT   'fingers' and contains a calmodulin-binding IQ motif.";
RL   J. Biol. Chem. 270:13503-13511(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Seelig H.P.;
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH RAB5A.
RX   MEDLINE=98361239; PubMed=9697774; DOI=10.1038/28879;
RA   Simonsen A., Lippe R., Christoforidis S., Gaullier J.-M., Brech A.,
RA   Callaghan J.M., Toh B.-H., Murphy C., Zerial M., Stenmark H.;
RT   "EEA1 links PI(3)K function to Rab5 regulation of endosome fusion.";
RL   Nature 394:494-498(1998).
RN   [4]
RP   INTERACTION WITH RAB5A AND RAB5B.
RX   MEDLINE=99421752; PubMed=10491193;
RA   Callaghan J.M., Nixon S., Bucci C., Toh B.-H., Stenmark H.;
RT   "Direct interaction of EEA1 with Rab5b.";
RL   Eur. J. Biochem. 265:361-366(1999).
RN   [5]
RP   INTERACTION WITH STX6, AND SUBCELLULAR LOCATION.
RX   MEDLINE=99436077; PubMed=10506127; DOI=10.1074/jbc.274.41.28857;
RA   Simonsen A., Gaullier J.-M., D'Arrigo A., Stenmark H.;
RT   "The Rab5 effector EEA1 interacts directly with syntaxin-6.";
RL   J. Biol. Chem. 274:28857-28860(1999).
RN   [6]
RP   MUTAGENESIS OF ASP-1352; ASN-1357; 1367-VAL-THR-1368; ARG-1375 AND
RP   ARG-1400, HOMODIMERIZATION, AND INTERACTION WITH PHOSPHATIDYLINOSITOL
RP   3-PHOSPHATE.
RX   MEDLINE=99322673; PubMed=10394369; DOI=10.1016/S1097-2765(01)80013-7;
RA   Kutateladze T.G., Ogburn K.D., Watson W.T., de Beer T., Emr S.D.,
RA   Burd C.G., Overduin M.;
RT   "Phosphatidylinositol 3-phosphate recognition by the FYVE domain.";
RL   Mol. Cell 3:805-811(1999).
RN   [7]
RP   MUTAGENESIS OF TRP-1349; CYS-1358; PHE-1365; ARG-1370; ARG-1371;
RP   HIS-1372; HIS-1373; CYS-1374; ARG-1375; CYS-1377; GLY-1378; CYS-1385;
RP   ARG-1400 AND CYS-1405, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP   PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
RX   MEDLINE=20387352; PubMed=10807926; DOI=10.1074/jbc.M906554199;
RA   Gaullier J.-M., Roenning E., Gillooly D.J., Stenmark H.;
RT   "Interaction of the EEA1 FYVE finger with phosphatidylinositol 3-
RT   phosphate and early endosomes. Role of conserved residues.";
RL   J. Biol. Chem. 275:24595-24600(2000).
RN   [8]
RP   INTERACTION WITH RAB22A.
RX   MEDLINE=21859373; PubMed=11870209;
RA   Kauppi M., Simonsen A., Bremnes B., Vieira A., Callaghan J.M.,
RA   Stenmark H., Olkkonen V.M.;
RT   "The small GTPase Rab22 interacts with EEA1 and controls endosomal
RT   membrane trafficking.";
RL   J. Cell Sci. 115:899-911(2002).
RN   [9]
RP   MUTAGENESIS OF GLU-39; PHE-41; ILE-42; PRO-44; MET-47 AND TYR-60,
RP   HOMODIMERIZATION, AND INTERACTION WITH RAB5C.
RX   MEDLINE=22499593; PubMed=12493736; DOI=10.1074/jbc.M211514200;
RA   Merithew E., Stone C., Eathiraj S., Lambright D.G.;
RT   "Determinants of Rab5 interaction with the N-terminus of early
RT   endosome antigen 1.";
RL   J. Biol. Chem. 278:8494-8500(2003).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1289-1411 IN COMPLEX WITH
RP   PHOSPHATIDYLINOSITOL 3-PHOSPHATE, AND HOMODIMERIZATION.
RX   MEDLINE=21617582; PubMed=11741531; DOI=10.1016/S1097-2765(01)00385-9;
RA   Dumas J.J., Merithew E., Sudharshan E., Rajamani D., Hayes S.,
RA   Lawe D., Corvera S., Lambright D.G.;
RT   "Multivalent endosome targeting by homodimeric EEA1.";
RL   Mol. Cell 8:947-958(2001).
RN   [11]
RP   STRUCTURE BY NMR OF 1346-1410 ALONE AND IN COMPLEX WITH
RP   PHOSPHATIDYLINOSITOL 3-PHOSPHATE.
RX   MEDLINE=21143489; PubMed=11230696; DOI=10.1126/science.291.5509.1793;
RA   Kutateladze T.G., Overduin M.;
RT   "Structural mechanism of endosome docking by the FYVE domain.";
RL   Science 291:1793-1796(2001).
CC   -!- FUNCTION: Binds phospholipid vesicles containing
CC       phosphatidylinositol 3-phosphate and participates in endosomal
CC       trafficking.
CC   -!- SUBUNIT: Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and
CC       RAB22A that have been activated by GTP-binding.
CC   -!- INTERACTION:
CC       O15023:kiaa0305; NbExp=1; IntAct=EBI-298113, EBI-298055;
CC       Q9UL26:RAB22A; NbExp=1; IntAct=EBI-298113, EBI-399456;
CC       P20339:RAB5A; NbExp=3; IntAct=EBI-298113, EBI-399437;
CC       P61020:RAB5B; NbExp=1; IntAct=EBI-298113, EBI-399401;
CC       Q63635:Stx6 (xeno); NbExp=2; IntAct=EBI-298113, EBI-398854;
CC       O60784:TOM1; NbExp=1; IntAct=EBI-298113, EBI-74634;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Endosome; early endosome; early
CC       endosomal membrane; peripheral membrane protein.
CC   -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions
CC       with phosphatidylinositol 3-phosphate.
CC   -!- DISEASE: Antibodies against EEA1 are found in sera from patients
CC       with subacute cutaneous lupus erythematosus and other autoimmune
CC       diseases.
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
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DR   EMBL; L40157; AAA79121.1; -; mRNA.
DR   EMBL; X78998; CAA55632.1; -; mRNA.
DR   PIR; A57013; A57013.
DR   UniGene; Hs.567367; -.
DR   PDB; 1HYI; NMR; A=1347-1411.
DR   PDB; 1HYJ; NMR; A=1347-1411.
DR   PDB; 1JOC; X-ray; A/B=1287-1411.
DR   IntAct; Q15075; -.
DR   Ensembl; ENSG00000102189; Homo sapiens.
DR   HGNC; HGNC:3185; EEA1.
DR   MIM; 605070; gene.
DR   GO; GO:0005829; C:cytosol; IDA.
DR   GO; GO:0005769; C:early endosome; IDA.
DR   GO; GO:0019897; C:extrinsic to plasma membrane; IDA.
DR   GO; GO:0005624; C:membrane fraction; TAS.
DR   GO; GO:0005516; F:calmodulin binding; NAS.
DR   GO; GO:0030742; F:GTP-dependent protein binding; IDA.
DR   GO; GO:0005545; F:phosphatidylinositol binding; IDA.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA.
DR   GO; GO:0008270; F:zinc ion binding; TAS.
DR   GO; GO:0045022; P:early endosome to late endosome transport; NAS.
DR   GO; GO:0016189; P:synaptic vesicle to endosome fusion; TAS.
DR   GO; GO:0006906; P:vesicle fusion; IMP.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
KW   3D-structure; Antigen; Coiled coil; Metal-binding; Zinc; Zinc-finger.
FT   CHAIN         1   1411       Early endosome antigen 1.
FT                                /FTId=PRO_0000098706.
FT   ZN_FING      41     64       C2H2-type.
FT   ZN_FING    1352   1410       FYVE-type.
FT   COILED       74   1348       Potential.
FT   COMPBIAS    397    758       Gln/Glu/Lys-rich.
FT   COMPBIAS    937   1032       Gln/Glu/Lys-rich.
FT   COMPBIAS   1093   1231       Glu/Lys-rich.
FT   MUTAGEN      39     39       E->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN      41     41       F->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN      42     42       I->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN      44     44       P->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN      47     47       M->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN      60     60       Y->A: Strongly reduces interaction with
FT                                RAB5C.
FT   MUTAGEN    1349   1349       W->A: Reduces phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1352   1352       D->V: Reduces phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1357   1357       N->D: Reduces phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1358   1358       C->S: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1365   1365       F->A: Strongly reduces
FT                                phosphatidylinositol 3-phosphate binding
FT                                and endosomal location.
FT   MUTAGEN    1367   1368       VT->EE,GG: Abolishes phosphatidylinositol
FT                                3-phosphate binding and endosomal
FT                                location.
FT   MUTAGEN    1370   1370       R->A: Abolishes endosomal location.
FT   MUTAGEN    1371   1371       R->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1372   1372       H->A: Abolishes endosomal location.
FT   MUTAGEN    1373   1373       H->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1374   1374       C->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1375   1375       R->G: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1377   1377       C->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1378   1378       G->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1385   1385       C->A: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   MUTAGEN    1400   1400       R->G: Strongly reduces
FT                                phosphatidylinositol 3-phosphate binding
FT                                and abolishes endosomal location.
FT   MUTAGEN    1405   1405       C->S: Abolishes phosphatidylinositol 3-
FT                                phosphate binding and endosomal location.
FT   CONFLICT    255    255       C -> S (in Ref. 1).
FT   CONFLICT    258    259       LQ -> FE (in Ref. 1).
FT   CONFLICT    277    277       A -> S (in Ref. 1).
FT   CONFLICT    284    284       A -> R (in Ref. 1).
FT   CONFLICT    520    520       D -> E (in Ref. 1).
FT   CONFLICT    575    576       EQ -> DE (in Ref. 1).
FT   CONFLICT    583    584       KL -> NV (in Ref. 1).
FT   CONFLICT    680    680       Q -> H (in Ref. 1).
FT   CONFLICT   1325   1325       Missing (in Ref. 1).
FT   HELIX      1290   1346
FT   HELIX      1352   1354
FT   STRAND     1357   1357
FT   TURN       1359   1361
FT   STRAND     1364   1364
FT   STRAND     1367   1369
FT   STRAND     1372   1373
FT   TURN       1375   1377
FT   STRAND     1380   1381
FT   HELIX      1383   1385
FT   STRAND     1386   1386
FT   STRAND     1388   1390
FT   TURN       1393   1394
FT   STRAND     1396   1397
FT   STRAND     1399   1401
FT   HELIX      1403   1408
FT   TURN       1409   1410
SQ   SEQUENCE   1411 AA;  162466 MW;  C3B17777FE34B6BD CRC64;
     MLRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY
     EAVHDAGNDS GHGGESNLAL KRDDVTLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ
     QQEAKPDGLV TDSSAELQSL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD
     EERSLREAAE QKVTRLTEEL NKEATVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM
     TLERERESEK LKDECKKLQS QYASSEATIS QLRSELAKGP QEVAVYVQEL QKLKSSVNEL
     TQKNQTLTEN LLKKEQDYTK LEEKHNEESV SKKNIQATLH QKDLDCQQLQ SRLSASETSL
     HRIHVELSEK GEATQKLKEE LSEVETKYQH LKAEFKQLQQ QREEKEQHGL QLQSEINQLH
     SKLLETERQL GEAHGRLKEQ RQLSSEKLMD KEQQVADLQL KLSRLEEQLK EKVTNSTELQ
     HQLDKTKQQH QEQQALQQST TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKSKENIS
     LLEKEREDLY AKIQAGEGET AVLNQLQEKN HTLQEQVTQL TEKLKNQSES HKQAQENLHD
     QVQEQKAHLR AAQDRVLSLE TSVNELNSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKTA
     QRADLQNHLD TAQNALQDKQ QELNKITTQL DQVTAKLQDK QEHCSQLESH LKEYKEKYLS
     LEQKTEELEG QIKKLEADSL EVKASKEQAL QDLQQQRQLN TDLELRATEL SKQLEMEKEI
     VSSTRLDLQK KSEALESIKQ KLTKQEEEKQ ILKQDFETLS QETKIQHEEL NNRIQTTVTE
     LQKVKMEKEA LMTELSTVKD KLSKVSDSLK NSKSEFEKEN QKGKAAILDL EKTCKELKHQ
     LQVQMENTLK EQKELKKSLE KEKEASHQLK LELNSMQEQL IQAQNTLKQN EKEEQQLQGN
     INELKQSSEQ KKKQIEALQG ELKIAVLQKT ELENKLQQQL TQAAQELAAE KEKISVLQNN
     YEKSQETFKQ LQSDFYGRES ELLATRQDLK SVEEKLSLAQ EDLISNRNQI GNQNKLIQEL
     KTAKATLEQD SAKKEQQLQE RCKALQDIQK EKSLKEKELV NEKSKLAEIE EIKCRQEKEI
     TKLNEELKSH KLESIKEITN LKDAKQLLIQ QKLELQGKAD SLKAAVEQEK RNQQILKDQV
     KKEEEELKKE FIEKEAKLHS EIKEKEVGMK KHEENEAKLT MQITALNENL GTVKKEWQSS
     QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKVLELQRKL
     DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMA CGKGFSVTVR RHHCRQCGNI
     FCAECSAKNA LTPSSKKPVR VCDACFNDLQ G
//
ID   EEA1_MOUSE     STANDARD;      PRT;  1411 AA.
AC   Q8BL66; Q6DIC2;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   16-MAY-2006, entry version 26.
DE   Early endosome antigen 1.
GN   Name=Eea1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-946.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Binds phospholipid vesicles containing
CC       phosphatidylinositol 3-phosphate and participates in endosomal
CC       trafficking (By similarity).
CC   -!- SUBUNIT: Homodimer. Binds STX6. Binds RAB5A, RAB5B, RAB5C and
CC       RAB22A that have been activated by GTP-binding (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Endosome; early
CC       endosome; early endosomal membrane; peripheral membrane protein
CC       (By similarity).
CC   -!- SIMILARITY: Contains 1 C2H2-type zinc finger.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- CAUTION: Ref.2 sequence differs from that shown due to a stop
CC       codon in position 105 which was translated as Tyr to extend the
CC       sequence.
CC   -----------------------------------------------------------------------
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DR   EMBL; BC075637; AAH75637.1; -; mRNA.
DR   EMBL; AK046231; BAC32647.1; ALT_SEQ; mRNA.
DR   UniGene; Mm.210035; -.
DR   UniGene; Mm.408385; -.
DR   SMR; Q8BL66; 1289-1411.
DR   Ensembl; ENSMUSG00000036499; Mus musculus.
DR   MGI; MGI:2442192; Eea1.
DR   GO; GO:0005769; C:early endosome; IDA.
DR   InterPro; IPR002017; Spectrin.
DR   InterPro; IPR010989; t-snare.
DR   InterPro; IPR010978; tRNA_bd_arm.
DR   InterPro; IPR007087; Znf_C2H2.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   SMART; SM00064; FYVE; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
KW   Coiled coil; Metal-binding; Zinc; Zinc-finger.
FT   CHAIN         1   1411       Early endosome antigen 1.
FT                                /FTId=PRO_0000098707.
FT   ZN_FING      41     64       C2H2-type.
FT   ZN_FING    1352   1410       FYVE-type.
FT   COILED       78   1348       Potential.
FT   COMPBIAS    396    706       Gln/Glu/Lys-rich.
FT   CONFLICT    225    225       V -> I (in Ref. 2).
SQ   SEQUENCE   1411 AA;  160915 MW;  2365A51EF92019FD CRC64;
     MFRRILQRTP GRVGSQGSDL DSSATPINTV DVNNESSSEG FICPQCMKSL GSADELFKHY
     QAVHDAGNDS GHGGEAGLAL TRDDITLLRQ EVQDLQASLK EEKWYSEELK KELEKYQGLQ
     QQEAKSDGLV TDSSAELQAL EQQLEEAQTE NFNIKQMKDL FEQKAAQLAT EIADIKSKYD
     EEKSLRAAAE QKVTHLTEDL NKQTTVIQDL KTELLQRPGI EDVAVLKKEL VQVQTLMDNM
     TLERERESEK LKDECKKLQS EHAHLEATIN QLRSELAKGP QEVAVYVQEI QKLKGSINEL
     TQKNQNLTEK LQKKDLDYTH LEEKHNEESA SRKTLQASLH QRDLDCQQLQ ARLTASESSL
     QRAQGELSEK AEAAQKLREE LREVESTRQH LKVEVKQLQQ QREEKEQHGL QLQGEVSQLH
     CKLLETERQL GEAHGRLKEQ RQLSSEKLME KEQQVADLQL KLSRLEEQLK EKVTNSTELQ
     HQLEKSKQQH QEQQALQQSA TAKLREAQND LEQVLRQIGD KDQKIQNLEA LLQKGKESVS
     LLEKEREDLY AKIQAGEGET AVLNQLQEKN HALQQQLTQL TEKLKNQSES HKQAEENLHD
     QVQEQKAHLR AAQDRVLSLE TSVSELSSQL NESKEKVSQL DIQIKAKTEL LLSAEAAKAA
     QRADLQNHLD TAQHALQDKQ QELNKVSVQL DQLTAKFQEK QEHCIQLESH LKDHKEKHLS
     LEQKVEDLEG HIKKLEADAL EVKASKEQAL QSLQQQRQLS TDLELRNAEL SRELQEQEEV
     VSCTKLDLQN KSEILENIKQ TLTKKEEENV VLKQEFEKLS QDSKTQHKEL GDRMQAAVTE
     LTAVKAQKDA LLAELSTTKE KLSKVSDSLK NSKSEFEKEN QKGKAAVLDL EKACKELKHQ
     LQVQAESALK EQEDLKKSLE KEKETSQQLK IELNSVKGEV SQAQNTLKQK EKDEQQLQGT
     INQLKQSAEQ KKKQIEALQG EVKNAVSQKT VLENKLQQQS SQAAQELAAE KGKLSALQSN
     YEKCQADLKQ LQSDLYGKES ELLATRQDLK SVEEKLTLAQ EDLISNRNQI GNQNKSIQEL
     QAAKASLEQD SAKKEALLKE QSKALEDAQR EKSVKEKELV AEKSKLAEME EIKCRQEKEI
     TKLNEELKSH KQESIKEITN LKDAKQLLIQ QKLELQGRVD SLKAALEQEK ESQQLMREQV
     KKEEEKRKEE FSEKEAKLHS EIKEKEAGMK KHEENEAKLT MQVTTLNENL GTVKKEWQSS
     QRRVSELEKQ TDDLRGEIAV LEATVQNNQD ERRALLERCL KGEGEIEKLQ TKALELQRKL
     DNTTAAVQEL GRENQSLQIK HTQALNRKWA EDNEVQNCMS CGKCFSVTVR RHHCRQCGNI
     FCAECSTKNA LTPSSKKPVR VCDACFNDLQ G
//
ID   FAB1_SCHPO     STANDARD;      PRT;  1932 AA.
AC   O59722; O43072;
DT   16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2003, sequence version 2.
DT   30-MAY-2006, entry version 40.
DE   Phosphatidylinositol-4-phosphate 5-kinase fab1 (EC 2.7.1.68) (1-
DE   phosphatidylinositol-4-phosphate kinase) (PIP5K) (PtdIns(4)P-5-kinase)
DE   (Diphosphoinositide kinase).
GN   Name=fab1; Synonyms=ste12; ORFNames=SPBC3E7.01, SPBC6B1.11c;
OS   Schizosaccharomyces pombe (Fission yeast).
OC   Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes;
OC   Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=4896;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX   MEDLINE=21893055; PubMed=11895483;
RA   Morishita M., Morimoto F., Kitamura K., Koga T., Fukui Y., Maekawa H.,
RA   Yamashita I., Shimoda C.;
RT   "Phosphatidylinositol 3-phosphate 5-kinase is required for the
RT   cellular response to nutritional starvation and mating pheromone
RT   signals in Schizosaccharomyces pombe.";
RL   Genes Cells 7:199-215(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972;
RX   MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
CC   -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-4-
CC       phosphate on the fifth hydroxyl of the myo-inositol ring, to form
CC       phosphatidylinositol-4,5-biphosphate. Required for survival under
CC       conditions of nitrogen starvation. May have a role in the
CC       secretion of pheromone peptides.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 4-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. During cell fusion of opposite
CC       mating types, migrates to the isthmus.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 PI5K domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL023534; CAA19005.1; -; Genomic_DNA.
DR   EMBL; AL021838; CAA17054.1; -; Genomic_DNA.
DR   PIR; T40375; T40375.
DR   HSSP; Q960X8; 1DVP.
DR   GeneDB_Spombe; SPBC3E7.01; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-004849-MONOMER; -.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase...; IGI.
DR   GO; GO:0006897; P:endocytosis; TAS.
DR   InterPro; IPR002498; PIP5K.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Complete proteome; Kinase; Metal-binding; Transferase; Zinc;
KW   Zinc-finger.
FT   CHAIN         1   1932       Phosphatidylinositol-4-phosphate 5-kinase
FT                                fab1.
FT                                /FTId=PRO_0000185450.
FT   ZN_FING      60    119       FYVE-type.
SQ   SEQUENCE   1932 AA;  220135 MW;  B9826516D4504229 CRC64;
     MSEVETPTAA SPTFPVETSH RLDTLHTSST EQIIKDSENV VHTTLKLPTS TLSREFWMKD
     ERTNNCSLCE TEFTLFRRKH HCRICGKIIC KYCLKEAPGF IFRLQGSIKV CRPCASILVN
     NYSRSQLFNH SLNESKNRDL TEQHPFVTLD ELNSNDQVLS SFGDLSSTFE MPNNIHPPEV
     APMIAIPSSR SNYDSPGWAH HSIFLDWSKR NLDSNVINVE DSESGKYNAL TITNSYDAGP
     SSVSTDYRPV NFGKVPSYSK LRKNKAFSSA KVSDMYLSAD ERNRLEDFSK GDRGLSFVNL
     SPNIKATSYD RLSTVINEPF ISRSSSLTDE RGLADSGNSY HHFSDSDDES LFNDGLGLSF
     HANSAIIKQR QQNVASIQRY GNESYLSNFL KAFLPKTVCD YLFPSSTIPD GLPALIENFN
     ARVDKVNHPG GTEEPLPYQG KSRASSVVTS SKSTCILPPW ILFSDSFNQL VCTFLGKLLF
     QMLNDEGVDS PMQWVLCLPK ILLKMALDLG PDIRSGDDID VRSYVKIKKI PGGSIQDCFL
     VNGVLFSKKA SSKSMDRSLR RPRIALLTFS LDYACDEQRI LSLDLIISQQ EEYIINLVNR
     ICMLKPNLVF AQGQIPSIAL KYFEEHGVIA FHGLKESVLY DIARCCRADI ISSIDKLSLC
     PRLGTCGRFQ LRTYVVDENK GLRKTFAILD RCSERLGCTI VLRGADYNQL SKVKKIVELV
     VLIAYHIKLE CALLRDKFVN MPELFETTYQ SLSRKSLPSF ASTAADKEKS QNHEKKSLNS
     DNQSLRPLEN ENQSVSSTQG SNSPLELINN LPASDDYSSI TKALKTRFLT FSPFLSKPLP
     RLLNQVNYYQ FIRNKLLKDV KLHPYSPTGS FVMKQSENDN VEESYEESYK FFCIDERYHF
     LEKQWTLYYS HSKLMFSPFS SQRIILLYSI INKETSVPCI GPERCLLEFY RETDCTLGQY
     IEDSCLNTNV SCGGEYCKTN DMLWHYRSYV HGNSRISVFL ESFSCPVPGL EEKIIMWSYC
     KFCKKNTHIT VMSEETWKYS FGKYLEFMFY NSQIRDRFEF CDHSVMAQHV HYFGYCNMAL
     RFQRDLIEIF ELFVPSVTLR NNPSYIKELK EKEYKRLKGV IEKCLSSVAS RINQIKCDWV
     TDPEKFESCT SEISKFRTLL SSDYTELYSE FDSIYLNSST SDYLSLNSIL RVLQGKMVKW
     EQRFLDYQRL YLPSYKELSK IAAAQIKKVF LERPLSQTPL DLPETLENTQ IDIYPSFKTE
     STDDQLEKVT QTNVASNKRV APYADSMANV GSPESDCFSV ATSSDIPKAN IDFTNDISTQ
     NTFPASPVSN SGFSRQTYPN ISQRQGVNML SHKRKSASTS DRRFVNASST SGMNMPISSS
     ISAKISSIQN STKYSPRKPI PAKDVRVSSL VRRFEELSLQ LQEKQKRDEE LIKARRKRAL
     PVVPSKPVVE VFNDLNEAFD DENSEDENGI NDTKENRATE SNFSGVDSMS KERENVSSNE
     DNSPEAFEDI FGILFKNESG LEEQQNLEPS SQMDKEGSKL PTSGPLADKT SVYRILSAFW
     NEWNSLNPPP FEFPLQPTEH MFSDSNVIIR EDEPSSLISF TLSSPDYLSK MVEIEDSMDE
     ALTNQGLQGS TQFKIENLML KPTGTHLKYQ FEEGSARLSC KVFFAEQFSA LRRACGCEET
     FVTSLARCSL WESSGGKSGS AFLKTFDKKY ILKVLSRLES DSLLNFAPAY FDYISKVFFH
     ELPTALTKIF GFYRVDIRNP TTGTICKTDI MIMENVFYDE CPSRIFDLKG SMRNRHVEST
     GKVDEVLLDE NLVELIYESP IFVSEQLKSL LHSCLWNDTL FLSKLNIMDY SLIVGIDYTK
     KELYVGIIDF IRTYTWDKKL ESWVKEKGLV GRGPEPTIVT PKQYKNRFRK AMDCYILASQ
     DFETGEGFKF CE
//
ID   FAB1_YEAST     STANDARD;      PRT;  2278 AA.
AC   P34756;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   30-MAY-2006, entry version 57.
DE   1-phosphatidylinositol-3-phosphate 5-kinase FAB1 (EC 2.7.1.150)
DE   (Phosphatidylinositol-3-phosphate 5-kinase) (Type III PIP kinase).
GN   Name=FAB1; OrderedLocusNames=YFR019W;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=95392039; PubMed=7663021;
RA   Yamamoto A., Dewald D.B., Boronenkov I.V., Anderson R.A., Emr S.D.,
RA   Koshland D.;
RT   "Novel PI(4)P 5-kinase homologue, Fab1p, essential for normal vacuole
RT   function and morphology in yeast.";
RL   Mol. Biol. Cell 6:525-539(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S288c / AB972;
RX   MEDLINE=95400292; PubMed=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M.,
RA   Sasanuma S., Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K.,
RA   Yamazaki M., Tashiro H., Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from
RT   Saccharomyces cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   MEDLINE=99035548; PubMed=9811604; DOI=10.1016/S0960-9822(07)00513-1;
RA   Cooke F.T., Dove S.K., McEwen R.K., Painter G., Holmes A.B.,
RA   Hall M.N., Michell R.H., Parker P.J.;
RT   "The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p
RT   is essential for vacuole function in S. cerevisiae.";
RL   Curr. Biol. 8:1219-1222(1998).
RN   [4]
RP   ENZYME REGULATION, AND SUBCELLULAR LOCATION.
RX   PubMed=11889142; DOI=10.1083/jcb.200201002;
RA   Bonangelino C.J., Nau J.J., Duex J.E., Brinkman M., Wurmser A.E.,
RA   Gary J.D., Emr S.D., Weisman L.S.;
RT   "Osmotic stress-induced increase of phosphatidylinositol 3,5-
RT   bisphosphate requires Vac14p, an activator of the lipid kinase
RT   Fab1p.";
RL   J. Cell Biol. 156:1015-1028(2002).
RN   [5]
RP   ENZYME REGULATION.
RX   PubMed=11950935; DOI=10.1091/mbc.01-10-0498;
RA   Gary J.D., Sato T.K., Stefan C.J., Bonangelino C.J., Weisman L.S.,
RA   Emr S.D.;
RT   "Regulation of Fab1 phosphatidylinositol 3-phosphate 5-kinase pathway
RT   by Vac7 protein and Fig4, a polyphosphoinositide phosphatase family
RT   member.";
RL   Mol. Biol. Cell 13:1238-1251(2002).
RN   [6]
RP   SUBCELLULAR LOCATION.
RX   MEDLINE=22923954; PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION.
RX   MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA   Dephoure N., O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
CC   -!- FUNCTION: Catalyzes the phosphorylation of phosphatidylinositol-3-
CC       phosphate on the fifth hydroxyl of the myo-inositol ring, to form
CC       phosphatidylinositol-3,5-bisphosphate. Required for endocytic-
CC       vacuolar pathway and nuclear migration. The product of the
CC       reaction it catalyzes functions as an important regulator of
CC       vacuole homeostasis perhaps by controlling membrane flux to and/or
CC       from the vacuole.
CC   -!- CATALYTIC ACTIVITY: ATP + 1-phosphatidyl-1D-myo-inositol 3-
CC       phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate.
CC   -!- COFACTOR: Magnesium or manganese.
CC   -!- ENZYME REGULATION: Activated by VAC14 and VAC7. VAC14 acts as a
CC       specific osmotic response regulator.
CC   -!- SUBCELLULAR LOCATION: Vacuole; vacuolar membrane; peripheral
CC       membrane protein. Endosome; endosomal membrane; peripheral
CC       membrane protein.
CC   -!- MISCELLANEOUS: Present with 149 molecules/cell.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 1 PI5K domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U01017; AAA81360.1; -; Genomic_DNA.
DR   EMBL; D50617; BAA09258.1; -; Genomic_DNA.
DR   PIR; S56274; S56274.
DR   HSSP; P40343; 1VFY.
DR   GermOnline; 140173; -.
DR   Ensembl; YFR019W; Saccharomyces cerevisiae.
DR   GenomeReviews; D50617_GR; YFR019W.
DR   SGD; S000001915; FAB1.
DR   LinkHub; P34756; -.
DR   GO; GO:0005739; C:mitochondrion; IDA.
DR   GO; GO:0005774; C:vacuolar membrane; TAS.
DR   GO; GO:0000285; F:1-phosphatidylinositol-3-phosphate 5-kinase...; IDA.
DR   GO; GO:0006644; P:phospholipid metabolism; IGI.
DR   GO; GO:0006950; P:response to stress; TAS.
DR   GO; GO:0007033; P:vacuole organization and biogenesis; IMP.
DR   InterPro; IPR002498; PIP5K.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   PANTHER; PTHR11353; Cpn60/TCP-1; 1.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF01504; PIP5K; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00330; PIPKc; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Complete proteome; Kinase; Membrane; Metal-binding; Transferase;
KW   Vacuole; Zinc; Zinc-finger.
FT   CHAIN         1   2278       1-phosphatidylinositol-3-phosphate 5-
FT                                kinase FAB1.
FT                                /FTId=PRO_0000185451.
FT   ZN_FING     240    299       FYVE-type.
FT   COMPBIAS    393    397       Poly-Pro.
FT   COMPBIAS    571    590       Poly-Asn.
FT   COMPBIAS   1808   1811       Poly-Thr.
FT   COMPBIAS   1891   1897       Poly-Gln.
FT   CONFLICT   2275   2275       R -> W (in Ref. 2).
SQ   SEQUENCE   2278 AA;  257420 MW;  1A0A30E13165DE41 CRC64;
     MSSEEPHASI SFPDGSHVRS SSTGTSSVNT IDATLSRPNY IKKPSLHIMS TSTTSTTTDL
     VTNPILSNIS VPKISPPTSS SIATATSTSH VTGTASHSNI KANANTSTSV NKKNLPPTTS
     GRIPSSTIKR YPSRYKPSHS LQLPIKNDSN FKRSSIYASK STVTAIPIRN NRPISMQNSY
     ARTPDSDHDD VGDEVSSIKS ASSSLTASLS KSFLFAFYNN RKKDKTSNNG VLSKEYWMKD
     ESSKECFSCG KTFNTFRRKH HCRICGQIFC SSCTLLIDGD RFGCHAKMRV CYNCYEHADT
     YEDSSDEEND STMQLNEPRS RSRSRSSNTN PYSHSHSHLH LISQDNHNGT DLHDPVAATD
     NPQQQNEVYL LNDDDVQSIM TSGEDSKLFI STPPPPPKMA IPATKQGGSL EISFDSENDR
     ALHYQDDNPG RHHHLDSVPT RYTIRDMDNI SHYDTNSNST LRPHYNTNNS TITINNLNNT
     TSNNSNYNNT NSNSNINNPA HSLRRSIFHY VSSNSVNKDS NNSSATPASS AQSSSILDPA
     NRIIGNYAHR NYKFKFNYNS KGPSQQNDTA NGNNDNNNNN NNNNNNNNNN SASGIADNNN
     IPSNDNGTTF TLDKKKRNPL TKSKSTSAYL EYPLNEEDSS EDEGSMSIYS VLNDDHKTDN
     PIRSMRNSTK SFQRAQASLQ RMRFRRKSKS KHFPNNSKSS IYRDLNFLTN STPNLLSVVS
     DDNLYDDSSP LQDKASSSAA SRLTDRKFSN SSGSNNNSNS NSNINTDPWK RIASISGFKL
     KKEKKRELNE VSLLHMHALL KQLLNDQEIS NLQEWITLLD GALRKVLRTI LNARDLNTLD
     FRQTYVKIKR ISGGSPQNSE YIDGVVFSKA LPSKTMPRHL KNPRILLIMF PLEYQKNNNH
     FLSIESVFRQ EREYLDKLVS RLKSLHPDII YVGANVSGYA LELLNDSGIV VQFNMKPQVI
     ERIAKLTEAD IAISVDKLAT NIKMGECETF EVKSYIYGNI SKTYTFLRGC NPELGGTILL
     RGDSLENLRK IKQVSEFMVY AIFSLKLESS FFNDNFIQLS TDVYLKRAES KKLQVFEGYF
     ADFLIKFNNR ILTVSPTVDF PIPFLLEKAR GLEKKLIERI NQYESESDLD RQTQLNMLQG
     LESTITKKHL GNLIKFLHEM EIENLELEFQ KRSRQWEVSY SSSQNLLGTG SHQSITVLYS
     MVSTKTATPC VGPQIVTIDY FWDSDISIGQ FIENVVGTAR YPCQQGCNGL YLDHYRSYVH
     GSGKVDVLIE KFQTRLPKLK DIILTWSYCK KCGTSTPILQ ISEKTWNHSF GKYLEVMFWS
     YKDSVTGIGK CPHDFTKDHV KYFGYNDLVV RLEYSDLEVH ELITPPRKIK WKPHIDIKLK
     VELYYKILEK INNFYGSVLS RLERIKLDSM TKDKVLSGQA KIIELKSNAT EEQKLMLQDL
     DTFYADSPCD QHLPLNLVIK SLYDKAVNWN STFAIFAKSY LPSETDISRI TAKQLKKLFY
     DSSRKDSEDK KSLHDEKAKT RKPEKNELPL EGLKDVEKPK IDSKNTTENR DRTNEPQNAV
     TITTFKDDTP IIPTSGTSHL TVTPSASSVS SSLTPQTEER PPISRSGTGI SMTHDKSTRP
     NIRKMSSDSS LCGLASLANE YSKNNKVSKL ATFFDQMHFD ALSKEFELER ERERLQLNKD
     KYQAIRLQTS TPIVEIYKNV KDAVDEPLHS RSSGNNLSSA NVKTLEAPVG EHSRANNCNP
     PNLDQNLETE LENSISQWGE NILNPSGKTT ASTHLNSKPV VKETSENPKS IVRESDNSKS
     EPLPPVITTT TVNKVESTPQ PEKSLLMKTL SNFWADRSAY LWKPLVYPTC PSEHIFTDSD
     VIIREDEPSS LIAFCLSTSD YRNKMMNLNV QQQQQQQTAE AAPAKTGGNS GGTTQTGDPS
     VNISPSVSTT SHNKGRDSEI SSLVTTKEGL LNTPPIEGAR DRTPQESQTH SQANLDTLQE
     LEKIMTKKTA THLRYQFEEG LTVMSCKIFF TEHFDVFRKI CDCQENFIQS LSRCVKWDSN
     GGKSGSGFLK TLDDRFIIKE LSHAELEAFI KFAPSYFEYM AQAMFHDLPT TLAKVFGFYQ
     IQVKSSISSS KSYKMDVIIM ENLFYEKKTT RIFDLKGSMR NRHVEQTGKA NEVLLDENMV
     EYIYESPIHV REYDKKLLRA SVWNDTLFLA KMNVMDYSLV IGIDNEGYTL TVGIIDFIRT
     FTWDKKLESW VKEKGLVGGA SVIKQPTVVT PRQYKKRFRE AMERYILMVP DPWYREGN
//
ID   FGD1_HUMAN     STANDARD;      PRT;   961 AA.
AC   P98174; Q8N4D9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2003, sequence version 2.
DT   30-MAY-2006, entry version 56.
DE   FYVE, RhoGEF and PH domain-containing protein 1 (Faciogenital
DE   dysplasia 1 protein) (Zinc finger FYVE domain-containing protein 3)
DE   (Rho/Rac guanine nucleotide exchange factor FGD1) (Rho/Rac GEF).
GN   Name=FGD1; Synonyms=ZFYVE3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Craniofacial;
RX   MEDLINE=95042764; PubMed=7954831; DOI=10.1016/0092-8674(94)90552-5;
RA   Pasteris N.G., Cadle A., Logie L.J., Porteous M.E.M., Schwartz C.E.,
RA   Stevenson R.E., Glover T.W., Wilroy R.S., Gorski J.L.;
RT   "Isolation and characterization of the faciogenital dysplasia
RT   (Aarskog-Scott syndrome) gene: a putative Rho/Rac guanine nucleotide
RT   exchange factor.";
RL   Cell 79:669-678(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN   [3]
RP   FUNCTION.
RX   PubMed=8969170; DOI=10.1074/jbc.271.52.33169;
RA   Zheng Y., Fischer D.J., Santos M.F., Tigyi G., Pasteris N.G.,
RA   Gorski J.L., Xu Y.;
RT   "The faciogenital dysplasia gene product FGD1 functions as a Cdc42Hs-
RT   specific guanine-nucleotide exchange factor.";
RL   J. Biol. Chem. 271:33169-33172(1996).
RN   [4]
RP   VARIANT AAS HIS-522.
RX   MEDLINE=20546218; PubMed=11093277; DOI=10.1038/sj.ejhg.5200553;
RA   Schwartz C.E., Gillessen-Kaesbach G., May M., Cappa M., Gorski J.L.,
RA   Steindl K., Neri G.;
RT   "Two novel mutations confirm FGD1 is responsible for the Aarskog
RT   syndrome.";
RL   Eur. J. Hum. Genet. 8:869-874(2000).
RN   [5]
RP   VARIANT AAS GLN-610.
RX   MEDLINE=20389563; PubMed=10930571; DOI=10.1016/S0014-5793(00)01857-3;
RA   Orrico A., Galli L., Falciani M., Bracci M., Cavaliere M.L.,
RA   Rinaldi M.M., Musacchio A., Sorrentino V.;
RT   "A mutation in the pleckstrin homology (PH) domain of the FGD1 gene in
RT   an Italian family with faciogenital dysplasia (Aarskog-Scott
RT   syndrome).";
RL   FEBS Lett. 478:216-220(2000).
RN   [6]
RP   VARIANT NONSYNDROMAL X-LINKED MENTAL RETARDATION LEU-312.
RX   PubMed=11940089;
RA   Lebel R.R., May M., Pouls S., Lubs H.A., Stevenson R.E.,
RA   Schwartz C.E.;
RT   "Non-syndromic X-linked mental retardation associated with a missense
RT   mutation (P312L) in the FGD1 gene.";
RL   Clin. Genet. 61:139-145(2002).
RN   [7]
RP   VARIANTS AAS ILE-205; ALA-380 AND HIS-443.
RX   PubMed=14560308; DOI=10.1038/sj.ejhg.5201081;
RA   Orrico A., Galli L., Cavaliere M.L., Garavelli L., Fryns J.-P.,
RA   Crushell E., Rinaldi M.M., Medeira A., Sorrentino V.;
RT   "Phenotypic and molecular characterisation of the Aarskog-Scott
RT   syndrome: a survey of the clinical variability in light of FGD1
RT   mutation analysis in 46 patients.";
RL   Eur. J. Hum. Genet. 12:16-23(2004).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho-
CC       and Rac proteins, by exchanging bound GDP for free GTP. Plays a
CC       role in regulating the actin cytoskeleton and cell shape.
CC   -!- SUBUNIT: Interacts with DBNL/ABP1 and CTTN (By similarity). Binds
CC       CDC42.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Associated with
CC       membrane ruffles and lamellipodia (By similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in fetal heart, brain, lung, kidney
CC       and placenta. Less expressed in liver; adult heart, brain, lung,
CC       pancreas and skeletal muscle.
CC   -!- DISEASE: Defects in FGD1 are the cause of Aarskog-Scott syndrome
CC       (AAS) [MIM:305400]. This faciogenital dysplasia is a rare
CC       multisystemic disorder characterized by disproportionately short
CC       stature, and by facial, skeletal, and urogenital anomalies.
CC   -!- DISEASE: Defects in FGD1 are a cause of nonsyndromal X-linked
CC       mental retardation.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- WEB RESOURCE: NAME=GeneReviews;
CC       URL="http://www.genetests.org/query?gene=FGD1".
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; U11690; AAA57004.1; -; mRNA.
DR   EMBL; BC034530; AAH34530.1; -; mRNA.
DR   UniGene; Hs.584507; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSG00000102302; Homo sapiens.
DR   HGNC; HGNC:3663; FGD1.
DR   MIM; 305400; gene+phenotype.
DR   GO; GO:0005794; C:Golgi apparatus; ISS.
DR   GO; GO:0030027; C:lamellipodium; ISS.
DR   GO; GO:0001726; C:ruffle; ISS.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA.
DR   GO; GO:0005515; F:protein binding; ISS.
DR   GO; GO:0031267; F:small GTPase binding; IDA.
DR   GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; IDA.
DR   GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0007275; P:development; TAS.
DR   GO; GO:0046847; P:filopodium formation; IDA.
DR   GO; GO:0009887; P:organ morphogenesis; TAS.
DR   GO; GO:0043088; P:regulation of Cdc42 GTPase activity; IDA.
DR   GO; GO:0008360; P:regulation of cell shape; ISS.
DR   GO; GO:0007165; P:signal transduction; TAS.
DR   InterPro; IPR001331; GDS_CDC24.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Cytoskeleton; Disease mutation; Guanine-nucleotide releasing factor;
KW   Metal-binding; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    961       FYVE, RhoGEF and PH domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000080940.
FT   DOMAIN      373    561       DH.
FT   DOMAIN      590    689       PH 1.
FT   DOMAIN      821    921       PH 2.
FT   ZN_FING     730    790       FYVE-type.
FT   MOTIF       171    179       SH3-binding (Potential).
FT   MOTIF       179    187       SH3-binding (Potential).
FT   COMPBIAS      7    330       Pro-rich.
FT   VARIANT     205    205       S -> I (in AAS).
FT                                /FTId=VAR_019268.
FT   VARIANT     312    312       P -> L (in nonsyndromal X-linked mental
FT                                retardation).
FT                                /FTId=VAR_019269.
FT   VARIANT     380    380       E -> A (in AAS).
FT                                /FTId=VAR_019270.
FT   VARIANT     443    443       R -> H (in AAS).
FT                                /FTId=VAR_019271.
FT   VARIANT     522    522       R -> H (in AAS).
FT                                /FTId=VAR_015236.
FT   VARIANT     610    610       R -> Q (in AAS).
FT                                /FTId=VAR_015237.
FT   CONFLICT     10     23       AGPSEPEHPATNPP -> RRAFGARTPGHEPA (in Ref.
FT                                1).
FT   CONFLICT    195    195       A -> G (in Ref. 1).
SQ   SEQUENCE   961 AA;  106561 MW;  30963F7B9931E45C CRC64;
     MHGHRAPGGA GPSEPEHPAT NPPGAAPPAC ADSDPGASEP GLLARRGSGS ALGGPLDPQF
     VGPSDTSLGA APGHRVLPCG PSPQHHRALR FSYHLEGSQP RPGLHQGNRI LVKSLSLDPG
     QSLEPHPEGP QRLRSDPGPP TETPSQRPSP LKRAPGPKPQ VPPKPSYLQM PRMPPPLEPI
     PPPPSRPLPA DPRVAKGLAP RAEASPSSAA VSSLIEKFER EPVIVASDRP VPGPSPGPPE
     PVMLPQPTSQ PPVPQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
     SDDGPPSHSL CPGPPALASV PVALADPHRP GSQEVDSDLE EEDDEEEEEE KDREIPVPLM
     ERQESVELTV QQKVFHIANE LLQTEKAYVS RLHLLDQVFC ARLLEEARNR SSFPADVVHG
     IFSNICSIYC FHQQFLLPEL EKRMEEWDRY PRIGDILQKL APFLKMYGEY VKNFDRAVEL
     VNTWTERSTQ FKVIIHEVQK EEACGNLTLQ HHMLEPVQRI PRYELLLKDY LLKLPHGSPD
     SKDAQKSLEL IATAAEHSNA AIRKMERMHK LLKVYELLGG EEDIVSPTKE LIKEGHILKL
     SAKNGTTQDR YLILFNDRLL YCVPRLRLLG QKFSVRARID VDGMELKESS NLNLPRTFLV
     SGKQRSLELQ ARTEEEKKDW VQAINSTLLK HEQTLETFKL LNSTNREDED TPPNSPNVDL
     GKRAPTPIRE KEVTMCMRCQ EPFNSITKRR HHCKACGHVV CGKCSEFRAR LVYDNNRSNR
     VCTDCYVALH GVPGSSPACS QHTPQRRRSI LEKQASVAAE NSVICSFLHY MEKGGKGWHK
     AWFVVPENEP LVLYIYGAPQ DVKAQRSLPL IGFEVGPPEA GERPDRRHVF KITQSHLSWY
     FSPETEELQR RWMAVLGRAG RGDTFCPGPT LSEDREMEEA PVAALGATAE PPESPQTRDK
     T
//
ID   FGD1_MOUSE     STANDARD;      PRT;   960 AA.
AC   P52734;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-MAY-2006, entry version 43.
DE   FYVE, RhoGEF and PH domain-containing protein 1 (Faciogenital
DE   dysplasia 1 protein homolog) (Zinc finger FYVE domain-containing
DE   protein 3) (Rho/Rac guanine nucleotide exchange factor FGD1) (Rho/Rac
DE   GEF).
GN   Name=Fgd1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96081343; PubMed=8535076;
RA   Pasteris N.G., de Gouyon B., Cadle A.B., Campbell K., Herman G.E.,
RA   Gorski J.L.;
RT   "Cloning and regional localization of the mouse faciogenital dysplasia
RT   (Fgd1) gene.";
RL   Mamm. Genome 6:658-661(1995).
RN   [2]
RP   FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DBNL AND CTTN, AND
RP   MUTAGENESIS OF PRO-159; PRO-162 AND LYS-164.
RX   PubMed=12913069; DOI=10.1093/hmg/ddg209;
RA   Hou P., Estrada L., Kinley A.W., Parsons J.T., Vojtek A.B.,
RA   Gorski J.L.;
RT   "Fgd1, the Cdc42 GEF responsible for faciogenital dysplasia, directly
RT   interacts with cortactin and mAbp1 to modulate cell shape.";
RL   Hum. Mol. Genet. 12:1981-1993(2003).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho-
CC       and Rac proteins, by exchanging bound GDP for free GTP. Plays a
CC       role in regulating the actin cytoskeleton and cell shape.
CC   -!- SUBUNIT: Interacts with DBNL/ABP1 and CTTN. Binds CDC42 (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Associated with membrane ruffles
CC       and lamellipodia.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; U22325; AAA96001.1; -; mRNA.
DR   UniGene; Mm.219461; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSMUSG00000025265; Mus musculus.
DR   MGI; MGI:104566; Fgd1.
DR   GO; GO:0005794; C:Golgi apparatus; IDA.
DR   GO; GO:0030027; C:lamellipodium; IDA.
DR   GO; GO:0001726; C:ruffle; IDA.
DR   GO; GO:0005515; F:protein binding; IPI.
DR   GO; GO:0007010; P:cytoskeleton organization and biogenesis; IDA.
DR   GO; GO:0008360; P:regulation of cell shape; IDA.
DR   InterPro; IPR001331; GDS_CDC24.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS00741; DH_1; FALSE_NEG.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Cytoskeleton; Guanine-nucleotide releasing factor; Metal-binding;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    960       FYVE, RhoGEF and PH domain-containing
FT                                protein 1.
FT                                /FTId=PRO_0000080941.
FT   DOMAIN      372    560       DH.
FT   DOMAIN      589    688       PH 1.
FT   DOMAIN      820    920       PH 2.
FT   ZN_FING     729    789       FYVE-type.
FT   MOTIF       171    179       SH3-binding (Potential).
FT   MOTIF       179    187       SH3-binding (Potential).
FT   COMPBIAS      7    330       Pro-rich.
FT   MUTAGEN     159    159       P->A: Abolishes binding to DBNL.
FT   MUTAGEN     162    162       P->A: Abolishes binding to DBNL.
FT   MUTAGEN     164    164       K->E: No effect on binding to DBNL.
SQ   SEQUENCE   960 AA;  106478 MW;  41C1B84DE490FC51 CRC64;
     MHGHRVPGGP GPSDPERSAA NTPGAAPLAC ADSDPGALEP GLPVSRGSGT ALGGPLDPQF
     VGPSDASLGA PPSSRVLPCG PSPQHHRALR FSYHLEGSQP RPGLHQGNRI LVKSLSLDPG
     QSLEPHPEGP QRLRSDPGPP TEIPGPRPSP LKRAPGPKPQ VPPKPSYLQM PRVLPPPEPI
     PPPPSRPLPA DPRVAKGLVP RAEASTSSAA VSSLIEKFER EPVIVASDRP APGPCPVPPE
     PAMLPQPPPQ PTGSQLPEGE ASRCLFLLAP GPRDGEKVPN RDSGIDSISS PSNSEETCFV
     SDDGPPIHSL CPGPPALASM PVALADPHRP GSQEVDSDLE EEEEEEEEEK EREIPVPPME
     RQESVELTVQ QKVFHIANEL LQTEKAYVSR LHLLDQVFCA RLLEEARNRS SFPADVVHGI
     FSNICSIYCF HQQFLLPELE KRMEEWDRYP RIGDILQKLA PFLKMYGEYV KNFDRAVELV
     NTWTERSTQF KVIIHEVQKE EACRNLTLQH HMLEPVQRIP RYELLLKDYL LKLPHGSPDS
     KDAQKSLELI ATAAEHSNAA IRKMERMHKL LKVYELLGGE EDIVSPTKEL IKEGHILKLS
     AKNGTTQDRY LILFNDRLLY CVPRLRLLGQ KFTVRARIDV DGMELKESSN LNMPRTFLVS
     GKQRSLELQA RTEEEKKDWV QAINSTLLKH EQTLETFKLL NSTNRDDEDT PPNSPNVDLG
     KRAPTPIREK EVTMCMRCQE PFNSITKRRH HCKACGHVVC GKCSEFRARL IYDNNRSNRV
     CTDCYVALHG APGSSPACSQ HTPQRRRSIL EKQASVAAEN SVICSFLHYM EKGGKGWHKA
     WFVVPENEPL VLYIYGAPQD VKAQRSLPLI GFEVGPPEAG ERPDRRHVFK ITQSHLSWYF
     SPETEELQRR WMAVLGRAGR GDTFCPGPTL SEDKEMEETP VAASGATAEP PEASQTRDKT
//
ID   FGD2_HUMAN     STANDARD;      PRT;   655 AA.
AC   Q7Z6J4; Q5T8I1; Q6P6A8; Q6ZNL5; Q8IZ32; Q8N868; Q9H7M2;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   30-MAY-2006, entry version 21.
DE   FYVE, RhoGEF and PH domain-containing protein 2 (Zinc finger FYVE
DE   domain-containing protein 4).
GN   Name=FGD2; Synonyms=ZFYVE4;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
RX   MEDLINE=21082933; PubMed=11214971; DOI=10.1093/dnares/7.6.357;
RA   Hattori A., Okumura K., Nagase T., Kikuno R., Hirosawa M., Ohara O.;
RT   "Characterization of long cDNA clones from human adult spleen.";
RL   DNA Res. 7:357-366(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC   TISSUE=Spleen;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22935763; PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP   HIS-32.
RC   TISSUE=Blood, Lymph, and Spleen;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: May activate CDC42, a member of the Ras-like family of
CC       Rho- and Rac proteins, by exchanging bound GDP for free GTP. May
CC       play a role in regulating the actin cytoskeleton and cell shape
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q7Z6J4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7Z6J4-2; Sequence=VSP_013065, VSP_013070, VSP_013072;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q7Z6J4-3; Sequence=VSP_013068, VSP_013069;
CC         Note=No experimental confirmation available;
CC       Name=4;
CC         IsoId=Q7Z6J4-4; Sequence=VSP_013066, VSP_013071;
CC         Note=No experimental confirmation available;
CC       Name=5;
CC         IsoId=Q7Z6J4-5; Sequence=VSP_013067, VSP_013068;
CC         Note=May be due to an intron retention. No experimental
CC         confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- CAUTION: Ref.3 sequence differs from that shown due to erroneous
CC       gene model prediction.
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AK024456; BAB15746.1; ALT_INIT; mRNA.
DR   EMBL; AK097230; BAC04982.1; -; mRNA.
DR   EMBL; AK131079; BAC85129.1; ALT_INIT; mRNA.
DR   EMBL; AL160264; CAI20471.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC023645; AAH23645.1; -; mRNA.
DR   EMBL; BC053655; AAH53655.1; -; mRNA.
DR   EMBL; BC062363; AAH62363.1; -; mRNA.
DR   UniGene; Hs.509664; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSG00000146192; Homo sapiens.
DR   HGNC; HGNC:3664; FGD2.
DR   MIM; 605091; gene.
DR   GO; GO:0005794; C:Golgi apparatus; ISS.
DR   GO; GO:0030027; C:lamellipodium; ISS.
DR   GO; GO:0001726; C:ruffle; ISS.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS.
DR   GO; GO:0005515; F:protein binding; ISS.
DR   GO; GO:0031267; F:small GTPase binding; ISS.
DR   GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0046847; P:filopodium formation; ISS.
DR   GO; GO:0043088; P:regulation of Cdc42 GTPase activity; ISS.
DR   GO; GO:0008360; P:regulation of cell shape; ISS.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Polymorphism;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    655       FYVE, RhoGEF and PH domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000080942.
FT   DOMAIN      102    290       DH.
FT   DOMAIN      319    418       PH 1.
FT   DOMAIN      544    641       PH 2.
FT   ZN_FING     458    518       FYVE-type.
FT   VAR_SEQ       1    423       Missing (in isoform 2).
FT                                /FTId=VSP_013065.
FT   VAR_SEQ       1    372       Missing (in isoform 4).
FT                                /FTId=VSP_013066.
FT   VAR_SEQ       1     22       MKGASEEKLASVSNLVTVFENS -> MFPKKARHPGAPALG
FT                                ICTRQPKSTPGTCCCFPCSPGRKPSGLSLLL (in
FT                                isoform 5).
FT                                /FTId=VSP_013067.
FT   VAR_SEQ     101    104       EPEK -> VPEG (in isoform 3 and isoform
FT                                5).
FT                                /FTId=VSP_013068.
FT   VAR_SEQ     105    655       Missing (in isoform 3).
FT                                /FTId=VSP_013069.
FT   VAR_SEQ     424    442       NETFKAAAQGPEGDIQEQE -> MGGRRSPRAHSCPTPLNP
FT                                Q (in isoform 2).
FT                                /FTId=VSP_013070.
FT   VAR_SEQ     460    655       MVTMCMRCQEPFNALTRRRHHCRACGYVVCARCSDYRAELK
FT                                YDDNRPNRVCLHCYAFLTGNVLPEAKEDKRRGILEKGSSAT
FT                                PDQSLMCSFLQLIGDKWGKSGPRGWCVIPRDDPLVLYVYAA
FT                                PQDMRAHTSIPLLGYQVTVGPQGDPRVFQLQQSGQLYTFKA
FT                                ETEELKGRWVKAMERAASGWSPSWPNDGDLSD -> HGDHV
FT                                HALPGALQRSDAPSPPLPGLRLCEYSCQHSCLHLRHPGLHL
FT                                HHPGLHLSYLGLRLIHLGLHLPHLGLHLCHLHLSLRGLHLC
FT                                HPGLYLSYLGFHLIHLGFHLIHLGLHLPHLGLYLSHLGLHL
FT                                PHLGFHQCHPGLYLSHLGLYLPYLGLYPPSSGAAVPILAKS
FT                                AGFNQCSPVVLGTSSEPGVCITTSSGPHSTPQEAAVSHFLD
FT                                GKMRPIEVKLLAEGTPEADPMNLPAFLSSFSTTLRPRARKW
FT                                SPVLVEGHLAPHPLRPCPTTSPGPCPLCTHPPRHPLFTRFG
FT                                (in isoform 4).
FT                                /FTId=VSP_013071.
FT   VAR_SEQ     585    655       DMRAHTSIPLLGYQVTVGPQGDPRVFQLQQSGQLYTFKAET
FT                                EELKGRWVKAMERAASGWSPSWPNDGDLSD -> VRPPPAR
FT                                PPSGPGLPTACV (in isoform 2).
FT                                /FTId=VSP_013072.
FT   VARIANT      32     32       Q -> H (in dbSNP:831510).
FT                                /FTId=VAR_021491.
SQ   SEQUENCE   655 AA;  74892 MW;  DB60098249C2B340 CRC64;
     MKGASEEKLA SVSNLVTVFE NSRTPEAAPR GQRLEDVHHR PECRPPESPG PREKTNVGEA
     VGSEPRTVSR RYLNSLKNKL SSEAWRKSCQ PVTLSGSGTQ EPEKKIVQEL LETEQAYVAR
     LHLLDQVFFQ ELLKTARSSK AFPEDVVRVI FSNISSIYQF HSQFFLPELQ RRLDDWTANP
     RIGDVIQKLA PFLKMYSEYV KNFERAAELL ATWTDKSPLF QEVLTRIQSS EASGSLTLQH
     HMLEPVQRIP RYELLLKEYI QKLPAQAPDQ ADAQKALDMI FSAAQHSNAA ITEMERLQDL
     WEVYQRLGLE DDIVDPSNTL LREGPVLKIS FRRNDPMERY LFLFNNMLLY CVPRVIQVGA
     QFQVRTRIDV AGMKVRELMD AEFPHSFLVS GKQRTLELQA RSQEEMISWM QAFQAAIDQI
     EKRNETFKAA AQGPEGDIQE QELQSEELGL RAPQWVRDKM VTMCMRCQEP FNALTRRRHH
     CRACGYVVCA RCSDYRAELK YDDNRPNRVC LHCYAFLTGN VLPEAKEDKR RGILEKGSSA
     TPDQSLMCSF LQLIGDKWGK SGPRGWCVIP RDDPLVLYVY AAPQDMRAHT SIPLLGYQVT
     VGPQGDPRVF QLQQSGQLYT FKAETEELKG RWVKAMERAA SGWSPSWPND GDLSD
//
ID   FGD2_MOUSE     STANDARD;      PRT;   655 AA.
AC   Q8BY35; O88841; Q7TSE3; Q8VDH4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   30-MAY-2006, entry version 26.
DE   FYVE, RhoGEF and PH domain-containing protein 2.
GN   Name=Fgd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC   TISSUE=Spleen;
RX   MEDLINE=99389726; PubMed=10458911; DOI=10.1006/geno.1999.5903;
RA   Pasteris N.G., Gorski J.L.;
RT   "Isolation, characterization, and mapping of the mouse and human Fgd2
RT   genes, faciogenital dysplasia (FGD1; Aarskog syndrome) gene
RT   homologues.";
RL   Genomics 60:57-66(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Brathwaite M., Waeltz P., Schlessinger D., Nagaraja R.;
RT   "Genomic sequence analysis in the mouse t-complex region.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=Czech II; TISSUE=Mammary gland;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: May activate CDC42, a member of the Ras-like family of
CC       Rho- and Rac proteins, by exchanging bound GDP for free GTP. May
CC       play a role in regulating the actin cytoskeleton and cell shape
CC       (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BY35-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BY35-2; Sequence=VSP_013073;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in spleen and lung.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -!- CAUTION: Ref.1 sequence differs from that shown due to a
CC       frameshift in position 606.
CC   -!- CAUTION: Ref.2 (AAP45200) sequence differs from that shown due to
CC       erroneous gene model prediction.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
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DR   EMBL; AF017368; AAC35430.1; ALT_FRAME; mRNA.
DR   EMBL; AY301264; AAP45199.1; -; Genomic_DNA.
DR   EMBL; AY301264; AAP45200.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK042260; BAC31206.1; -; mRNA.
DR   EMBL; BC021845; AAH21845.1; -; mRNA.
DR   UniGene; Mm.279187; -.
DR   HSSP; Q15075; 1HYJ.
DR   MGI; MGI:1347084; Fgd2.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    655       FYVE, RhoGEF and PH domain-containing
FT                                protein 2.
FT                                /FTId=PRO_0000080943.
FT   DOMAIN      102    290       DH.
FT   DOMAIN      319    418       PH 1.
FT   DOMAIN      544    641       PH 2.
FT   ZN_FING     458    518       FYVE-type.
FT   VAR_SEQ       1    194       Missing (in isoform 2).
FT                                /FTId=VSP_013073.
FT   CONFLICT     39     39       S -> I (in Ref. 1).
SQ   SEQUENCE   655 AA;  74634 MW;  F5272F107A29BDBE CRC64;
     MERACEKQDS VCNLVAVFEN NRTPGEAPGS HSLEDQPHSP EHQLSLSPEP WEAPPVKEAL
     KSEFRPVSRT YLSSLKNKLS SGAWRRSCQP GVSPGPETQE PEEKRVVREL LETEQAYVAR
     LHLLDQVFFQ ELLREAGRSK AFPEDVVKLI FSNISSIYRF HAQFFLPELQ RRVDDWAATP
     RIGDVIQKLA PFLKMYSEYV KNFERAAELL ATWMDKSQPF QEVVTRIQCS EASSSLTLQH
     HMLEPVQRIP RYELLLKEYV QKLPAQAPDL EDAQRALDMI FSAAQHSNAA IAEMERLQGL
     WDVYQRLGLE DDIVDPSNTL LREGPVLKIS FRRSDPMERY LVLFNNMLLY CVPRVLQVGA
     QFQVRTRIDV AGMKVRELTD AEFPHSFLVS GKQRTLELQA RSRDEMVSWM QACQAAIDQV
     EKRSETFKAA VQGPQGDTQE PKPQVEELGL RAPQWVRDKM VTMCMRCQEP FNALTRRRHH
     CRACGYVVCA KCSDYRAELK YDSNRPNRVC LTCYTFLTGN VLPQGKEDKR RGILEKEASA
     APEQSLVCSF LQLIGDKCSR SLPRSWCVIP RDDPLVLYVY AAPQDTKAHT SIPLLGYQVI
     SGPQGDPRVF QLQQSGQQYT FKAESVELQG RWVTAIKRAA SGRTPEGPDE EDVSD
//
ID   FGD3_HUMAN     STANDARD;      PRT;   725 AA.
AC   Q5JSP0; Q7Z7D9; Q8N5G1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   30-MAY-2006, entry version 16.
DE   FYVE, RhoGEF and PH domain-containing protein 3 (Zinc finger FYVE
DE   domain-containing protein 5).
GN   Name=FGD3; Synonyms=ZFYVE5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Shan Y.X., Yu L.;
RT   "Cloning and characterization of a human FGD3 gene: a novel
RT   faciogenital dysplasia (FGD1; Aarskog syndrome) gene homolog.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA   Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA   Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA   Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA   Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA   Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA   Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA   Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA   Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA   Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA   Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA   McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA   Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA   Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA   Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA   Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA   Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA   Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA   Rogers J., Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   ILE-275.
RC   TISSUE=Brain;
RX   MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA   Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA   Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA   Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA   Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA   Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA   Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA   Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA   Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA   Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA   Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA   Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA   Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA   Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA   Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA   Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA   Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA   Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT   "Generation and initial analysis of more than 15,000 full-length human
RT   and mouse cDNA sequences.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
CC   -!- FUNCTION: Promotes the formation of filopodia. May activate CDC42,
CC       a member of the Ras-like family of Rho- and Rac proteins, by
CC       exchanging bound GDP for free GTP. Plays a role in regulating the
CC       actin cytoskeleton and cell shape (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5JSP0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5JSP0-2; Sequence=VSP_013074, VSP_013075;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AY211386; AAP20645.1; -; mRNA.
DR   EMBL; AL389924; CAI41117.1; -; Genomic_DNA.
DR   EMBL; AL451065; CAI41117.1; JOINED; Genomic_DNA.
DR   EMBL; AL389924; CAI41118.1; -; Genomic_DNA.
DR   EMBL; AL451065; CAI41118.1; JOINED; Genomic_DNA.
DR   EMBL; BC032429; AAH32429.1; -; mRNA.
DR   UniGene; Hs.411081; -.
DR   PDB; 2COC; NMR; A=605-703.
DR   HGNC; HGNC:16027; FGD3.
DR   GO; GO:0005794; C:Golgi apparatus; ISS.
DR   GO; GO:0030027; C:lamellipodium; ISS.
DR   GO; GO:0001726; C:ruffle; ISS.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS.
DR   GO; GO:0005515; F:protein binding; ISS.
DR   GO; GO:0031267; F:small GTPase binding; ISS.
DR   GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0046847; P:filopodium formation; ISS.
DR   GO; GO:0043088; P:regulation of Cdc42 GTPase activity; ISS.
DR   GO; GO:0008360; P:regulation of cell shape; ISS.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   3D-structure; Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Polymorphism;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    725       FYVE, RhoGEF and PH domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000080944.
FT   DOMAIN      157    341       DH.
FT   DOMAIN      370    469       PH 1.
FT   DOMAIN      604    703       PH 2.
FT   ZN_FING     532    588       FYVE-type.
FT   VAR_SEQ     596    634       KTPTADPQPSLLCGPLRLSESGETWSEVWAAIPMSDPQV
FT                                -> VGAPSSCSPPGGAAEPPDTCSCAPAAPAASAFGVSLGP
FT                                G (in isoform 2).
FT                                /FTId=VSP_013074.
FT   VAR_SEQ     635    725       Missing (in isoform 2).
FT                                /FTId=VSP_013075.
FT   VARIANT     275    275       V -> I (in dbSNP:3802384).
FT                                /FTId=VAR_021492.
SQ   SEQUENCE   725 AA;  79401 MW;  665A7FF5BE16B44B CRC64;
     MESGRGSSTP PGPIAALGMP DTGPGSSSLG KLQALPVGPR AHCGDPVSLA AAGDGSPDIG
     PTGELSGSLK IPNRDSGIDS PSSSVAGENF PCEEGLEAGP SPTVLGAHAE MALDSQVPKV
     TPQEEADSDV GEEPDSENTP QKADKDAGLA QHSGPQKLLH IAQELLHTEE TYVKRLHLLD
     QVFCTRLTDA GIPPEVIMGI FSNISSIHRF HGQFLLPELK TRITEEWDTN PRLGDILQKL
     APFLKMYGEY VKNFDRAVGL VSTWTQRSPL FKDVVHSIQK QEVCGNLTLQ HHMLEPVQRV
     PRYELLLKDY LKRLPQDAPD RKDAERSLEL ISTAANHSNA AIRKVEKMHK LLEVYEQLGG
     EEDIVNPANE LIKEGQIQKL SAKNGTPQDR HLFLFNSMIL YCVPKLRLMG QKFSVREKMD
     ISGLQVQDIV KPNTAHTFII TGRKRSLELQ TRTEEEKKEW IQIIQATIEK HKQNSETFKA
     FGGAFSQDED PSLSPDMPIT STSPVEPVVT TEGSSGAAGL EPRKLSSKTR RDKEKQSCKS
     CGETFNSITK RRHHCKLCGA VICGKCSEFK AENSRQSRVC RDCFLTQPVA PESTEKTPTA
     DPQPSLLCGP LRLSESGETW SEVWAAIPMS DPQVLHLQGG SQDGRLPRTI PLPSCKLSVP
     DPEERLDSGH VWKLQWAKQS WYLSASSAEL QQQWLETLST AAHGDTAQDS PGALQLQVPM
     GAAAP
//
ID   FGD3_MOUSE     STANDARD;      PRT;   733 AA.
AC   O88842; Q8BQ72;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   30-MAY-2006, entry version 37.
DE   FYVE, RhoGEF and PH domain-containing protein 3.
GN   Name=Fgd3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Spleen;
RX   MEDLINE=20184742; PubMed=10721717; DOI=10.1016/S0378-1119(99)00518-1;
RA   Pasteris N.G., Nagata K., Hall A., Gorski J.L.;
RT   "Isolation, characterization, and mapping of the mouse Fgd3 gene, a
RT   new faciogenital dysplasia (FGD1; Aarskog syndrome) gene homologue.";
RL   Gene 242:237-247(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
CC   -!- FUNCTION: Promotes the formation of filopodia. May activate CDC42,
CC       a member of the Ras-like family of Rho- and Rac proteins, by
CC       exchanging bound GDP for free GTP. Plays a role in regulating the
CC       actin cytoskeleton and cell shape.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O88842-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O88842-2; Sequence=VSP_013076, VSP_013077;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in adult brain, spleen, lung and
CC       skeletal muscle. Detected in embryos from E7 to E17.
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
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CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AF017369; AAC35431.1; -; mRNA.
DR   EMBL; AK051395; BAC34624.1; -; mRNA.
DR   UniGene; Mm.291089; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSMUSG00000037946; Mus musculus.
DR   MGI; MGI:1353657; Fgd3.
DR   GO; GO:0046847; P:filopodium formation; IDA.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    733       FYVE, RhoGEF and PH domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000080945.
FT   DOMAIN      153    337       DH.
FT   DOMAIN      366    465       PH 1.
FT   DOMAIN      612    711       PH 2.
FT   ZN_FING     528    584       FYVE-type.
FT   VAR_SEQ     516    532       IESRKSSSKTRRDKEKP -> VSDPHPGISRSERCLGR
FT                                (in isoform 2).
FT                                /FTId=VSP_013076.
FT   VAR_SEQ     533    733       Missing (in isoform 2).
FT                                /FTId=VSP_013077.
FT   CONFLICT      7      7       S -> P (in Ref. 2).
FT   CONFLICT    126    126       V -> M (in Ref. 2).
SQ   SEQUENCE   733 AA;  80624 MW;  86CDFEBB5DC1E8E3 CRC64;
     MELGRSSSTP QEEAISPLGV LGTGPSSSPL GKLQALPIGP GAHRGAHSSS APAGDSSTRE
     PSGAMKIPNR DSGIDSPSSS VASENFPCEE SSEGSPSPAI LGLPSETASD SRVPQDNPQE
     EEDSGVGEEP DPKVTLFRPQ EDVSLTQCSD PQKLLHIAQE LLHTEEAYVK RLHLLDQVFC
     TKLTEAGIPL EVTTGIFSNI SSIYRFHGQF LLPELQKRIT EEWDTNPRLG DILQKLAPFL
     KMYGEYVKNF DRAMGLVSTW TQRSPQFKDV IHTIQKQEVC GNLTLQHHML EPVQRVPRYE
     LLLKDYLKRL PRDAPDRKDA ERSLELISTA ADHSNAAIRK MEKMHKLLEV YEQLGGEEDI
     VNPANELIKE GSIQKLSAKN GTTQDRHLFL FNNVMLYCVP KLRLMGQKLS VREKMDISDL
     QVQDIVKPNA ACTFIITGRK RSLELQTRTE EEKKEWIQVI QATVEKHKQK SETFRAFGGA
     CSQDEEPTLS PDQPVMSTSS VEPAGVADSN GGTPGIESRK SSSKTRRDKE KPGCKSCGET
     FNSITKRRYR CKLCGEVICR KCSEFKAENS KQSRVCRECF LEEPLVPPSP SSETPTELKQ
     NAEKPPSVDP RPSLLCGTLN LSDDGTTWNE VWAAIPESDP QVLDLLAGSQ AGRLLYSIPL
     SGCNITMPDP EEGLEAGCAW KLHQGSQTWW LSAPSTKLQQ CWLKALGTAV HGDTAGDRPG
     ASQPQAPAGT DTP
//
ID   FGD3_PONPY     STANDARD;      PRT;   737 AA.
AC   Q5R5T1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   18-APR-2006, entry version 11.
DE   FYVE, RhoGEF and PH domain-containing protein 3.
GN   Name=FGD3;
OS   Pongo pygmaeus (Orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Promotes the formation of filopodia. May activate CDC42,
CC       a member of the Ras-like family of Rho- and Rac proteins, by
CC       exchanging bound GDP for free GTP. Plays a role in regulating the
CC       actin cytoskeleton and cell shape (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CR860772; CAH92885.1; -; mRNA.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Cytoskeleton; Guanine-nucleotide releasing factor; Metal-binding;
KW   Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    737       FYVE, RhoGEF and PH domain-containing
FT                                protein 3.
FT                                /FTId=PRO_0000080946.
FT   DOMAIN      157    341       DH.
FT   DOMAIN      370    469       PH 1.
FT   DOMAIN      616    715       PH 2.
FT   ZN_FING     532    588       FYVE-type.
SQ   SEQUENCE   737 AA;  80555 MW;  28C77937884E1923 CRC64;
     MESGGGSSTP PGPIAALGMP DSGPGSSSLG KLQALPVGPR AHCGDPGSLA AAGDGSLDTG
     STGELSGSLK IPNRDSGIDS PSSSVAGENF PCEEGLEAGP SPTVLGAHPE MALDSQVPKV
     TPREEADSDV GEEPDSENTP QKADKDAGLA QHSGPQKLLH IAQELLHTEE TYVKRLHLLD
     QVFCTRLTDA GIPPEVIMGI FSNISSIHRF HGQFLLPELK TRITEEWDTN PRLGDILQKL
     APFLKMYGEY VKNFDRAVGL VSTWTQRSPL FKDVVHSIQK QEVCGNLTLQ HHMLEPVQRV
     PRYELLLKDY LKRLPQDAPD QKDAERSLEL ISTAANHSNA AIRKVEKMHK LLEVYEQLGG
     EEDIANPANE LIKEGQIQKL SAKNGTPQDR HLFLFNSMIL YCVPKLRLMG QKFSVREKMD
     ISGLQVQDIV KPNTAHTFII TGRKRSLELQ TRTEEEKKEW IQIIQATIEK HKQNSETFKA
     FGGAFSQDED PSLSPDMPIT STSPVEPVVT TEGGSGAAGL EPRKLSSKTR RDKEKQSCKS
     CGETFNSITK RRHHCKLCGV VICGKCSEFK AENSRQSRVC RECFLTQPVA PESPSPEAPA
     KPRRSTEKTP TADPQPSLLC GPLRLSESGE TWSEVWAAIP MSDPQVLHLQ GGSQDGWLPR
     TIPLPSCKLS VPDPEERLDS GHVWKLQWAK QSWYLSASSA ELQQRWLETL STAARGDTAQ
     DSPGALQPQV PTGAAAP
//
ID   FGD4_HUMAN     STANDARD;      PRT;   766 AA.
AC   Q96M96; Q6ULS2; Q8TCP6;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 27.
DE   FYVE, RhoGEF and PH domain-containing protein 4 (Actin filament-
DE   binding protein frabin) (FGD1-related F-actin-binding protein) (Zinc
DE   finger FYVE domain-containing protein 6).
GN   Name=FGD4; Synonyms=FRABP, ZFYVE6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Testis;
RA   Lu L., Huang X.Y., Xu M., Yin L.L., Li J.M., Zhou Z.M., Sha J.H.;
RT   "Cloning a new transcript of actin-filament binding protein frabin in
RT   testis.";
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Testis;
RG   The German cDNA consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION.
RX   PubMed=15133042; DOI=10.1074/jbc.M401592200;
RA   Chen X.M., Splinter P.L., Tietz P.S., Huang B.Q., Billadeau D.D.,
RA   LaRusso N.F.;
RT   "Phosphatidylinositol 3-kinase and frabin mediate Cryptosporidium
RT   parvum cellular invasion via activation of Cdc42.";
RL   J. Biol. Chem. 279:31671-31678(2004).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho-
CC       and Rac proteins, by exchanging bound GDP for free GTP. Plays a
CC       role in regulating the actin cytoskeleton and cell shape.
CC       Activates MAPK8 (By similarity).
CC   -!- SUBUNIT: Homooligomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Concentrated in
CC       filopodia and poorly detected at lamellipodia. Binds along the
CC       sides of actin fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q96M96-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q96M96-2; Sequence=VSP_013078, VSP_013082;
CC         Note=No experimental confirmation available;
CC       Name=3;
CC         IsoId=Q96M96-3; Sequence=VSP_013079, VSP_013080, VSP_013081;
CC         Note=No experimental confirmation available;
CC   -!- DOMAIN: The part of the protein spanning the actin filament-
CC       binding domain together with the DH domain and the first PH domain
CC       is necessary and sufficient for microspike formation. Activation
CC       of MAPK8 requires the presence of all domains with the exception
CC       of the actin filament-binding domain (By similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
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DR   EMBL; AY367054; AAQ72372.1; -; mRNA.
DR   EMBL; AK057294; BAB71413.1; -; mRNA.
DR   EMBL; AL713762; CAD28532.1; -; mRNA.
DR   UniGene; Hs.117835; -.
DR   HSSP; Q15075; 1HYJ.
DR   Ensembl; ENSG00000139132; Homo sapiens.
DR   HGNC; HGNC:19125; FGD4.
DR   GO; GO:0005794; C:Golgi apparatus; ISS.
DR   GO; GO:0030027; C:lamellipodium; ISS.
DR   GO; GO:0001726; C:ruffle; ISS.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS.
DR   GO; GO:0005515; F:protein binding; ISS.
DR   GO; GO:0031267; F:small GTPase binding; ISS.
DR   GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0007010; P:cytoskeleton organization and biogenesis; ISS.
DR   GO; GO:0046847; P:filopodium formation; ISS.
DR   GO; GO:0043088; P:regulation of Cdc42 GTPase activity; ISS.
DR   GO; GO:0008360; P:regulation of cell shape; ISS.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Actin-binding; Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    766       FYVE, RhoGEF and PH domain-containing
FT                                protein 4.
FT                                /FTId=PRO_0000080947.
FT   DOMAIN      206    393       DH.
FT   DOMAIN      422    521       PH 1.
FT   DOMAIN      643    740       PH 2.
FT   ZN_FING     559    619       FYVE-type.
FT   REGION        1    150       Actin filament-binding (By similarity).
FT   VAR_SEQ       1    248       Missing (in isoform 2).
FT                                /FTId=VSP_013078.
FT   VAR_SEQ       1     30       MEEIKPASASCVSKEKPSKVSDLISRFEGG -> MFSCFLC
FT                                ILSF (in isoform 3).
FT                                /FTId=VSP_013079.
FT   VAR_SEQ     201    207       ETNEQKL -> VEHETSS (in isoform 3).
FT                                /FTId=VSP_013080.
FT   VAR_SEQ     208    766       Missing (in isoform 3).
FT                                /FTId=VSP_013081.
FT   VAR_SEQ     515    766       ALQETIDAFHQRHETFRNAIAKDNDIHSEVSTAELGKRAPR
FT                                WIRDNEVTMCMKCKEPFNALTRRRHHCRACGYVVCWKCSDY
FT                                KAQLEYDGGKLSKVCKDCYQIISGFTDSEEKKRKGILEIES
FT                                AEVSGNSVVCSFLQYMEKSKPWQKAWCVIPKQDPLVLYMYG
FT                                APQDVRAQATIPLLGYVVDEMPRSADLPHSFKLTQSKSVHS
FT                                FAADSEELKQKWLKVILLAVTGETPGGPNEHPATLDDHPEP
FT                                KKKSEC -> RRGFAMLPRLISNS (in isoform 2).
FT                                /FTId=VSP_013082.
FT   CONFLICT     79     79       A -> T (in Ref. 3).
FT   CONFLICT    303    303       V -> A (in Ref. 1).
SQ   SEQUENCE   766 AA;  86596 MW;  125E9B0C008BAE5E CRC64;
     MEEIKPASAS CVSKEKPSKV SDLISRFEGG SSLSNYSDLK KESAVNLNAP RTPGRHGLTT
     TPQQKLLSQH LPQRQGNDAD KTQGAQTCVA NGVMAAQNQM ECEEEKAATL SSDTSIQASE
     PLLDTHIVNG ERDETATAPA SPTTDSCDGN ASDSSYRTPG IGPVLPLEER GAETETKVQE
     RENGESPLEL EQLDQHHEMK ETNEQKLHKI ANELLLTERA YVNRLDLLDQ VFYCKLLEEA
     NRGSFPAEMV NKIFSNISSI NAFHSKFLLP ELEKRMQEWE TTPRIGDILQ KLAPFLKMYG
     EYVKGFDNAM ELVKNMTERI PQFKSVVEEI QKQKICGSLT LQHHMLEPVQ RIPRYEMLLK
     DYLRKLPPDS LDWNDAKKSL EIISTAASHS NSAIRKMENL KKLLEIYEML GEEEDIVNPS
     NELIKEGQIL KLAARNTSAQ ERYLFLFNNM LLYCVPKFSL VGSKFTVRTR VGIDGMKIVE
     TQNEEYPHTF QVSGKERTLE LQASSAQDKE EWIKALQETI DAFHQRHETF RNAIAKDNDI
     HSEVSTAELG KRAPRWIRDN EVTMCMKCKE PFNALTRRRH HCRACGYVVC WKCSDYKAQL
     EYDGGKLSKV CKDCYQIISG FTDSEEKKRK GILEIESAEV SGNSVVCSFL QYMEKSKPWQ
     KAWCVIPKQD PLVLYMYGAP QDVRAQATIP LLGYVVDEMP RSADLPHSFK LTQSKSVHSF
     AADSEELKQK WLKVILLAVT GETPGGPNEH PATLDDHPEP KKKSEC
//
ID   FGD4_MOUSE     STANDARD;      PRT;   766 AA.
AC   Q91ZT5; Q3UEB6; Q8BW60; Q8BZI7; Q91ZT3; Q91ZT4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   30-MAY-2006, entry version 29.
DE   FYVE, RhoGEF and PH domain-containing protein 4 (Actin filement-
DE   binding protein frabin) (FGD1-related F-actin-binding protein).
GN   Name=Fgd4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION,
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6; TISSUE=Brain;
RX   MEDLINE=21418809; PubMed=11527409; DOI=10.1006/bbrc.2001.5481;
RA   Ikeda W., Nakanishi H., Takekuni K., Itoh S., Takai Y.;
RT   "Identification of splicing variants of Frabin with partly different
RT   functions and tissue distribution.";
RL   Biochem. Biophys. Res. Commun. 286:1066-1072(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-754 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Diencephalon, and Oviduct;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   FUNCTION.
RX   PubMed=10871857; DOI=10.1038/sj.onc.1203631;
RA   Ono Y., Nakanishi H., Nishimura M., Kakizaki M., Takahashi K.,
RA   Miyahara M., Satoh-Horikawa K., Mandai K., Takai Y.;
RT   "Two actions of frabin: direct activation of Cdc42 and indirect
RT   activation of Rac.";
RL   Oncogene 19:3050-3058(2000).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=11952837;
RA   Kim Y., Ikeda W., Nakanishi H., Tanaka Y., Takekuni K., Itoh S.,
RA   Monden M., Takai Y.;
RT   "Association of frabin with specific actin and membrane structures.";
RL   Genes Cells 7:413-420(2002).
CC   -!- FUNCTION: Activates CDC42, a member of the Ras-like family of Rho-
CC       and Rac proteins, by exchanging bound GDP for free GTP. Activates
CC       MAPK8 (By similarity). Plays a role in regulating the actin
CC       cytoskeleton and cell shape. Promotes the formation of
CC       lamellipodia.
CC   -!- SUBUNIT: Homooligomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Concentrated in
CC       filopodia and poorly detected at lamellipodia. Binds along the
CC       sides of actin fibers (By similarity).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1; Synonyms=Frabin alpha;
CC         IsoId=Q91ZT5-1; Sequence=Displayed;
CC       Name=2; Synonyms=Frabin beta;
CC         IsoId=Q91ZT5-2; Sequence=VSP_013086, VSP_013087;
CC       Name=3; Synonyms=Frabin gamma;
CC         IsoId=Q91ZT5-3; Sequence=VSP_013084, VSP_013085;
CC       Name=4;
CC         IsoId=Q91ZT5-4; Sequence=VSP_013083, VSP_013084, VSP_013085;
CC         Note=No experimental confirmation available;
CC   -!- TISSUE SPECIFICITY: Detected in brain, thymus, lung, heart,
CC       skeletal muscle, small intestine, liver, kidney, spleen and
CC       testis.
CC   -!- DOMAIN: The part of the protein spanning the actin filament-
CC       binding domain together with the DH domain and the first PH domain
CC       is necessary and sufficient for microspike formation. Activation
CC       of MAPK8 requires the presence of all domains with the exception
CC       of the actin filament-binding domain (By similarity).
CC   -!- SIMILARITY: Contains 1 DH (DBL-homology) domain.
CC   -!- SIMILARITY: Contains 1 FYVE-type zinc finger.
CC   -!- SIMILARITY: Contains 2 PH domains.
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DR   EMBL; AF402611; AAL05631.1; -; mRNA.
DR   EMBL; AF402612; AAL05632.1; -; mRNA.
DR   EMBL; AF402613; AAL05633.1; -; mRNA.
DR   EMBL; AK034504; BAC28733.1; -; mRNA.
DR   EMBL; AK054242; BAC35703.2; -; mRNA.
DR   EMBL; AK149626; BAE28995.1; -; mRNA.
DR   UniGene; Mm.256131; -.
DR   UniGene; Mm.396746; -.
DR   HSSP; Q15075; 1HYJ.
DR   IntAct; Q91ZT5; -.
DR   Ensembl; ENSMUSG00000022788; Mus musculus.
DR   MGI; MGI:2183747; Fgd4.
DR   GO; GO:0030175; C:filopodium; IDA.
DR   GO; GO:0030027; C:lamellipodium; IDA.
DR   GO; GO:0030032; P:lamellipodium biogenesis; IDA.
DR   GO; GO:0030035; P:microspike biogenesis; IDA.
DR   InterPro; IPR001849; PH.
DR   InterPro; IPR011993; PH_type.
DR   InterPro; IPR000219; RhoGEF.
DR   InterPro; IPR000306; Znf_FYVE.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   Pfam; PF01363; FYVE; 1.
DR   Pfam; PF00169; PH; 2.
DR   Pfam; PF00621; RhoGEF; 1.
DR   SMART; SM00064; FYVE; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM00325; RhoGEF; 1.
DR   PROSITE; PS50010; DH_2; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   PROSITE; PS50178; ZF_FYVE; 1.
KW   Actin-binding; Alternative splicing; Cytoskeleton;
KW   Guanine-nucleotide releasing factor; Metal-binding; Repeat; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    766       FYVE, RhoGEF and PH domain-containing
FT                                protein 4.
FT                                /FTId=PRO_0000080948.
FT   DOMAIN      206    393       DH.
FT   DOMAIN      422    521       PH 1.
FT   DOMAIN      643    740       PH 2.
FT   ZN_FING     559    619       FYVE-type.
FT   REGION        1    150       Actin filament-binding (By similarity).
FT   VAR_SEQ       1     44       Missing (in isoform 4).
FT                                /FTId=VSP_013083.
FT   VAR_SEQ     504    504       S -> R (in isoform 3 and isoform 4).
FT                                /FTId=VSP_013084.
FT   VAR_SEQ     505    766       Missing (in isoform 3 and isoform 4).
FT                                /FTId=VSP_013085.
FT   VAR_SEQ     589    603       VCWKCSDYKAQLEYD -> SEASSLSQLLEMVYR (in
FT                                isoform 2).
FT                                /FTId=VSP_013086.
FT   VAR_SEQ     604    766       Missing (in isoform 2).
FT                                /FTId=VSP_013087.
FT   CONFLICT     36     36       Y -> C (in Ref. 2; BAC35703).
FT   CONFLICT     49     49       I -> V (in Ref. 2; BAC35703).
FT   CONFLICT    278    278       E -> K (in Ref. 2; B