ID 41_BOVIN STANDARD; PRT; 617 AA. AC Q9N179; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 18-APR-2006, entry version 31. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=EPB41; Synonyms=E41P; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Japanese black; TISSUE=Bone marrow; RA Saito D., Inaba M., Koshino I., Matsumoto M., Ono K.; RT "The interaction of bovine red blood cell protein 4.1 with red blood RT cell membranes."; RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions (By similarity). CC -!- PTM: Phosphorylation on Tyr-413 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex (By CC similarity). CC -!- SIMILARITY: Contains 1 FERM 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; AF222767; AAF61703.1; -; mRNA. DR UniGene; Bt.33189; -. DR HSSP; P11171; 1GG3. DR SMR; Q9N179; 1-279. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Nuclear protein; Phosphorylation; KW Structural protein. FT CHAIN 1 617 Protein 4.1. FT /FTId=PRO_0000219388. FT DOMAIN 1 282 FERM. FT REGION 401 466 Spectrin--actin-binding. FT REGION 467 617 Carboxyl-terminal (CTD). FT MOD_RES 413 413 Phosphotyrosine (by EGFR) (By FT similarity). FT MOD_RES 465 465 Phosphoserine (by CDC2) (By similarity). SQ SEQUENCE 617 AA; 69258 MW; 5B49D5008AD900FB CRC64; MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGADY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKEKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV EPADRTPRPT SAPAIAPSPA AEGGVPGAPV KKAQKETVQV EVKQEEAPPE DAEPEPSEAW KKKRERLDGE NIYIRHSNLM LEDLDKSQEE IKKHHASISE LKKNFMESVP EPRPSEWDKR LSTHSPFRTL NINGQIPTGE GPPLVKTQTV TISDTANAVK SEIPTKDVPI VHTETKTITY EAAQTDDSNG DLDPGVLLTA QTITSETTSS TTTTQITKTV KGGISETRIE KRIVITGDAD IDHDQVLVQA IKEAKEQHPD MSVTKVVVHQ ETEISEE // ID 41_CANFA STANDARD; PRT; 810 AA. AC Q6Q7P4; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-MAY-2006, entry version 17. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=EPB41; OS Canis familiaris (Dog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; OC Canis. OX NCBI_TaxID=9615; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Cocker spaniel; TISSUE=Kidney; RX PubMed=15525677; DOI=10.1091/mbc.E04-05-0426; RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., RA Jagadeeswaran R., Benz E.J. Jr.; RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 RT kinase."; RL Mol. Biol. Cell 16:117-127(2005). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain (By similarity). CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions (By similarity). CC -!- SIMILARITY: Contains 1 FERM 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; AY553843; AAS59144.1; -; mRNA. DR UniGene; Cfa.3914; -. DR SMR; Q6Q7P4; 211-489. DR Ensembl; ENSCAFG00000011677; Canis familiaris. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Glycoprotein; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN 1 810 Protein 4.1. FT /FTId=PRO_0000219389. FT DOMAIN 211 492 FERM. FT REGION 615 659 Spectrin--actin-binding. FT REGION 660 810 Carboxyl-terminal (CTD). FT COMPBIAS 680 752 Thr-rich. FT MOD_RES 61 61 Phosphothreonine (By similarity). FT MOD_RES 658 658 Phosphoserine (By similarity). SQ SEQUENCE 810 AA; 90688 MW; 8F033CCA3C157602 CRC64; MTTEKSLVAE AENSQHQQQK EEGEGVTNSG QQETQLEELS QEAAEGDNHC EQKLKTSNGD TPTHEDLTKN KERTSENRGL SRLFSSFLKR PKSQVSEEEG KDVESAKEKC EGGQKEIEFG TSLDEEIILK APIAAPEPEL KTDPSLDLHS LSSAETQPAQ EEHREDPDFE TKEGGGLEEC SKIEVKEESP ESKAERELKA SQKSIRRHRN MHCKVSLLDD TVYECVVEKH AKGQDLLKRV CEHLNLLEED YFGLAIWDNG ASKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVSGRLP CSFATLALLG SYTIQSELGD YDPELHGAEY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISYKRSSFFI KIRPGEQEQY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTLPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAV DSDRSPRPTS APAIAQSQDA EGTVPGAPVK KTVVSKAQKE TVKDEEKKEE GPPDQAEPEP TEVWKDLDKS QEEIKKHHAS ISELKKNFME SVPEPRPSEW DKRLSTHSPF RTLNINGQLP TGEGPPLVKT QTVTISDTAN SVKSEIPTKD VPIVHTETKT ITYEAAQTDD SNGDLDPGVL LTAQTITSET TSSTTTTQIT KTVKGGISET RIEKRIVITG DADIDHDQVL VQAIKEAKEQ HPDMSVTKVV VHQETEISEE // ID 41_CHICK STANDARD; PRT; 90 AA. AC P12264; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 04-APR-2006, entry version 45. DE Erythroid protein 4.1 (Band 4.1) (Fragment). GN Name=EPB41; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING. RX MEDLINE=87260822; PubMed=3474611; RA Ngai J., Stack J.H., Moon R.T., Lazarides E.; RT "Regulated expression of multiple chicken erythroid membrane skeletal RT protein 4.1 variants is governed by differential RNA processing and RT translational control."; RL Proc. Natl. Acad. Sci. U.S.A. 84:4432-4436(1987). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=1; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=P12264-1; Sequence=Displayed; CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- SIMILARITY: Contains 1 FERM 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; M16962; AAA48762.1; -; mRNA. DR PIR; A27056; A27056. DR UniGene; Gga.2886; -. DR HSSP; P11171; 1GG3. DR SMR; P12264; 1-90. DR Ensembl; ENSGALG00000001326; Gallus gallus. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PROSITE; PS00660; FERM_1; PARTIAL. DR PROSITE; PS00661; FERM_2; PARTIAL. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN <1 >90 Erythroid protein 4.1. FT /FTId=PRO_0000219392. FT DOMAIN 1 90 FERM. FT NON_TER 1 1 FT NON_TER 90 90 SQ SEQUENCE 90 AA; 10395 MW; 8938A0C88816604A CRC64; EFLENAKKLS MYGVDLHHAK DLEGVDITLG VCSSGLLVYK DKLRINRFPW PKVLKISYKR SSFFIKIRPG EQEQYESTIG FKLPSYRAAK // ID 41_DROME STANDARD; PRT; 1698 AA. AC Q9V8R9; Q24440; Q24441; Q24442; Q9V8R8; Q9V8S0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 30-MAY-2006, entry version 44. DE Protein 4.1 homolog (Protein coracle). GN Name=cora; ORFNames=CG11949; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2 AND 3), AND FUNCTION. RC STRAIN=Oregon-R; TISSUE=Embryo; RX MEDLINE=94215495; PubMed=8162854; RA Fehon R.G., Dawson I.A., Artavanis-Tsakonas S.; RT "A Drosophila homologue of membrane-skeleton protein 4.1 is associated RT with septate junctions and is encoded by the coracle gene."; RL Development 120:545-557(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORMS 1; 3 AND 4). RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [3] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC STRAIN=Berkeley; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: An integral component of the septate junction. May play CC a role in cell-cell interactions that are necessary for proper CC development. Vital for embryonic development. CC -!- INTERACTION: CC Q9VHU9-1:CG9636; NbExp=1; IntAct=EBI-219149, EBI-219164; CC -!- SUBCELLULAR LOCATION: Septate junction in the apical-lateral CC domain of epithelial cells during embryonic and imaginal disk CC development. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; CC IsoId=Q9V8R9-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9V8R9-2; Sequence=VSP_000476, VSP_000477, VSP_000479, CC VSP_000480, VSP_000481; CC Name=3; CC IsoId=Q9V8R9-3; Sequence=VSP_000475, VSP_000478, VSP_000479; CC Name=4; CC IsoId=Q9V8R9-4; Sequence=VSP_000476, VSP_000477, VSP_000479; CC Name=5; CC IsoId=Q9V8R9-5; Sequence=VSP_000474, VSP_000478; CC -!- TISSUE SPECIFICITY: At onset of germ band retraction, expression CC is seen in epidermis, hindgut and foregut. During retraction, CC expression extends to tracheal branches and salivary glands. CC -!- DEVELOPMENTAL STAGE: Expressed weakly in 4-8 hours embryos, more CC abundant expression in 8-12 hours and remains throughout later CC embryonic and larval stages. CC -!- SIMILARITY: Contains 1 FERM 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; L27467; AAB59187.1; -; mRNA. DR EMBL; L27468; AAA28742.1; -; mRNA. DR EMBL; L27469; AAA28743.1; -; mRNA. DR EMBL; AE003796; AAF57591.1; -; Genomic_DNA. DR EMBL; AE003796; AAF57592.1; -; Genomic_DNA. DR EMBL; AE003796; AAF57593.1; -; Genomic_DNA. DR EMBL; AY070992; AAL48614.1; -; mRNA. DR PIR; T13800; T13800. DR UniGene; Dm.4694; -. DR HSSP; P11171; 1GG3. DR IntAct; Q9V8R9; -. DR Ensembl; CG11949; Drosophila melanogaster. DR FlyBase; FBgn0010434; cora. DR BioCyc; DMEL-XXX-02:DMEL-XXX-02-005495-MONOMER; -. DR GO; GO:0005918; C:septate junction; IDA. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0007391; P:dorsal closure; TAS. DR GO; GO:0008362; P:embryonic cuticle biosynthesis (sensu Insecta); TAS. DR GO; GO:0009790; P:embryonic development; IMP. DR GO; GO:0007163; P:establishment and/or maintenance of cell po...; NAS. DR GO; GO:0045216; P:intercellular junction assembly and mainten...; TAS. DR GO; GO:0006612; P:protein targeting to membrane; TAS. DR GO; GO:0035151; P:regulation of tracheal tube size; IMP. DR GO; GO:0007435; P:salivary gland morphogenesis; TAS. DR GO; GO:0019991; P:septate junction assembly; TAS. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Alternative splicing; Complete proteome; Developmental protein; KW Membrane. FT CHAIN 1 1698 Protein 4.1 homolog. FT /FTId=PRO_0000219394. FT DOMAIN 32 314 FERM. FT REGION 317 434 Hydrophilic. FT REGION 1286 1698 Carboxyl-terminal (CTD). FT COMPBIAS 404 449 Lys-rich. FT COMPBIAS 731 775 Ala-rich. FT COMPBIAS 1437 1643 Thr-rich. FT VAR_SEQ 1 312 Missing (in isoform 5). FT /FTId=VSP_000474. FT VAR_SEQ 409 409 K -> KSSTGTASASSQSSLEGDYETNLEIEAIEAEPPVQ FT (in isoform 2 and isoform 4). FT /FTId=VSP_000476. FT VAR_SEQ 409 409 K -> KLMRQSSTGTASASSQSSLEGDYETNLEIEAIEAEP FT PVQ (in isoform 3). FT /FTId=VSP_000475. FT VAR_SEQ 482 1480 Missing (in isoform 3 and isoform 5). FT /FTId=VSP_000478. FT VAR_SEQ 482 1290 Missing (in isoform 2 and isoform 4). FT /FTId=VSP_000477. FT VAR_SEQ 1554 1587 Missing (in isoform 2, isoform 3 and FT isoform 4). FT /FTId=VSP_000479. FT VAR_SEQ 1629 1635 VSSKTRT -> GGGGGGI (in isoform 2). FT /FTId=VSP_000480. FT VAR_SEQ 1636 1698 Missing (in isoform 2). FT /FTId=VSP_000481. FT CONFLICT 970 970 I -> V (in Ref. 1; AAB59187). SQ SEQUENCE 1698 AA; 184168 MW; 93940FC4F1ACEB83 CRC64; MPAEIKPSAP AEPETPTKSK PKSSSSSHGK PALARVTLLD GSLLDVSIDR KAIGRDVINS ICAGLNLIEK DYFGLTYETP TDPRTWLDLE KPVSKFFRTD TWPLTFAVKF YPPEPSQLKE DITRYHLCLQ VRNDILEGRL PCTFVTHALL GSYLVQSEMG DYDAEEMPTR AYLKDFKIAP NQTAELEDKV MDLHKTHKGQ SPAEAELHYL ENAKKLAMYG VDLHPAKDSE GVDIMLGVCA SGLLVYRDKL RINRFAWPKI LKISYKRHHF YIKIRPGEFE QYESTIGFKL ANHRAAKKLW KSCVEHHTFF RLMTPEPVSK SKMFPVFGST YRYKGRTQAE STNTPVDRTP PKFNRTLSGA RLTSRSMDAL ALAEKEKVAR KSSTLDHRGD RNADGDAHSR SPIKNKKEKD ADKEAKLREK KQKEKEEKER KEREKRELEE KKKAEKAAKA ALAAGAAAGA AVNGNDELND SNKSDKSSGR RGVGIFSSGR KSKSGSPSKD GKDKSGKDKD KEVGRLGLVV TSGLGDNQQD QNLDEAARNA AKNRGSTTPG VTRQYEYAVD NDGNTSPTRK SYTPGGFRYD QDPNSRKSGA DGQEQLSPTS QQKKIGLAFN YAPGNENALK ETAEKLKAGQ LSPRTQDKLN RGQLSPKSRA KLLQDPLLSP TTRAKLQGSA VDAAAVPLSD SQKRSYSPTK GPQGYSSGAP GSYKPISDPT ADFLESQRYN KEPGYVGPSK ADVAAGLAGA AGSKKPGSPT KTGKGAPGAA AAAAAGAAGA AAAAAKPKKR RVKIMVITSK FDPSTKRIDA ENGSIEHSTG ILDPATGLID TKYGVIDPKK GTLEALNTKT GKKEVFQGDV DGKTGNLHLV SGVADPKTGR LDDTLGQIVC ITPQDNPVVE LTVITSRIDP ATGKIDTVNG DVERSLGVLN LDTGLLDTKY GEINTRTGEL KAIDPKSGKI VVSKNVKVDP GTGQITILGI VDPKTNKIDP NQGRLIEVGQ QIDPIVEVTS LAGKFDSKRN IIDPKTAQVE TSGGQFDPKA GKIDTKYGQI DLVKHTITFN DPKSGKTVTR DIKIEPTTGQ IVLKNQVNPK NNKPDKDYAR IISLRIVQQR VDPATKAPIT EVSASKDKDI VVDPKSNQIW VPTGATDPAT KEQQYISSSV DPKTGYVITI YGYLDPKTNE IKKQTKLDPN TIKIEPTSGK IYTATGEVDQ ATGEPLYAAT QVDPESGEVY TKLARVDPKT GKIVIVRILL ISKTDERGRP EEIDPSTCEI DPVSGRVLKF FNKTVYVYNM IDPVTGEIVQ VDPNDPRFAG ARTTVTHTMT LTGEIDPVTG RIKSEYGDID PNTGDIDPAT AVTDPVTGKL ILNYAQIDPS HFGKQAQVQT TTETVPITRQ QFFDGVKHIS KGALRRDSEG SSDDDMTAQY GADQVNEILI GSPAGQAGGK LGKPVSTPTV VKTTTKQVLT KNIDGVTHNV EEEVRNLGTG EVTYSTQEHK ADATPTDLSG AYVTATAVTT RTATTHEDLG KNAKTEQLEE KTVATTRTHD PNKQQQRVVT QEVKTTATVT SGDQYQRRDS VSSTSSGDSG TPIDGPYDGA SVVRTDNQKS PLFTTSATTG PHVESTRVVL GEDTPGFSGH GEIISTQTVS SKTRTVETIT YKTERDGIVE TRVEQKITIQ SDGDPIDHDK ALAEAIQEAT AMNPDMTVEK IEIQQQTQ // ID 41_HUMAN STANDARD; PRT; 864 AA. AC P11171; P11176; Q14245; Q5TB35; Q5VXN8; Q8IXV9; Q9Y578; Q9Y579; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 4. DT 30-MAY-2006, entry version 77. DE Protein 4.1 (Band 4.1) (P4.1) (EPB4.1) (4.1R). GN Name=EPB41; Synonyms=E41P; 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 4), AND PROTEIN SEQUENCE OF RP 378-393. RC TISSUE=Reticulocyte; RX MEDLINE=87092279; PubMed=3467321; RA Conboy J.G., Kan Y.W., Shohet S.B., Mohandas N.; RT "Molecular cloning of protein 4.1, a major structural element of the RT human erythrocyte membrane skeleton."; RL Proc. Natl. Acad. Sci. U.S.A. 83:9512-9516(1986). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX MEDLINE=89132003; PubMed=3223413; RA Tang T.K., Leto T.L., Marchesi V.T., Benz E.J. Jr.; RT "Expression of specific isoforms of protein 4.1 in erythroid and non- RT erythroid tissues."; RL Adv. Exp. Med. Biol. 241:81-95(1988). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5 AND 6). RX MEDLINE=88234496; PubMed=3375238; RA Tang T.K., Leto T.L., Correas I., Alonso M.A., Marchesi V.T., RA Benz E.J. Jr.; RT "Selective expression of an erythroid-specific isoform of protein RT 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 85:3713-3717(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX MEDLINE=91217063; PubMed=2022644; RA Conboy J.G., Chan J.Y.C., Chasis J.A., Kan Y.W., Mohandas N.; RT "Tissue- and development-specific alternative RNA splicing regulates RT expression of multiple isoforms of erythroid membrane protein 4.1."; RL J. Biol. Chem. 266:8273-8280(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Huang S.C., Wang C., Lichtenauer U., Vortmeyer A., Zhuang Z.; RT "Sequence of protein 4.1 from a human neuroblastoma cell line: LAN5."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RG Human chromosome 1 international sequencing consortium; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). 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 [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 157-227, AND VARIANT ILE-214. RA Lichtenauer U., Huang S.C., Vortmeyer A., Zhuang Z.; RT "Valine to isoleucine polymorphism in exon 4 of human protein 4.1."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE OF 669-864 (ISOFORM 4), AND ALTERNATIVE SPLICING. RX MEDLINE=89057876; PubMed=3194408; RA Conboy J.G., Chan J., Mohandas N., Kan Y.W.; RT "Multiple protein 4.1 isoforms produced by alternative splicing in RT human erythroid cells."; RL Proc. Natl. Acad. Sci. U.S.A. 85:9062-9065(1988). RN [10] RP PROTEIN SEQUENCE OF 534-541; 693-701 AND 793-794, AND PHOSPHORYLATION RP AT SERINE RESIDUES. RX MEDLINE=91027920; PubMed=2171679; DOI=10.1016/0167-4889(90)90095-U; RA Horne W.C., Prinz W.C., Tang E.K.; RT "Identification of two cAMP-dependent phosphorylation sites on RT erythrocyte protein 4.1."; RL Biochim. Biophys. Acta 1055:87-92(1990). RN [11] RP PROTEIN SEQUENCE OF 648-714. RX MEDLINE=87008553; PubMed=3531202; RA Correas I., Speicher D.W., Marchesi V.T.; RT "Structure of the spectrin-actin binding site of erythrocyte protein RT 4.1."; RL J. Biol. Chem. 261:13362-13366(1986). RN [12] RP STRUCTURE OF CARBOHYDRATES. RX MEDLINE=90036892; PubMed=2808371; RA Inaba M., Maede Y.; RT "O-N-acetyl-D-glucosamine moiety on discrete peptide of multiple RT protein 4.1 isoforms regulated by alternative pathways."; RL J. Biol. Chem. 264:18149-18155(1989). RN [13] RP PHOSPHORYLATION AT TYR-660. RX MEDLINE=91271361; PubMed=1647028; RA Subrahmanyan G., Bertics P.J., Anderson R.A.; RT "Phosphorylation of protein 4.1 on tyrosine-418 modulates its function RT in vitro."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5222-5226(1991). RN [14] RP INTERACTION WITH DLG1. RX MEDLINE=95024052; PubMed=7937897; RA Lue R.A., Marfatia S.M., Branton D., Chishti A.H.; RT "Cloning and characterization of hdlg: the human homologue of the RT Drosophila discs large tumor suppressor binds to protein 4.1."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9818-9822(1994). RN [15] RP INTERACTION WITH CALMODULIN. RX MEDLINE=20158947; PubMed=10692436; DOI=10.1074/jbc.275.9.6360; RA Nunomura W., Takakuwa Y., Parra M., Conboy J.G., Mohandas N.; RT "Ca(2+)-dependent and Ca(2+)-independent calmodulin binding sites in RT erythrocyte protein 4.1. Implications for regulation of protein 4.1 RT interactions with transmembrane proteins."; RL J. Biol. Chem. 275:6360-6367(2000). RN [16] RP INTERACTION WITH CENPJ. RX MEDLINE=20459281; PubMed=11003675; RX DOI=10.1128/MCB.20.20.7813-7825.2000; RA Hung L.-Y., Tang C.J., Tang T.K.; RT "Protein 4.1 R-135 interacts with a novel centrosomal protein (CPAP) RT which is associated with the gamma-tubulin complex."; RL Mol. Cell. Biol. 20:7813-7825(2000). RN [17] RP CHARACTERIZATION OF C-TERMINAL DOMAIN. RX MEDLINE=21325946; PubMed=11432737; RA Scott C., Phillips G.W., Baines A.J.; RT "Properties of the C-terminal domain of 4.1 proteins."; RL Eur. J. Biochem. 268:3709-3717(2001). RN [18] RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING. RX MEDLINE=22421379; PubMed=12427749; DOI=10.1074/jbc.M201521200; RA Luque C.M., Perez-Ferreiro C.M., Perez-Gonzalez A., Englmeier L., RA Koffa M.D., Correas I.; RT "An alternative domain containing a leucine-rich sequence regulates RT nuclear cytoplasmic localization of protein 4.1R."; RL J. Biol. Chem. 278:2686-2691(2003). RN [19] RP MUTAGENESIS OF THR-60 AND SER-712, AND PHOSPHORYLATION AT THR-60 AND RP SER-712. RX PubMed=15525677; DOI=10.1091/mbc.E04-05-0426; RA Huang S.-C., Liu E.S., Chan S.-H., Munagala I.D., Cho H.T., RA Jagadeeswaran R., Benz E.J. Jr.; RT "Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 RT kinase."; RL Mol. Biol. Cell 16:117-127(2005). RN [20] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 210-488. RX MEDLINE=20473226; PubMed=11017195; DOI=10.1038/82819; RA Han B.-G., Nunomura W., Takakuwa Y., Mohandas N., Jap B.K.; RT "Protein 4.1R core domain structure and insights into regulation of RT cytoskeletal organization."; RL Nat. Struct. Biol. 7:871-875(2000). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes. CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin, CENPJ and DLG1. Also found to CC associate with contractile apparatus and tight junctions. CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; CC IsoId=P11171-1; Sequence=Displayed; CC Name=2; CC IsoId=P11171-2; Sequence=VSP_000470; CC Name=3; CC IsoId=P11171-3; Sequence=VSP_000468, VSP_000471; CC Name=4; Synonyms=Erythroid; CC IsoId=P11171-4; Sequence=VSP_000468, VSP_000470, VSP_000473; CC Name=5; Synonyms=Non-erythroid A; CC IsoId=P11171-5; Sequence=VSP_000469, VSP_000470, VSP_000472; CC Name=6; Synonyms=Non-erythroid B; CC IsoId=P11171-6; Sequence=VSP_000468, VSP_000469, VSP_000470, CC VSP_000472; CC Name=7; CC IsoId=P11171-7; Sequence=VSP_000471, VSP_012872, VSP_012873; CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- PTM: Phosphorylation on Tyr-660 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex. CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain. CC -!- DISEASE: Defects in EPB41 are the cause of elliptocytosis 1 (EL1) CC [MIM:130500]. EL1 is a rhesus-linked form of hereditary CC elliptocytosis. Elliptocytosis (also known as ovalocytosis) is a CC genetically heterogeneous, autosomal dominant hematologic CC disorder. It is characterized by variable hemolytic anemia and CC elliptical or oval red cell shape. CC -!- DISEASE: Defects in EPB41 are a cause of hereditary CC pyropoikilocytosis (HPP) [MIM:266140]. HPP is an autosomal CC recessive hematologic disorder characterized by hemolytic anemia, CC microspherocytosis, poikilocytosis, and an unusual thermal CC sensitivity of red cells. CC -!- SIMILARITY: Contains 1 FERM 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; M14993; AAA35795.1; -; mRNA. DR EMBL; J03796; AAA35793.1; -; mRNA. DR EMBL; J03796; AAA35794.1; -; mRNA. DR EMBL; M61733; AAA35797.1; -; mRNA. DR EMBL; AF156225; AAD42222.1; -; mRNA. DR EMBL; AL138785; CAI21967.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21967.1; JOINED; Genomic_DNA. DR EMBL; AL138785; CAI21968.1; -; Genomic_DNA. DR EMBL; AL138785; CAI21970.1; -; Genomic_DNA. DR EMBL; AL357500; CAI21970.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71636.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71636.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71637.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71637.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71638.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71638.1; JOINED; Genomic_DNA. DR EMBL; AL357500; CAH71639.1; -; Genomic_DNA. DR EMBL; AL138785; CAH71639.1; JOINED; Genomic_DNA. DR EMBL; BC039079; AAH39079.1; -; mRNA. DR EMBL; AF156226; AAD42223.1; -; Genomic_DNA. DR PIR; A39810; MMHUE4. DR UniGene; Hs.175437; -. DR UniGene; Hs.619217; -. DR PDB; 1GG3; X-ray; A/B/C=210-488. DR GlycoSuiteDB; P11171; -. DR Ensembl; ENSG00000159023; Homo sapiens. DR HGNC; HGNC:3377; EPB41. DR MIM; 130500; gene+phenotype. DR MIM; 266140; phenotype. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0008091; C:spectrin; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; NAS. DR GO; GO:0008015; P:circulation; TAS. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW 3D-structure; Actin-binding; Alternative splicing; Cytoskeleton; KW Direct protein sequencing; Elliptocytosis; Glycoprotein; KW Hereditary hemolytic anemia; Nuclear protein; Phosphorylation; KW Polymorphism; Pyropoikilocytosis; Structural protein. FT CHAIN 1 864 Protein 4.1. FT /FTId=PRO_0000219390. FT DOMAIN 210 491 FERM. FT REGION 494 614 Hydrophilic. FT REGION 615 713 Spectrin--actin-binding. FT REGION 714 864 Carboxyl-terminal (CTD). FT MOD_RES 60 60 Phosphothreonine (by CDC2). FT MOD_RES 660 660 Phosphotyrosine (by EGFR). FT MOD_RES 712 712 Phosphoserine (by CDC2). FT VAR_SEQ 1 209 Missing (in isoform 3, isoform 4 and FT isoform 6). FT /FTId=VSP_000468. FT VAR_SEQ 228 262 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000469. FT VAR_SEQ 616 648 Missing (in isoform 2, isoform 4, isoform FT 5 and isoform 6). FT /FTId=VSP_000470. FT VAR_SEQ 635 648 Missing (in isoform 3 and isoform 7). FT /FTId=VSP_000471. FT VAR_SEQ 649 669 Missing (in isoform 5 and isoform 6). FT /FTId=VSP_000472. FT VAR_SEQ 729 733 PPLVK -> VSTLS (in isoform 7). FT /FTId=VSP_012872. FT VAR_SEQ 734 864 Missing (in isoform 7). FT /FTId=VSP_012873. FT VAR_SEQ 772 805 Missing (in isoform 4). FT /FTId=VSP_000473. FT VARIANT 214 214 V -> I. FT /FTId=VAR_009122. FT MUTAGEN 60 60 T->A: Loss of CDC2-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-712. FT MUTAGEN 712 712 S->A: Loss of CDC2-mediated FT phosphorylation. Abolishes targeting onto FT the mitotic spindle; when associated with FT A-60. FT CONFLICT 51 51 Q -> H (in Ref. 5). FT CONFLICT 76 76 S -> N (in Ref. 5). FT CONFLICT 168 168 F -> S (in Ref. 8). FT CONFLICT 259 259 A -> T (in Ref. 5). FT CONFLICT 665 665 N -> S (in Ref. 5). FT CONFLICT 669 669 E -> K (in Ref. 9). FT CONFLICT 679 679 K -> E (in Ref. 5). FT CONFLICT 802 802 Q -> K (in Ref. 2, 3, 7 and 9). FT CONFLICT 852 852 K -> L (in Ref. 9). FT CONFLICT 863 863 D -> E (in Ref. 9). FT STRAND 211 215 FT TURN 217 218 FT STRAND 219 219 FT STRAND 221 225 FT TURN 228 229 FT HELIX 232 243 FT TURN 244 245 FT STRAND 247 247 FT STRAND 250 252 FT STRAND 254 256 FT STRAND 259 261 FT STRAND 264 264 FT TURN 267 268 FT STRAND 269 269 FT HELIX 271 274 FT TURN 275 277 FT STRAND 278 278 FT STRAND 280 285 FT STRAND 287 288 FT STRAND 291 292 FT HELIX 293 295 FT STRAND 296 297 FT HELIX 299 314 FT TURN 315 316 FT STRAND 317 318 FT HELIX 322 337 FT STRAND 339 339 FT TURN 342 343 FT STRAND 344 344 FT STRAND 346 347 FT HELIX 350 352 FT STRAND 353 353 FT STRAND 357 358 FT HELIX 361 373 FT STRAND 376 376 FT HELIX 379 392 FT STRAND 393 393 FT TURN 394 397 FT STRAND 399 402 FT STRAND 405 405 FT TURN 406 407 FT STRAND 408 408 FT STRAND 412 426 FT STRAND 430 433 FT HELIX 434 436 FT STRAND 439 443 FT TURN 444 445 FT STRAND 446 450 FT STRAND 454 458 FT STRAND 462 466 FT STRAND 468 469 FT HELIX 470 486 SQ SEQUENCE 864 AA; 97017 MW; B466E7A9D7FBF12B CRC64; MTTEKSLVTE AENSQHQQKE EGEEAINSGQ QEPQQEESCQ TAAEGDNWCE QKLKASNGDT PTHEDLTKNK ERTSESRGLS RLFSSFLKRP KSQVSEEEGK EVESDKEKGE GGQKEIEFGT SLDEEIILKA PIAAPEPELK TDPSLDLHSL SSAETQPAQE ELREDPDFEI KEGEGLEECS KIEVKEESPQ SKAETELKAS QKPIRKHRNM HCKVSLLDDT VYECVVEKHA KGQDLLKRVC EHLNLLEEDY FGLAIWDNAT SKTWLDSAKE IKKQVRGVPW NFTFNVKFYP PDPAQLTEDI TRYYLCLQLR QDIVAGRLPC SFATLALLGS YTIQSELGDY DPELHGVDYV SDFKLAPNQT KELEEKVMEL HKSYRSMTPA QADLEFLENA KKLSMYGVDL HKAKDLEGVD IILGVCSSGL LVYKDKLRIN RFPWPKVLKI SYKRSSFFIK IRPGEQEQYE STIGFKLPSY RAAKKLWKVC VEHHTFFRLT STDTIPKSKF LALGSKFRYS GRTQAQTRQA SALIDRPAPH FERTASKRAS RSLDGAAAVD SADRSPRPTS APAITQGQVA EGGVLDASAK KTVVPKAQKE TVKAEVKKED EPPEQAEPEP TEAWKVEKTH IEVTVPTSNG DQTQKLAEKT EDLIRMRKKK RERLDGENIY IRHSNLMLED LDKSQEEIKK HHASISELKK NFMESVPEPR PSEWDKRLST HSPFRTLNIN GQIPTGEGPP LVKTQTVTIS DNANAVKSEI PTKDVPIVHT ETKTITYEAA QTDDNSGDLD PGVLLTAQTI TSETPSSTTT TQITKTVKGG ISETRIEKRI VITGDADIDH DQVLVQAIKE AKEQHPDMSV TKVVVHQETE IADE // ID 41_MOUSE STANDARD; PRT; 858 AA. AC P48193; Q68FF1; Q6NVF5; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 30-MAY-2006, entry version 47. DE Protein 4.1 (Band 4.1) (P4.1) (4.1R). GN Name=Epb41; Synonyms=Epb4.1; 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 ALTERNATIVE SPLICING. RC STRAIN=BALB/c; RX MEDLINE=93155238; PubMed=8429050; RA Huang J.-P., Tang C.-J.C., Kou G.-H., Marchesi V.T., Benz E.J. Jr., RA Tang T.K.; RT "Genomic structure of the locus encoding protein 4.1. Structural basis RT for complex combinational patterns of tissue-specific alternative RNA RT splicing."; RL J. Biol. Chem. 268:3758-3766(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 [3] RP PROTEIN SEQUENCE OF 709-713, MASS SPECTROMETRY, AND CHARACTERIZATION RP OF CARBOXY-TERMINAL DOMAIN. RX MEDLINE=21325946; PubMed=11432737; RA Scott C., Phillips G.W., Baines A.J.; RT "Properties of the C-terminal domain of 4.1 proteins."; RL Eur. J. Biochem. 268:3709-3717(2001). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. Recruits CC DLG1 to membranes (By similarity). CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin and DLG1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Comment=A number of isoforms are produced; CC Name=1; CC IsoId=P48193-1; Sequence=Displayed; CC Name=2; CC IsoId=P48193-2; Sequence=VSP_012874; CC Note=No experimental confirmation available; CC -!- PTM: O-glycosylated; contains N-acetylglucosamine side chains in CC the C-terminal domain (By similarity). CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- PTM: Phosphorylation on Tyr-654 reduces the ability of 4.1 to CC promote the assembly of the spectrin/actin/4.1 ternary complex. CC -!- SIMILARITY: Contains 1 FERM 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; L00919; AAA37122.1; -; mRNA. DR EMBL; L00919; AAA37123.1; -; mRNA. DR EMBL; BC068138; AAH68138.1; -; mRNA. DR EMBL; BC079875; AAH79875.1; -; mRNA. DR PIR; A46613; A46613. DR UniGene; Mm.30038; -. DR HSSP; P11171; 1GG3. DR SMR; P48193; 211-489. DR Ensembl; ENSMUSG00000028906; Mus musculus. DR MGI; MGI:95401; Epb4.1. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; KW Direct protein sequencing; Glycoprotein; Nuclear protein; KW Phosphorylation; Structural protein. FT CHAIN 1 858 Protein 4.1. FT /FTId=PRO_0000219391. FT DOMAIN 211 492 FERM. FT REGION 495 608 Hydrophilic. FT REGION 609 707 Spectrin--actin-binding. FT REGION 710 858 Carboxyl-terminal (CTD). FT MOD_RES 62 62 Phosphothreonine (By similarity). FT MOD_RES 654 654 Phosphotyrosine (By similarity). FT MOD_RES 706 706 Phosphoserine (By similarity). FT VAR_SEQ 610 663 Missing (in isoform 2). FT /FTId=VSP_012874. FT CONFLICT 1 3 MTT -> EPLKGREPRRARTRPGPARPGPCQVPVLCSP FT (in Ref. 2). FT CONFLICT 8 8 V -> A (in Ref. 2). FT CONFLICT 232 233 NL -> KG (in Ref. 2). FT CONFLICT 443 443 S -> Y (in Ref. 2). FT CONFLICT 576 576 R -> A (in Ref. 2). SQ SEQUENCE 858 AA; 95990 MW; 5F2FEF077946134E CRC64; MTTEKSLVAE AENSQHQQQK EEGEGATNSG QQETQLEEAS QAAAAEGSDQ GEQKLKASNG DTPTHEDLTK NKERTSESRG LSRLLSSFLK RPKSQVSEEE GREVESEKEK GEGGQKEIEL GNSLDEDIIL KAPIAAPEPE LKTDPSLDLH SLSSIETQPA QEEHREDPDS ETKEGEGIEE CSGTEVKEDP ESRAEREPEA SQKPVRRHRN MHCKVSLLDD TVYECVVEKH ANLQDLLKRV CEHLNLLEED YFGLALWDSA TSKTWLDSAK EIKKQVRGVP WNFTFNVKFY PPDPAQLTED ITRYYLCLQL RQDIVAGRLP CSFATLALLG SYTIQSELGD YDPELHGMDY VSDFKLAPNQ TKELEEKVME LHKSYRSMTP AQADLEFLEN AKKLSMYGVD LHKAKDLEGV DIILGVCSSG LLVYKDKLRI NRFPWPKVLK ISSKRSSFFI KIRPGEQEHY ESTIGFKLPS YRAAKKLWKV CVEHHTFFRL TSTDTIPKSK FLALGSKFRY SGRTQAQTRQ ASALIDRPAP HFERTASKRA SRSLDGAAAA ESTDRSPRPT SAPAIAQSQV TEGPGRPIKK TPKEAVKVEE KRGEEPAEPA EPEPTEAWKV EKTHTEVTVP TSNGDQTQKL AGKGEDLIRM RKKKRERLDG ENIYIRHSNL MLEDLDKSQE EIKKHHASIS ELKKNFMESV PEPRPSEWDK RLSTHSPFRT LNINGQVPTG DGPPLVKTQT VTISDTANAV KSEIPTKDVP IVHTETKTIT YEAAQTEDSN GDLDPGVLLT AQTITSETTS STTTTQITKT VKGGISETRI EKRIVITGDA DIDHDQVLVQ AIKEAKEQHP DMSVTKVVVH QETEISEE // ID 41_XENLA STANDARD; PRT; 801 AA. AC P11434; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 04-APR-2006, entry version 55. DE Cytoskeletal protein 4.1 (Band 4.1). GN Name=epb41; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=90249600; PubMed=2186944; RA Spencer M., Giebelhaus D.H., Kelly G.M., Bicknell J., Florio S.K., RA Bunt-Milam A., Moon R.T.; RT "Membrane skeleton protein 4.1 in developing Xenopus: expression in RT postmitotic cells of the retina."; RL Dev. Biol. 139:279-291(1990). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-550. RX MEDLINE=88223353; PubMed=2453290; RA Giebelhaus D.H., Eib D.W., Moon R.T.; RT "Antisense RNA inhibits expression of membrane skeleton protein 4.1 RT during embryonic development of Xenopus."; RL Cell 53:601-615(1988). CC -!- FUNCTION: Protein 4.1 is a major structural element of the CC erythrocyte membrane skeleton. It plays a key role in regulating CC membrane physical properties of mechanical stability and CC deformability by stabilizing spectrin-actin interaction. CC -!- SUBUNIT: Binds with a high affinity to glycophorin and with lower CC affinity to band III protein. Associates with the nuclear mitotic CC apparatus. Binds calmodulin (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- TISSUE SPECIFICITY: Found exclusively in photoreceptors following CC the terminal mitosis of retinal neurons. When retinal CC synaptogenesis is complete, protein 4.1 is also expressed in the CC inner retina. In adult amphibian retinas, protein 4.1 is detected CC in photoreceptors, bipolar cells, and ganglion cell axons. CC -!- PTM: Phosphorylated at multiple sites by different protein kinases CC and each phosphorylation event selectively modulates the protein's CC functions. CC -!- SIMILARITY: Contains 1 FERM 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; M20621; AAA49695.1; -; mRNA. DR PIR; A37353; A37353. DR UniGene; Xl.691; -. DR HSSP; P11171; 1GG3. DR SMR; P11434; 193-471. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Nuclear protein; Phosphorylation; KW Structural protein. FT CHAIN 1 801 Cytoskeletal protein 4.1. FT /FTId=PRO_0000219393. FT DOMAIN 193 474 FERM. FT REGION 477 587 Hydrophilic. FT REGION 588 651 Spectrin--actin-binding. FT REGION 653 801 Carboxyl-terminal (CTD). SQ SEQUENCE 801 AA; 89429 MW; 07FA508552359A0F CRC64; MTTEKGLLAE AESPPQDQKQ EGEEEVESCT TQPVVGSGDK DPETEQSQES PSTTSPSTRK SKDRHSQGKG LSRLFSSFLK RPKSQVSSDE KEVELLGEKG QDQKDVDEGL GEQLEDDVFL KAPIAAPEPE LRTDPSLDLH SLSSAETQPA QEEQKEDQDP EADCEDVEGK EPIKKPEGES KASHKVVRRS PNMRCKVTLL DDTVYECDLE KHAKGQDIFK KVCSHLNIVE EDYFGLAIWE SPTCKVWLDP LKDIRKQVHG GPCEFTSNVK FYPPDPAQLS EDITRYYLCL QLRKDIFSGR LPCSFATLAL LGSYTVQSEV GDYEEDLHGV DYVSEFKLSP NQTKDLEEKV GELHKSYRSM TPAQADLEFL ENAKKLTMYG VDIHQAKDLE GVDIKLGVCS GGLMVFKDNL RINRFPWPKV LKISYKRSSF FIKIRPGEQE QYESTIGFKL PSYKAAKKLW KVCVEHHTFF RLTSTESIPK HRFLSLGSTF RYSGRTQAQT RHASALIDRP APHFVRTGSK RASRSLDGAA VATPEASRTH RPVSAPVFPP EFPAVQRKTP GPRVEEMPKK TEEKPKEGMP NQRESPKDVK ATQQDSPSPT VNGDKVKDLE KTQDEIIRHH ASIRELKKSF MESVPAPRPS EWDKRLSTHS PFRTLSFNGQ VQTGTDGPPL VKTQTVTISN ATNGEKGEIP TKEVPLVHTE TKTITYEAAR SDDVNTDQEP GILLTAHTIT SETTSSTTTT QITKTVKGGI SETLIEKRIV ITGDGDLDHD QVLVQAIKEA KEQHPDMSVT KGVVHQETEI A // ID E41L1_HUMAN STANDARD; PRT; 881 AA. AC Q9H4G0; O15046; Q4VXN4; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2001, sequence version 2. DT 30-MAY-2006, entry version 45. DE Band 4.1-like protein 1 (Neuronal protein 4.1) (4.1N). GN Name=EPB41L1; Synonyms=KIAA0338; 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]. RC TISSUE=Brain; RX MEDLINE=97349984; PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., RA Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., RA Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [3] RP INTERACTION WITH CENTG1. RX MEDLINE=20578809; PubMed=11136977; DOI=10.1016/S0092-8674(00)00195-1; RA Ye K., Hurt K.J., Wu F.Y., Fang M., Luo H.R., Hong J.J., Blackshaw S., RA Ferris C.D., Snyder S.H.; RT "PIKE: A nuclear GTPase that enhances PI3kinase activity and is RT regulated by protein 4.1N."; RL Cell 103:919-930(2000). CC -!- FUNCTION: May function to confer stability and plasticity to CC neuronal membrane via multiple interactions, including the CC spectrin-actin-based cytoskeleton, integral membrane channels and CC membrane-associated guanylate kinases. CC -!- SUBUNIT: Interacts with CENTG1. CC -!- TISSUE SPECIFICITY: Highest expression in brain, lower in heart, CC kidney, pancreas, placenta, lung and skeletal muscle. CC -!- SIMILARITY: Contains 1 FERM 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; AB002336; BAA20796.1; ALT_INIT; mRNA. DR EMBL; AL121895; CAI95018.1; -; Genomic_DNA. DR UniGene; Hs.437422; -. DR HSSP; P11171; 1GG3. DR SMR; Q9H4G0; 99-375. DR Ensembl; ENSG00000088367; Homo sapiens. DR H-InvDB; HIX0015775; -. DR HGNC; HGNC:3378; EPB41L1. DR MIM; 602879; gene. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Phosphorylation; Structural protein. FT CHAIN 1 881 Band 4.1-like protein 1. FT /FTId=PRO_0000219395. FT DOMAIN 97 378 FERM. FT REGION 483 541 Spectrin--actin-binding. FT REGION 746 881 Carboxyl-terminal (CTD). FT MOD_RES 466 466 Phosphoserine (By similarity). FT MOD_RES 475 475 Phosphothreonine (By similarity). FT MOD_RES 546 546 Phosphoserine (By similarity). FT MOD_RES 550 550 Phosphothreonine (By similarity). FT MOD_RES 648 648 Phosphoserine (By similarity). FT MOD_RES 650 650 Phosphoserine (By similarity). FT MOD_RES 686 686 Phosphothreonine (By similarity). SQ SEQUENCE 881 AA; 98503 MW; D923CF554EDB41D3 CRC64; MTTETGPDSE VKKAQEEAPQ QPEAAAAVTT PVTPAGHGHP EANSNEKHPS QQDTRPAEQS LDMEEKDYSE ADGLSERTTP SKAQKSPQKI AKKYKSAICR VTLLDASEYE CEVEKHGRGQ VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKRDEDGE SGGQRSEAEE GEVRTPTKIK ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWERERRLPS SPASPSPKGT PEKANERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD TVFLKDNHLA IERKCSSITV SSTSSLEAEV DFTVIGDYHG SAFEDFSRSL PELDRDKSDS DTEGLLFSRD LNKGAPSQDD ESGGIEDSPD RGACSTPDMP QFEPVKTETM TVSSLAIRKK IEPEAVLQTR VSAMDNTQQV DGSASVGREF IATTPSITTE TISTTMENSL KSGKGAAAMI PGPQTVATEI RSLSPIIGKD VLTSTYGATA ETLSTSTTTH VTKTVKGGFS ETRIEKRIII TGDEDVDQDQ ALALAIKEAK LQHPDMLVTK AVVYRETDPS PEERDKKPQE S // ID E41L1_MOUSE STANDARD; PRT; 879 AA. AC Q9Z2H5; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 30-MAY-2006, entry version 44. DE Band 4.1-like protein 1 (Neuronal protein 4.1) (4.1N). GN Name=Epb41l1; Synonyms=Epb4, Epb4.1l1; 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]. RC TISSUE=Brain; RX MEDLINE=99343811; PubMed=10414974; RA Walensky L.D., Blackshaw S., Liao D., Watkins C.C., Weier H.-U.G., RA Parra M., Huganir R.L., Conboy J.G., Mohandas N., Snyder S.H.; RT "A novel neuron-enriched homolog of the erythrocyte membrane RT cytoskeletal protein 4.1."; RL J. Neurosci. 19:6457-6467(1999). RN [2] RP PHOSPHORYLATION AT THR-685, AND MASS SPECTROMETRY. RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [3] RP PHOSPHORYLATION AT SER-466; THR-475; SER-546; THR-550; SER-648 AND RP SER-650. RX PubMed=15572359; DOI=10.1074/jbc.M411220200; RA Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., RA Blackstock W.P., Choudhary J.S., Grant S.G.; RT "Proteomic analysis of in vivo phosphorylated synaptic proteins."; RL J. Biol. Chem. 280:5972-5982(2005). RN [4] RP PHOSPHORYLATION AT SER-546; THR-550 AND SER-648, AND MASS RP SPECTROMETRY. RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: May function to confer stability and plasticity to CC neuronal membrane via multiple interactions, including the CC spectrin-actin-based cytoskeleton, integral membrane channels and CC membrane-associated guanylate kinases. CC -!- SUBUNIT: Interacts with CENTG1 (By similarity). CC -!- TISSUE SPECIFICITY: Highest expression in brain, also present in CC kidney, olfactory epithelium, retina, sensory ganglia, CC gastrointestinal tract (only enteric neurons) and lung. CC -!- SIMILARITY: Contains 1 FERM 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; AF061283; AAC68583.1; -; mRNA. DR UniGene; Mm.20852; -. DR HSSP; P11171; 1GG3. DR SMR; Q9Z2H5; 99-375. DR IntAct; Q9Z2H5; -. DR Ensembl; ENSMUSG00000027624; Mus musculus. DR MGI; MGI:103010; Epb4.1l1. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Phosphorylation; Structural protein. FT CHAIN 1 879 Band 4.1-like protein 1. FT /FTId=PRO_0000219396. FT DOMAIN 97 378 FERM. FT REGION 381 482 Hydrophilic. FT REGION 483 541 Spectrin--actin-binding. FT REGION 743 879 Carboxyl-terminal (CTD). FT MOD_RES 466 466 Phosphoserine. FT MOD_RES 475 475 Phosphothreonine. FT MOD_RES 546 546 Phosphoserine. FT MOD_RES 550 550 Phosphothreonine. FT MOD_RES 648 648 Phosphoserine. FT MOD_RES 650 650 Phosphoserine. FT MOD_RES 685 685 Phosphothreonine. SQ SEQUENCE 879 AA; 98315 MW; 2EB501A4B4DCA325 CRC64; MTTETGPDSE VKKAQEETPQ QPEAAAAVTT PVTPAGHSHP ETNSNEKHLT QQDTRPAEQS LDMDDKDYSE ADGLSERTTP SKAQKSPQKI AKKFKSAICR VTLLDASEYE CEVEKHGRGQ VLFDLVCEHL NLLEKDYFGL TYCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDAE EHVGNYVSEL RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS SSKRYTMSRS LDGAEFSRPA SVSENHDAGP DGDKREDDAE SGGRRSEAEE GEVRTPTKIK ELKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWDRERRLPS SPASPSPKGT PEKASERAGL REGSEEKVKP PRPRAPESDT GDEDQDQERD AVFLKDNHLA IERKCSSITV SSTSSLEAEV DFTVIGDYHG GAFEDFSRSL PELDRDKSDS ETEGLVFARD LKGPSSQEDE SGGLEDSPDR GACSTPEMPQ FESVKAETMT VSSLAIRKKI EPEAMLQSRV SAADSTQVDG GTPMVKDFMT TPPCITTETI STTMENSLKS GKGAAAMIPG PQTVATEIRS LSPIIGKDVL TSTYGATAET LSTSTTTHVT KTVKGGFSET RIEKRIIITG DEDVDQDQAL ALAIKEAKLQ HPDMLVTKAV VYRETDPSPE ERDKKPQES // ID E41L2_HUMAN STANDARD; PRT; 1005 AA. AC O43491; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 16-MAY-2006, entry version 46. DE Band 4.1-like protein 2 (Generally expressed protein 4.1) (4.1G). GN Name=EPB41L2; 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=Brain, and Heart; RX MEDLINE=98260680; PubMed=9598318; DOI=10.1006/geno.1998.5265; RA Parra M., Gascard P., Walensky L.D., Snyder S.H., Mohandas N., RA Conboy J.G.; RT "Cloning and characterization of 4.1G (EPB41L2), a new member of the RT skeletal protein 4.1 (EPB41) gene family."; RL Genomics 49:298-306(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Liu J., Zhou Y., Zhang B., Peng X., Yuan J., Qiang B.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP PHOSPHORYLATION AT SER-39; SER-499 AND SER-550. RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). CC -!- SUBUNIT: The CTD domain interacts with FKBP2 (By similarity). CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Contains 1 FERM 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; AF027299; AAC16923.1; -; mRNA. DR EMBL; AY047584; AAK95850.1; -; mRNA. DR UniGene; Hs.486470; -. DR HSSP; P11171; 1GG3. DR SMR; O43491; 218-496. DR Ensembl; ENSG00000079819; Homo sapiens. DR HGNC; HGNC:3379; EPB41L2. DR MIM; 603237; gene. DR GO; GO:0005886; C:plasma membrane; TAS. DR GO; GO:0008091; C:spectrin; TAS. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Phosphorylation; Polymorphism; KW Structural protein. FT CHAIN 1 1005 Band 4.1-like protein 2. FT /FTId=PRO_0000219397. FT DOMAIN 218 499 FERM. FT REGION 502 610 Hydrophilic. FT REGION 611 676 Spectrin--actin-binding. FT REGION 855 1005 Carboxyl-terminal (CTD). FT MOD_RES 39 39 Phosphoserine. FT MOD_RES 499 499 Phosphoserine. FT MOD_RES 550 550 Phosphoserine. FT VARIANT 17 17 Q -> H (in dbSNP:2297852). FT /FTId=VAR_020145. SQ SEQUENCE 1005 AA; 112588 MW; E86CB17488F6045F CRC64; MTTEVGSVSE VKKDSSQLGT DATKEKPKEV AENQQNQSSD PEEEKGSQPP PAAESQSSLR RQKREKETSE SRGISRFIPP WLKKQKSYTL VVAKDGGDKK EPTQAVVEEQ VLDKEEPLPE EQRQAKGDAE EMAQKKQEIK VEVKEEKPSV SKEEKPSVSK VEMQPTELVS KEREEKVKET QEDKLEGGAA KRETKEVQTN ELKAEKASQK VTKKTKTVQC KVTLLDGTEY SCDLEKHAKG QVLFDKVCEH LNLLEKDYFG LLFQESPEQK NWLDPAKEIK RQLRNLPWLF TFNVKFYPPD PSQLTEDITR YFLCLQLRQD IASGRLPCSF VTHALLGSYT LQAELGDYDP EEHGSIDLSE FQFAPTQTKE LEEKVAELHK THRGLSPAQA DSQFLENAKR LSMYGVDLHH AKDSEGVDIK LGVCANGLLI YKDRLRINRF AWPKILKISY KRSNFYIKVR PAELEQFEST IGFKLPNHRA AKRLWKVCVE HHTFYRLVSP EQPPKAKFLT LGSKFRYSGR TQAQTRQAST LIDRPAPHFE RTSSKRVSRS LDGAPIGVMD QSLMKDFPGA AGEISAYGPG LVSIAVVQDG DGRREVRSPT KAPHLQLIEG KKNSLRVEGD NIYVRHSNLM LEELDKAQED ILKHQASISE LKRNFMESTP EPRPNEWEKR RITPLSLQTQ GSSHETLNIV EEKKRAEVGK DERVITEEMN GKEISPGSGP GEIRKVEPVT QKDSTSLSSE SSSSSSESEE EDVGEYRPHH RVTEGTIREE QEYEEEVEEE PRPAAKVVER EEAVPEASPV TQAGASVITV ETVIQENVGA QKIPGEKSVH EGALKQDMGE EAEEEPQKVN GEVSHVDIDV LPQIICCSEP PVVKTEMVTI SDASQRTEIS TKEVPIVQTE TKTITYESPQ IDGGAGGDSG TLLTAQTITS ESVSTTTTTH ITKTVKGGIS ETRIEKRIVI TGDGDIDHDQ ALAQAIREAR EQHPDMSVTR VVVHKETELA EEGED // ID E41L2_MOUSE STANDARD; PRT; 988 AA. AC O70318; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 30-MAY-2006, entry version 46. DE Band 4.1-like protein 2 (Generally expressed protein 4.1) (4.1G). GN Name=Epb41l2; Synonyms=Epb4.1l2; 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], AND INTERACTION WITH FKBP2. RC TISSUE=Brain; RX MEDLINE=98198473; PubMed=9531554; DOI=10.1083/jcb.141.1.143; RA Walensky L.D., Gascard P., Fields M.E., Blackshaw S., Conboy J.G., RA Mohandas N., Snyder S.H.; RT "The 13-kD FK506 binding protein, FKBP13, interacts with a novel RT homologue of the erythrocyte membrane cytoskeletal protein 4.1."; RL J. Cell Biol. 141:143-153(1998). RN [2] RP PHOSPHORYLATION AT SER-38, AND MASS SPECTROMETRY. RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- SUBUNIT: The CTD domain interacts with FKBP2. CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Contains 1 FERM 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; AF044312; AAC40083.1; -; mRNA. DR UniGene; Mm.306026; -. DR HSSP; P11171; 1GG3. DR SMR; O70318; 214-489. DR IntAct; O70318; -. DR Ensembl; ENSMUSG00000019978; Mus musculus. DR MGI; MGI:103009; Epb4.1l2. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Cytoskeleton; Phosphorylation; Structural protein. FT CHAIN 1 988 Band 4.1-like protein 2. FT /FTId=PRO_0000219398. FT DOMAIN 211 492 FERM. FT REGION 495 651 Hydrophilic. FT REGION 652 837 Spectrin--actin-binding. FT REGION 838 988 Carboxyl-terminal (CTD). FT MOD_RES 38 38 Phosphoserine. FT MOD_RES 492 492 Phosphoserine (By similarity). FT MOD_RES 543 543 Phosphoserine (By similarity). SQ SEQUENCE 988 AA; 109833 MW; B0367A16C5A2EC05 CRC64; MTTEVGSASE VKKGSDQAGA DASKEKAKEV ENEQTPVSEP EEEKGSQPGP PVERQSTPRL RKRGKDPSEN RGISRFIPPW LKKQRSYNLV VAKDGGDKKE PTQADVEDQI LGKEESLPEE ESRAKGDAEE MAQRKHLEVQ VEVREAKPAL KSSVETQPAE EVRKDKEETI QDTQEEKLEG GAAKRETKEV QTSELKAEVA SQKATKKTKT VLAKVTLLDG TEYSCDLEKR AKGQVLFDRV CEHLNLLEKD YFGLLFQDHP EQKNWLDPAK EIKRQLKNLP WLFTFNVKFY PPDPSQLTED ITRYFLCLQL RQDIASGRLP CSFVTHALLG SYTLQAEHGD YDPEEYDSID LGDFQFAPAH TKELEEKVSE LHKTHRGLSP AQADSQFLEN AKRLSMYGVD LHHAKDSEGV DIKLGVCANG LLIYKDRLRI NRFAWPKILK ISYKRSNFYI KVRPAELEQF ESTIGFKLPN HRAAKRLWKV CVEHHTFYRL VSPEQPPKTK FLTLGSKFRY SGRTQAQTRE ASTLIDRPAP QFERASSKRV SRSLDGAPIG VVDQSPPGEG SVPGPGVISY TTIQDGRRDS KSPTKATPLP AEGKKNTLRV DGDNIYVRHS NLMLEDLDKA QEAILKHQAS ISELKRNFMA STPEPRPSEW EKRRVTPLPL QPQASSHETL NVVEEKKRAG VGKDESVITE EMNGKEMSPG HGPGETRKVE PVAHKDSTSL SSESSSSSSE SEEDVGEYQP HHRVTEGTIR EEQEECDEEL EEEPGQGAKV VEREAAVPDA VPDRQAGASV LPVETEAQEH VVAQKLPGEK GAHGGTAEQD PREEAEEDPH RVNGEVPHLD LDGLPEIICC SEPPVVKTEM VTISDASQRT EISTKEVPIV QTETKTITYE SPQIDGGAGG DSGVLLTAQT ITSESASTTT TTHITKTVKG GISETRIEKR IVITGDAALD HDQALAQAIR EAREQHPDMS VTRVVVHKET ELAEEGEE // ID E41L3_HUMAN STANDARD; PRT; 1087 AA. AC Q9Y2J2; O95713; Q9BRP5; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 30-MAY-2006, entry version 48. DE Band 4.1-like protein 3 (4.1B) (Differentially expressed in DE adenocarcinoma of the lung protein 1) (DAL-1). GN Name=EPB41L3; Synonyms=DAL1, KIAA0987; 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 A). RC TISSUE=Brain; RX MEDLINE=99246063; PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C). RC TISSUE=Lung; RX MEDLINE=99107198; PubMed=9892180; RA Tran Y.K., Boegler O., Gorse K.M., Wieland I., Green M.R., RA Newsham I.F.; RT "A novel member of the NF2/ERM/4.1 superfamily with growth suppressing RT properties in lung cancer."; RL Cancer Res. 59:35-43(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B). RC TISSUE=Lung; 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: Critical growth regulator in the pathogenesis of CC meningiomas. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist; CC Name=A; CC IsoId=Q9Y2J2-1; Sequence=Displayed; CC Name=B; CC IsoId=Q9Y2J2-2; Sequence=VSP_000482, VSP_000483, VSP_000484, CC VSP_000485; CC Name=C; CC IsoId=Q9Y2J2-3; Sequence=VSP_000482, VSP_000483, VSP_000484, CC VSP_000485, VSP_000486; CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain, with lower CC levels in kidney, intestine, and testis. CC -!- SIMILARITY: Contains 1 FERM domain. CC -!- CAUTION: Ref.2 sequence differs from that shown due to frameshifts CC in positions 29 and 59. 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; AB023204; BAA76831.1; ALT_INIT; mRNA. DR EMBL; AF069072; AAC79806.1; ALT_FRAME; mRNA. DR EMBL; BC006141; AAH06141.1; -; mRNA. DR UniGene; Hs.213394; -. DR HSSP; P11171; 1GG3. DR SMR; Q9Y2J2; 110-388. DR Ensembl; ENSG00000082397; Homo sapiens. DR HGNC; HGNC:3380; EPB41L3. DR MIM; 605331; gene. DR LinkHub; Q9Y2J2; -. DR GO; GO:0005886; C:plasma membrane; NAS. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; Phosphorylation; KW Structural protein. FT CHAIN 1 1087 Band 4.1-like protein 3. FT /FTId=PRO_0000219399. FT DOMAIN 110 391 FERM. FT REGION 394 513 Hydrophilic. FT REGION 514 860 Spectrin--actin-binding (Potential). FT REGION 861 1083 Carboxyl-terminal (CTD). FT MOD_RES 88 88 Phosphoserine (By similarity). FT MOD_RES 460 460 Phosphoserine (By similarity). FT MOD_RES 469 469 Phosphothreonine (By similarity). FT MOD_RES 704 704 Phosphothreonine (By similarity). FT MOD_RES 708 708 Phosphoserine (By similarity). FT MOD_RES 784 784 Phosphothreonine (By similarity). FT MOD_RES 787 787 Phosphoserine (By similarity). FT MOD_RES 788 788 Phosphoserine (By similarity). FT MOD_RES 962 962 Phosphoserine (By similarity). FT MOD_RES 1081 1081 Phosphothreonine (By similarity). FT VAR_SEQ 446 446 G -> GASVNENHEIYMKDSMSAA (in isoform B FT and isoform C). FT /FTId=VSP_000482. FT VAR_SEQ 503 689 Missing (in isoform B and isoform C). FT /FTId=VSP_000483. FT VAR_SEQ 708 719 Missing (in isoform B and isoform C). FT /FTId=VSP_000484. FT VAR_SEQ 784 824 Missing (in isoform B and isoform C). FT /FTId=VSP_000485. FT VAR_SEQ 835 1087 Missing (in isoform C). FT /FTId=VSP_000486. FT CONFLICT 32 32 Missing (in Ref. 2). FT CONFLICT 498 498 R -> Q (in Ref. 2). SQ SEQUENCE 1087 AA; 120678 MW; 0A33CA4A43F12620 CRC64; MTTESGSDSE SKPDQEAEPQ EAAGAQGRAG APVPEPPKEE QQQALEQFAA AAAHSTPVRR EVTDKEQEFA ARAAKQLEYQ QLEDDKLSQK SSSSKLSRSP LKIVKKPKSM QCKVILLDGS EYTCDVEKRS RGQVLFDKVC EHLNLLEKDY FGLTYRDAEN QKNWLDPAKE IKKQVRSGAW HFSFNVKFYP PDPAQLSEDI TRYYLCLQLR DDIVSGRLPC SFVTLALLGS YTVQSELGDY DPDECGSDYI SEFRFAPNHT KELEDKVIEL HKSHRGMTPA EAEMHFLENA KKLSMYGVDL HHAKDSEGVE IMLGVCASGL LIYRDRLRIN RFAWPKVLKI SYKRNNFYIK IRPGEFEQFE STIGFKLPNH RAAKRLWKVC VEHHTFFRLL LPEAPPKKFL TLGSKFRYSG RTQAQTRRAS ALIDRPAPYF ERSSSKRYTM SRSLDGEVGT GQYATTKGIS QTNLITTVTP EKKAEEERDE EEDKRRKGEE VTPISAIRHE GKSPGLGTDS CPLSPPSTHC APTSPTELRR RCKENDCKLP GYEPSRAEHL PGEPALDSDG PGRPYLGDQD VAFSYRQQTG KGTTLFSFSL QLPESFPSLL DDDGYLSFPN LSETNLLPQS LQHYLPIRSP SLVPCFLFIF FFLLSASFSV PYALTLSFPL ALCLCYLEPK AASLSASLDN DPSDSSEEET DSERTDTAAD GETTATESDQ EEDAELKAQE LEKTQDDLMK HQTNISELKR TFLETSTDTA VTNEWEKRLS TSPVRLAARQ EDAPMIEPLV PEETKQSSGE KLMDGSEIFS LLESARKPTE FIGGVTSTSQ SWVQKMETKT ESSGIETEPT VHHLPLSTEK VVQETVLVEE RRVVHASGDA SYSAGDSGDA AAQPAFTGIK GKEGSALTEG AKEEGGEEVA KAVLEQEETA AASRERQEEQ SAAIHISETL EQKPHFESST VKTETISFGS VSPGGVKLEI STKEVPVVHT ETKTITYESS QVDPGTDLEP GVLMSAQTIT SETTSTTTTT HITKTVKGGI SETRIEKRIV ITGDADIDHD QALAQAIKEA KEQHPDMSVT KVVVHKETEI TPEDGED // ID E41L3_MOUSE STANDARD; PRT; 929 AA. AC Q9WV92; Q9R102; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 30-MAY-2006, entry version 49. DE Band 4.1-like protein 3 (4.1B) (Differentially expressed in DE adenocarcinoma of the lung protein 1) (DAL-1) (DAL1P) (mDAL-1). GN Name=Epb41l3; Synonyms=Dal1, Epb4.1l3; 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; 3; 4; 5 AND 6). RC TISSUE=Brain; RX MEDLINE=20119278; PubMed=10652311; DOI=10.1074/jbc.275.5.3247; RA Parra M., Gascard P., Walensky L.D., Gimm J.A., Blackshaw S., Chan N., RA Takakuwa Y., Berger T., Lee G., Chasis J.A., Snyder S.H., Mohandas N., RA Conboy J.G.; RT "Molecular and functional characterization of protein 4.1B, a novel RT member of the protein 4.1 family with high level, focal expression in RT brain."; RL J. Biol. Chem. 275:3247-3255(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-929 (ISOFORM 7). RC STRAIN=BALB/c; TISSUE=Brain; RA Azam M., Andrabi S., Lin L., Newsham I., Chishti A.H.; RT "Mouse DAL-1 (mDAL-1) cDNA Sequence."; RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 719-929 (ISOFORMS 4/5/6/7). RA Marra M., Hillier L., Kucaba T., Martin J., Beck C., Wylie T., RA Underwood K., Steptoe M., Theising B., Allen M., Bowers Y., Person B., RA Swaller T., Gibbons M., Pape D., Harvey N., Schurk R., Ritter E., RA Kohn S., Shin T., Jackson Y., Cardenas M., McCann R., Waterston R., RA Wilson R.; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP PHOSPHORYLATION AT SER-470; SER-486; THR-495; SER-543; SER-547 AND RP SER-804, AND MASS SPECTROMETRY. RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [5] RP PHOSPHORYLATION AT SER-96; SER-486; THR-495; SER-543; SER-547; RP THR-623; SER-626 AND SER-627. RX PubMed=15572359; DOI=10.1074/jbc.M411220200; RA Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., RA Blackstock W.P., Choudhary J.S., Grant S.G.; RT "Proteomic analysis of in vivo phosphorylated synaptic proteins."; RL J. Biol. Chem. 280:5972-5982(2005). RN [6] RP PHOSPHORYLATION AT SER-96 AND THR-923, AND MASS SPECTROMETRY. RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). CC -!- FUNCTION: Isoform 2 (heart-specific) has the complete spectrin-- CC actin-binding (SAB) domain and fully interacts with spectrin and CC actin. CC -!- SUBCELLULAR LOCATION: Membrane; peripheral membrane protein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Experimental confirmation may be lacking for some CC isoforms; CC Name=1; Synonyms=4.1B-brain; CC IsoId=Q9WV92-1; Sequence=Displayed; CC Name=2; Synonyms=4.1B-heart; CC IsoId=Q9WV92-2; Sequence=VSP_000490, VSP_000489; CC Name=3; Synonyms=4.1B-kidney; CC IsoId=Q9WV92-3; Sequence=VSP_000490; CC Name=4; Synonyms=4.1b-brain; CC IsoId=Q9WV92-4; Sequence=VSP_000491; CC Name=5; Synonyms=4.1B-heart; CC IsoId=Q9WV92-5; Sequence=VSP_000490, VSP_000489, VSP_000491; CC Name=6; Synonyms=4.1B-kidney; CC IsoId=Q9WV92-6; Sequence=VSP_000490, VSP_000491; CC Name=7; CC IsoId=Q9WV92-7; Sequence=VSP_000487, VSP_000490, VSP_000488, CC VSP_000491; CC Note=Inferred from the cDNA sequence of Ref.2; CC -!- TISSUE SPECIFICITY: Highest expression in brain, lower in testis, CC adrenal gland, heart and kidney. Also present in muscle and CC epithelial cells. Isoform 1 is expressed in brain, isoform 2 is CC expressed in heart and isoform 3 is mostly expressed in kidney but CC also in heart and brain. Isoform 6 seems to be most abundant in CC kidney while isoform 4 and isoform 5 are predominantly expressed CC in heart and brain. CC -!- MISCELLANEOUS: The complete SAB domain is present only in the CC heart-specific isoforms (isoform 2 and isoform 5). CC -!- SIMILARITY: Contains 1 FERM 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; AF152247; AAD38048.1; -; mRNA. DR EMBL; AF177146; AAD51365.1; ALT_INIT; mRNA. DR UniGene; Mm.131135; -. DR HSSP; P11171; 1GG3. DR SMR; Q9WV92; 118-396. DR Ensembl; ENSMUSG00000024044; Mus musculus. DR MGI; MGI:103008; Epb4.1l3. DR InterPro; IPR008379; 4_1_CTD. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR InterPro; IPR007477; SAB. DR Pfam; PF05902; 4_1_CTD; 1. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF04382; SAB; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Actin-binding; Alternative splicing; Cytoskeleton; Membrane; KW Phosphorylation; Structural protein. FT CHAIN 1 929 Band 4.1-like protein 3. FT /FTId=PRO_0000219400. FT DOMAIN 118 399 FERM. FT REGION 402 528 Hydrophilic. FT REGION 559 602 Spectrin--actin-binding. FT REGION 777 929 Carboxyl-terminal (CTD). FT MOD_RES 96 96 Phosphoserine. FT MOD_RES 470 470 Phosphoserine. FT MOD_RES 486 486 Phosphoserine. FT MOD_RES 495 495 Phosphothreonine. FT MOD_RES 543 543 Phosphoserine. FT MOD_RES 547 547 Phosphoserine. FT MOD_RES 623 623 Phosphothreonine. FT MOD_RES 626 626 Phosphoserine. FT MOD_RES 627 627 Phosphoserine. FT MOD_RES 804 804 Phosphoserine. FT MOD_RES 923 923 Phosphothreonine. FT VAR_SEQ 455 472 Missing (in isoform 7). FT /FTId=VSP_000487. FT VAR_SEQ 547 558 Missing (in isoform 2, isoform 3, isoform FT 5, isoform 6 and isoform 7). FT /FTId=VSP_000490. FT VAR_SEQ 559 559 D -> NSLIKRIKGENVYVKHSNLMLED (in isoform FT 2 and isoform 5). FT /FTId=VSP_000489. FT VAR_SEQ 623 663 Missing (in isoform 7). FT /FTId=VSP_000488. FT VAR_SEQ 894 929 ALAQAIKEAKEQHPDMSVTKVVVHKETEITPEDGED -> E FT (in isoform 4, isoform 5, isoform 6 and FT isoform 7). FT /FTId=VSP_000491. FT CONFLICT 6 10 GSDSE -> RIRLR (in Ref. 2). FT CONFLICT 28 28 Q -> R (in Ref. 2). FT CONFLICT 288 288 A -> V (in Ref. 2). FT CONFLICT 306 306 V -> G (in Ref. 2). SQ SEQUENCE 929 AA; 103338 MW; F4975FF405DA44AE CRC64; MTTESGSDSE SKPDQEAEPQ EAAGPQGQAG AQPGPEPAGG NGSLNGEKQQ PALEQFPEAA AHSTPVKREI GDKDRDFAAA AAKQLEYQQF EDDKLSQRSS SSKLSRSPLK IVKRPKSMQC KVTLLDGSEY GCDVDKRSRG QVLFDKVCEH LNLLEKDYFG LTYRDAENQK NWLDPAKEIK KQIRSGAWHF SFNVKFYPPD PAQLSEDITR YYLCLQLRDD IVSGRLPCSF VTLALLGSYT VQSELGDYDP DECGNDYISE FRFAPNHTKE LEDKVIELHK SHRGMTPAEA EMHFLENAKK LSMYGVDLHH AKDSEGVEIM LGVCASGLLI YRDRLRINRF AWPKVLKISY KRNNFYIKIR PGEFEQFEST IGFKLPNHRA AKRLWKVCVE HHTFFRLLLP EAPPKKFLTL GSKFRYSGRT QAQTRRASAL IDRPAPYFER SSSKRYTMSR SLDGASVSEN HEIYMKDSVS AAEVGTGQYA TTKGISQTNL ITTVTPEKKA EEERVEEEDR RKKAEEATPV TALRHEGKTD SERTDTAADG ETSATESDQE EDAEIKAQDL DKTQDELMKH QTNISELKRT FLETSTETAL TNEWEKRLST SPVRLAARQE DAPMIEPLVP EETKQSSGEK LMDGSEILSL LESARKPTEF IGGVSSTTQS WVQKLETKTE PVEAEVESTP HPQPLSTEKV LQETILVEER HVMSVHASGD ASHTARDEVD AAESTPTDRR HTGKGKEGSS VTEAAKEQRG EEVDQSAPEQ EQPATVSHEE EQASTIRTSE GLEQKSHFES STVRVESTSV GSISPGGAKL EISTKEVPVV HTETKTITYE SSQVDPGADL EPGVLMSAQT ITSETTSTTT TTHITKTVKG GISETRIEKR IVITGDADID HDQALAQAIK EAKEQHPDMS VTKVVVHKET EITPEDGED // ID E41L4_BRARE STANDARD; PRT; 619 AA. AC O57457; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 04-APR-2006, entry version 35. DE Band 4.1-like protein 4 (Nbl4 protein). GN Name=epb4.1l4; Synonyms=epb41l4, nbl4; OS Brachydanio rerio (Zebrafish) (Danio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Cyprinidae; Danio. OX NCBI_TaxID=7955; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=98212541; PubMed=9551184; DOI=10.1139/bcb-75-5-623; RA Kelly G.M., Reversade B.; RT "Characterization of a cDNA encoding a novel band 4.1-like protein in RT zebrafish."; RL Biochem. Cell Biol. 75:623-632(1997). CC -!- FUNCTION: Not known, binds calmodulin. CC -!- TISSUE SPECIFICITY: In adults, it is found in the ovary, eye, CC heart and brain, but not in gut or skeletal muscle. CC -!- SIMILARITY: Contains 1 FERM 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; AF025306; AAB97965.1; -; mRNA. DR UniGene; Dr.577; -. DR HSSP; P11171; 1GG3. DR ZFIN; ZDB-GENE-990415-20; epb4.1l4. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Calmodulin-binding; Cytoskeleton; Structural protein. FT CHAIN 1 619 Band 4.1-like protein 4. FT /FTId=PRO_0000219403. FT DOMAIN 11 299 FERM. SQ SEQUENCE 619 AA; 70709 MW; 0DFD7324DE513663 CRC64; MSCFCSVQEE FYCEVLLLDE SKLILTTQQQ GIKKSTRGSV VLDYVFSHVN LAETEYFGVR YCDRSHQTFW LDPSKTLAEH KDLIATGPPY TLYFGVKFYA EDPGKLKEEI TRYQFFLQVK QDVLQGRLPC AFNISAQLAA LAIQSELGDY DPYKHTAGYV SEYRFVPDQK EDLEDSIEQI HKTLLGQVPA EAENNYLAIA KTLEMYGVDL HPVFGEKQAE YFLGLTPVGV VVYKNKTQVG KYFWPRITKV YFKETQFELR VLGRDCNETS FFFDAASKTA CKNLWKCCVE HHTFFRMPEN ESNSLTRKLS KFSSLGSKHR YSGKTAMQIG RESTETLPRA DLQVIRTRSK TYPKRSTQPA GRNNGGQAVT KMENTSEGQP KTSALTPVKS PRVKAESASV QQEKPSAPWE EDAPQSGLYN SASERNKSPK FPKAHRRSPS GGSENEPRHR RGQTADDAQA NKQHRRRSRS RGNTSSGSES ENSNREHRKK RNRSRQSNEM VDSAPQWEVV LRRQKEKTPN DPNQRRSRHR SRSRSPDVQA KEQLWKHIQK ELVDPSGLSE EQLKEIPYKK VETQGDPIKI RHSHSPRSFG STGAPTARTE RGLCCPKSTL ALIWFLLWL // ID E41L5_HUMAN STANDARD; PRT; 732 AA. AC Q9HCM4; Q9H975; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2001, sequence version 2. DT 18-APR-2006, entry version 31. DE Band 4.1-like protein 5. GN Name=EPB41L5; Synonyms=KIAA1548; 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]. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 188-732. RC TISSUE=Brain; RX MEDLINE=20450683; PubMed=10997877; DOI=10.1093/dnares/7.4.271; RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. RT XVIII. The complete sequences of 100 new cDNA clones from brain which RT code for large proteins in vitro."; RL DNA Res. 7:273-281(2000). CC -!- SIMILARITY: Contains 1 FERM 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; AK023019; BAB14360.1; -; mRNA. DR EMBL; AB046768; BAB13374.1; -; mRNA. DR UniGene; Hs.369232; -. DR HSSP; P11171; 1GG3. DR Ensembl; ENSG00000115109; Homo sapiens. DR HGNC; HGNC:19819; EPB41L5. DR LinkHub; Q9HCM4; -. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Cytoskeleton. FT CHAIN 1 732 Band 4.1-like protein 5. FT /FTId=PRO_0000219406. FT DOMAIN 43 327 FERM. FT CONFLICT 669 732 SGAMSNGLAGCEMLLTGKEGHGNKDGISLISPPAPFLVDAV FT TSSGPILAEEAVLKQKCLLTTEL -> LWSHFGRRSCPEAE FT VFTDH (in Ref. 1). SQ SEQUENCE 732 AA; 81758 MW; 76D5BD8CE099E761 CRC64; MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV KFYSSEPNNL REELTRYLFV LQLKQDILSG KLDCPFDTAV QLAAYNLQAE LGDYDLAEHS PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR DGNDYSLGLT PTGVLVFEGD TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK ARRSTSFERR PSKRYSRRTL QMKACATKPE ELSVHNNVST QSNGSQQAWG MRSALPVSPS ISSAPVPVEI ENLPQSPGTD QHDRKCIPLN IDLLNSPDLL ETTIGDVIGA SDTMETSQAL NDVNVATRLP GLGEPEVEYE TLKDTSEKLK QLEMENSPLL SPRSNIDVNI NSQEEVVKLT EKCLNNVIES PGLNVMRVPP DFKSNILKAQ VEAVHKVTKE DSLLSHKNAN VQDAATNSAV LNENNVPLPK ESLETLMLIT PADSGSVLKE ATDELDALLA SLTENLIDHT VAPQVSSTSM ITPRWIVPSG AMSNGLAGCE MLLTGKEGHG NKDGISLISP PAPFLVDAVT SSGPILAEEA VLKQKCLLTT EL // ID E41LA_HUMAN STANDARD; PRT; 598 AA. AC Q9HCS5; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 18-APR-2006, entry version 28. DE Band 4.1-like protein 4A (NBL4 protein). GN Name=EPB41L4A; Synonyms=EPB41L4; 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]. RX MEDLINE=20334634; PubMed=10874211; RA Ishiguro H., Furukawa Y., Daigo Y., Miyoshi Y., Nagasawa Y., RA Nishiwaki T., Kawasoe T., Fujita M., Satoh S., Miwa N., Fujii Y., RA Nakamura Y.; RT "Isolation and characterization of human NBL4, a gene involved in the RT beta-catenin/tcf signaling pathway."; RL Jpn. J. Cancer Res. 91:597-603(2000). CC -!- TISSUE SPECIFICITY: Expressed in many tissues. High levels of CC expression in brain, liver, thymus and peripheral blood leukocytes CC and low levels of expression in heart, kidney, testis and colon. CC -!- SIMILARITY: Contains 1 FERM 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; AB030240; BAB17229.1; -; mRNA. DR UniGene; Hs.584954; -. DR HSSP; P11171; 1GG3. DR Ensembl; ENSG00000129595; Homo sapiens. DR HGNC; HGNC:13278; EPB41L4A. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Cytoskeleton; Structural protein. FT CHAIN 1 598 Band 4.1-like protein 4A. FT /FTId=PRO_0000219401. FT DOMAIN 11 299 FERM. SQ SEQUENCE 598 AA; 69375 MW; DFCA76152285ECC5 CRC64; MGCFCAVPEE FYCEVLLLDE SKLTLTTQQQ GIKKSTKGSV VLDHVFHHVN LVEIDYFGLR YCDRSHQTYW LDPAKTLAEH KELINTGPPY TLYFGIKFYA EDPCKLKEEI TRYQFFLQVK QDVLQGRLPC PVNTAAQLGA YAIQSELGDY DPYKHTAGYV SEYRFVPDQK EELEEAIERI HKTLMGQIPS EAELNYLRTA KSLEMYGVDL HPVYGENKSE YFLGLTPVGV VVYKNKKQVG KYFWPRITKV HFKETQFELR VLGKDCNETS FFFEARSKTA CKHLWKCSVE HHTFFRMPEN ESNSLSRKLS KFGSIRYKHR YSGRTALQMS RDLSIQLPRP DQNVTRSRSK TYPKRIAQTQ PAESNTISRI TANMENGENE GTIKIIAPSP VKSFKKAKNE NSPDTQRSKS LMHSWEENGP QSGLYNSPSD RTKSPKFPYT RRRNPSCGSD NDSVQPVRRR KAHNSGEDSD LKQRRRSRSR CNTSSGSESE NSNREHRKKR NRIRQENDMV DSAPQWEAVL RRQKEKNQAD PNSRRSRHRS RSRSPDIQAK EELWKHIQKE LVDPSGLSEE QLKEIPYTKI ETQGDPIRIT HSHSPKLY // ID E41LA_MOUSE STANDARD; PRT; 554 AA. AC P52963; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-APR-2006, entry version 36. DE Band 4.1-like protein 4A (NBL4 protein). GN Name=Epb41l4a; Synonyms=Epb4.1l4, Epb4.1l4a, Epb41l4; 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=95074267; PubMed=7983158; RA Takeuchi K., Kawashima A., Nagafuchi A., Tsukita S.; RT "Structural diversity of band 4.1 superfamily members."; RL J. Cell Sci. 107:1921-1928(1994). CC -!- TISSUE SPECIFICITY: Brain, heart, lung, liver and spleen. Not CC detected in thymus and kidney. CC -!- SIMILARITY: Contains 1 FERM 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; D28818; BAA05978.1; -; mRNA. DR PIR; I55505; JU0188. DR UniGene; Mm.3465; -. DR HSSP; P11171; 1GG3. DR Ensembl; ENSMUSG00000024376; Mus musculus. DR MGI; MGI:103007; Epb4.1l4a. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Cytoskeleton; Structural protein. FT CHAIN 1 554 Band 4.1-like protein 4A. FT /FTId=PRO_0000219402. FT DOMAIN 11 299 FERM. SQ SEQUENCE 554 AA; 64082 MW; 7E63BAD0888DBEBE CRC64; MGCFCAVPEE FYCEVLLLDE SKLTLTTQQQ GIKKSTKGSV VLDHVFRHIN LVEIDYFGLR YCDRSHQTYW LDPAKTLAEH KELINTGPPY TLYFGIKFYA EDPCKLKEEI TRYQFFLQVK QDALQGRLPC PVNIAAQMGA YAIQAELGDH DPYKHTAGYV SEYRFVPDQK EELEEAIERI HKTLMGQAPS EAELNYLRTA KSLEMYGVDL HPVYGENKSE YFLGLTPSGV VVYKNKKQVG KYFWPRITKV HFKETQFELR VLGKDCNETS FFFEARSKTA CKHLWKCSVE HHTFFRMPDT ESNSLSRKLS KFGSISYKHR YRTALQMSRD LSIQLPRPNQ NVVRSRSKTY PKRVAQTQPT GSNNINRITA NTENGENEGT TKIIAPSPVK SFKKAKNENS PDPQRSKSHA PWEENGPQSG LYNSSSDRTK SPKFPCARQR NLSCGSDNDS SQLMRRRKAH NSGEDSDLKQ RRRSRSRCNT SSGSESENSN REHRKKRNRT RQENDMVDSG PQWEAVLRRQ KEKNQADPNN RRSRHRSRSR SPDIQAKEEL WKHI // ID E41LB_HUMAN STANDARD; PRT; 913 AA. AC Q9H329; Q9H328; Q9P2V3; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 30-MAY-2006, entry version 35. DE Band 4.1-like protein 4B (EHM2 protein) (FERM-containing protein CG1). GN Name=EPB41L4B; Synonyms=EHM2; 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] (ISOFORMS 1 AND 2). RX MEDLINE=20069079; PubMed=10603000; DOI=10.1007/s003350010017; RA Chadwick B.P., Leyne M., Gill S., Liebert C.B., Mull J., Mezey E., RA Robbins C.M., Pinkett H.W., Makalowska I., Maayan C., Blumenfeld A., RA Axelrod F.B., Brownstein M., Gusella J.F., Slaugenhaupt S.A.; RT "Cloning, mapping, and expression of a novel brain-specific transcript RT in the familial dysautonomia candidate region on chromosome 9q31."; RL Mamm. Genome 11:81-83(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RX MEDLINE=20247250; PubMed=10783258; DOI=10.1006/geno.2000.6154; RA Shimizu K., Nagamachi Y., Tani M., Kimura K., Shiroishi T., Wakana S., RA Yokota J.; RT "Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that RT is expressed in high-metastatic K1735 murine melanoma cells."; RL Genomics 65:113-120(2000). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9H329-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H329-2; Sequence=VSP_007202, VSP_007203; CC Name=3; CC IsoId=Q9H329-3; Sequence=VSP_007201, VSP_007202, VSP_007203; CC -!- SIMILARITY: Contains 1 FERM 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; AF153416; AAG43366.1; -; mRNA. DR EMBL; AF153418; AAG43368.1; -; mRNA. DR EMBL; AB032179; BAA96079.2; -; mRNA. DR UniGene; Hs.591901; -. DR HSSP; P11171; 1GG3. DR Ensembl; ENSG00000095203; Homo sapiens. DR HGNC; HGNC:19818; EPB41L4B. DR LinkHub; Q9H329; -. DR GO; GO:0005856; C:cytoskeleton; TAS. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Alternative splicing; Cytoskeleton. FT CHAIN 1 913 Band 4.1-like protein 4B. FT /FTId=PRO_0000219404. FT DOMAIN 71 355 FERM. FT COMPBIAS 490 503 His-rich. FT VAR_SEQ 1 22 MQRYAGRGGARGRRAGGRARWG -> MLRFLRRTFGRRSMQ FT RYARGAAGRGAAGQGDEREGG (in isoform 3). FT /FTId=VSP_007201. FT VAR_SEQ 456 504 SYPLPSPVLSSSDRLPFGIEENGGTPFLTAASGRHHHQHQH FT QHQHQHHS -> RPSFQDDRSHWKASASGDDSHFDYVHDQN FT QKNLGGMQSMMYRDKLMTAL (in isoform 2 and FT isoform 3). FT /FTId=VSP_007202. FT VAR_SEQ 505 913 Missing (in isoform 2 and isoform 3). FT /FTId=VSP_007203. FT CONFLICT 59 59 V -> M (in Ref. 2). SQ SEQUENCE 913 AA; 100720 MW; 371DD6355FF34C3C CRC64; MQRYAGRGGA RGRRAGGRAR WGPRGGPAAA ASSSALPAAP GGSVFPAGGG PLLTGGAAVH ISAAGAAKAT LYCRVFLLDG TEVSVDLPKH AKGQDLFDQI VYHLDLVETD YFGLQFLDSA QVAHWLDHAK PIKKQMKIGP AYALHFRVKY YSSEPNNLRE EFTRYLFVLQ LRHDILSGKL KCPYETAVEL AALCLQAELG ECELPEHTPE LVSEFRFIPN QTEAMEFDIF QRWKECRGKS PAQAELSYLN KAKWLEMYGV DMHVVRGRDG CEYSLGLTPT GILIFEGANK IGLFFWPKIT KMDFKKSKLT LVVVEDDDQG REQEHTFVFR LDSARTCKHL WKCAVEHHAF FRLRTPGNSK SNRSDFIRLG SRFRFSGRTE YQATHGSRLR RTSTFERKPS KRYPSRRHST FKASNPVIAA QLCSKTNPEV HNYQPQYHPN IHPSQPRWHP HSPNVSYPLP SPVLSSSDRL PFGIEENGGT PFLTAASGRH HHQHQHQHQH QHHSNYSLSL TLENKEGPLR SPNSSSKSLT KLSPGTPALF SEAAAHLKKL ELETVKAAGP WPPLHININK AEEKKVSEKT LQTPLLPSPV ADHVKCNILK AQLENASRVN IQGGKEESPF VNINKKSSLQ DASVRSPIPI RVETAQPAVE KPEIKPPRVR KLTRQYSFDE DDLPPDLAEA VGVTTSTTTN TTTAATQVSV PLPSPKVQNV SSPHKSEGKG LLSPGAKSPS DRGGAFTLEP GDLLMDFTEA TPLAEPASNP HCAHSRCSPP LSLPMKEETT GVCMYPPIKT RLIKTFPVDT MTPFPDTFTT GPQFTADFRD SKLQCCPGPT SPLIPAATLR PLTETVSTVQ TIYTTPETCF SGSQCRDTPA GTGEREDDEK TVDDQTVKFS PCHLEDGMVP SVHLLSSGFV CSL // ID E41LB_MOUSE STANDARD; PRT; 527 AA. AC Q9JMC8; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 18-APR-2006, entry version 27. DE Band 4.1-like protein 4B (EHM2 protein). GN Name=Epb41l4b; Synonyms=Ehm2, Epb4.1l4b; 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=20247250; PubMed=10783258; DOI=10.1006/geno.2000.6154; RA Shimizu K., Nagamachi Y., Tani M., Kimura K., Shiroishi T., Wakana S., RA Yokota J.; RT "Molecular cloning of a novel NF2/ERM/4.1 superfamily gene, Ehm2, that RT is expressed in high-metastatic K1735 murine melanoma cells."; RL Genomics 65:113-120(2000). CC -!- SIMILARITY: Contains 1 FERM 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; AB032366; BAA96078.1; -; mRNA. DR UniGene; Mm.28217; -. DR HSSP; P11171; 1GG3. DR Ensembl; ENSMUSG00000028434; Mus musculus. DR MGI; MGI:1859149; Epb4.1l4b. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Cytoskeleton. FT CHAIN 1 527 Band 4.1-like protein 4B. FT /FTId=PRO_0000219405. FT DOMAIN 85 369 FERM. SQ SEQUENCE 527 AA; 59578 MW; 9CC110068A841DDC CRC64; MLRFLRRTFG RRSMQRYARG AAGRGAAGLG DERDGGPRGG PAAAASSSVL PAAPGGSVFP AGGGPLLTGG AAVHISASGA AKATLYCRVF LLDGTEVSVD LPKHAKGQDL FDQIVYHLDL VETDYFGLQF LDSAQVTHWL DHAKPIKKQM KVGPAYALHF RVKYYSSEPN NLREEFTRYL FVLQLRHDIL SGKLKCPYET AVELAALCLQ AELGECELPE HTPELVSEFR FIPNQTEAME FDIFQRWKEY RGKSPAQAEL SYLNKAKWLE MYGVDMHVVR GRDGCEYSLG LTPTGILIFE GANKIGLFFW PKITKMDFKK SKLTLVVVED DDQGREQEHT FVFRLDSART CKHLWKCAVE HHAFFRLRTP SNSKSARSDF IRLGSRFRFS GRTEYQATHG SRLRRTSTFE RKPSKRYPSR RHSTFKASNP IIAAQLCSKA NPEVHNYQPQ YHPDVHPSQP RWRPHSPNVS NHSICKQNKP CFQDDRPHWK TSASGDGSHF DYVQDQNQRN LGGAYSVTYR DKLMTAL // ID EXPA_DROME STANDARD; PRT; 1427 AA. AC Q07436; Q9VPQ0; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 3. DT 04-APR-2006, entry version 37. DE Protein expanded. GN Name=ex; ORFNames=CG4114; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE. RC TISSUE=Imaginal disk; RX MEDLINE=94094747; PubMed=8269855; RA Boedigheimer M., Laughon A.; RT "Expanded: a gene involved in the control of cell proliferation in RT imaginal discs."; RL Development 118:1291-1301(1993). RN [2] RP SEQUENCE REVISION. RA Boedigheimer M.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX MEDLINE=20196006; PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [4] RP GENOME REANNOTATION. RX MEDLINE=22426069; PubMed=12537572; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., RA Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., RA Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a RT systematic review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Head; RX MEDLINE=22426066; PubMed=12537569; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., RA George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., RA Rubin G.M., Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). CC -!- FUNCTION: Involved in the control of cell proliferation in CC imaginal disks. May bind to certain proteins of signal CC transduction pathways by interaction with their SH3 domains. CC -!- SUBCELLULAR LOCATION: Apical surface of disk cells. CC -!- MISCELLANEOUS: Mutations of expanded protein cause hyperplasmia of CC the imaginal disk resulting in wing overgrowth. This overgrowth is CC limited to specific regions along the 2 wing axs. Defects also in CC eyes, head, thorax and limbs where duplication and bulging often CC occur. CC -!- SIMILARITY: Contains 1 FERM 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; L14768; AAB39774.1; -; mRNA. DR EMBL; AE003589; AAF51495.1; -; Genomic_DNA. DR EMBL; AY069068; AAL39213.1; -; mRNA. DR PIR; T13720; T13720. DR UniGene; Dm.247; -. DR Ensembl; CG4114; Drosophila melanogaster. DR FlyBase; FBgn0004583; ex. DR GO; GO:0016324; C:apical plasma membrane; TAS. DR GO; GO:0005915; C:zonula adherens; TAS. DR GO; GO:0045571; P:negative regulation of imaginal disc growth; TAS. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR009065; FERM. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; FALSE_NEG. DR PROSITE; PS50057; FERM_3; 1. KW Complete proteome; Developmental protein; SH3-binding. FT CHAIN 1 1427 Protein expanded. FT /FTId=PRO_0000219443. FT DOMAIN 26 399 FERM. FT MOTIF 1008 1016 SH3-binding (Potential). FT MOTIF 1012 1020 SH3-binding (Potential). FT MOTIF 1149 1157 SH3-binding (Potential). FT COMPBIAS 409 412 Poly-Glu. FT COMPBIAS 782 788 Poly-Pro. FT COMPBIAS 952 955 Poly-His. FT COMPBIAS 1002 1005 Poly-Pro. FT COMPBIAS 1011 1017 Poly-Pro. FT COMPBIAS 1081 1084 Poly-Pro. FT COMPBIAS 1149 1154 Poly-Pro. FT COMPBIAS 1158 1168 Poly-Ala. FT COMPBIAS 1170 1174 Poly-Ser. FT COMPBIAS 1199 1205 Poly-Pro. FT COMPBIAS 1416 1422 Poly-Gln. FT CONFLICT 160 161 EQ -> DE (in Ref. 1). FT CONFLICT 194 194 S -> L (in Ref. 1). FT CONFLICT 347 347 F -> S (in Ref. 1). FT CONFLICT 563 563 I -> T (in Ref. 1). FT CONFLICT 671 671 A -> D (in Ref. 1). FT CONFLICT 693 693 Q -> S (in Ref. 1). FT CONFLICT 1293 1294 SM -> FN (in Ref. 1). FT CONFLICT 1422 1422 Q -> QQQ (in Ref. 1). SQ SEQUENCE 1427 AA; 153644 MW; 3CC1AD0B4D900EB2 CRC64; MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR VREVYTQTCL HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW RSSHTHGLDA NGRPLLELHF RVQFYIESPF MLKDETSRHN YYLQLRHNIL QRDLPREQAE QALVFLAGLA LQADLGDAPP GTSNSKDDSG EETSASPSNG GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP PSLPPNGADY YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESTNSSS NPETTTFLWP NITKLSFERK KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA RLKEVSKREE EEAAESQRLH ASYACSRSLL LPYKSKNEQR ISVISSTSSN TTSGIVSDRV HSEDELEIMI NTPPAPLAAP STESLALAHL LDRPSVSRQT SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQR NSMGTTANDS STATDSPSSQ HNIGSQCSST CSTVVVTSPV NGAGASSSGA PIPVHSTSSS LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGAPPT ETSGVYTMHS SELTGQSSEI AESEKSSHYG MFQPQKLEET HVQHSDSVDG KKKEDFRPRS DSNVSTGSSF RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD QPPAPPPPYS ARHEKTGLCG PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PIPAPPPAIR RRDPPPYSIS SKPRPTSLIS VSSSAHPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS LHHHHVPSHH RHSGSAAIGI VPYGLHKSTA SLHHQQSCVL LPVIKPRQFL APPPPSLPRQ PPPPPPPNHP HLASHLYERE MARKQLELYQ QQLYSDVDYV IYPIQDPAVS QQEYLDAKQG SLLAAMAQAA PPPPHHPYLA MQVSPAIYRS TPYLPLTLST HSRYASTQNL SDTYVQLPGP GYSPLYSPSM ASLCSSYEPP PPPPLHPAAL AAAAAAGAGS SSSSMFARSR SDDNILNSLD LLPKGKRLPP PPPPPYVNRR LKKPPMPAPS EKPPPIPSKP IPSRMSPIPP RKPPTLNPHH ANSPLTKTSS GAQWAGERPR PDLGLGLGLN RGNNSILAQL QASMVAQSHA QAQAQALDIA LLREKSKHLD LPLISALCND RSLLKQTKVV INPKTGQEMP TSSAQPSGAT TNGVANSSAG AGTLSKARKG STVSHRHPQD KLPPLPVQQL AEANNYVIDP AVMMKQQQQQ QQHNKTS // ID EZRI_BOVIN STANDARD; PRT; 580 AA. AC P31976; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 04-APR-2006, entry version 46. DE Ezrin (p81) (Cytovillin) (Villin-2). GN Name=VIL2; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RA Bergson C.M., Zhao H., Saijoh K., Duman R.S., Nestler E.J.; RT "Ezrin and osteonectin, two proteins associated with cell shape and RT growth, are enriched in the locus coeruleus."; RL Mol. Cell. Neurosci. 4:64-73(1993). RN [2] RP PROTEIN SEQUENCE OF 1-15 AND 126-140. RC TISSUE=Kidney; RX MEDLINE=96239137; PubMed=8660651; DOI=10.1006/abbi.1996.0248; RA Galat A., Gerbod M.C., Bouet F., Riviere S.; RT "Proteins and their amino acid compositions: uniqueness, variability, RT and applications."; RL Arch. Biochem. Biophys. 330:229-237(1996). CC -!- FUNCTION: Probably involved in connections of major cytoskeletal CC structures to the plasma membrane. CC -!- SUBUNIT: Interacts with SLC9A3R1 and PACE1. Interacts with MPP5 CC (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane-associated. Localization to the CC apical membrane of parietal cells depends on the interaction with CC MPP5. Localizes to cell extensions and peripheral processes of CC astrocytes (By similarity). Microvillar peripheral membrane CC protein (cytoplasmic side). CC -!- PTM: Phosphorylated by tyrosine-protein kinases. CC -!- SIMILARITY: Contains 1 FERM 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; M98498; AAA30510.1; -; mRNA. DR PIR; I45889; I45889. DR UniGene; Bt.3583; -. DR HSSP; P15311; 1NI2. DR SMR; P31976; 1-296. DR GO; GO:0015629; C:actin cytoskeleton; ISS. DR GO; GO:0051015; F:actin filament binding; ISS. DR GO; GO:0005515; F:protein binding; ISS. DR GO; GO:0051017; P:actin filament bundle formation; ISS. DR InterPro; IPR000299; Band_4.1. DR InterPro; IPR011174; ERM. DR InterPro; IPR011259; ERM_C. DR InterPro; IPR000798; Ez/rad/moesin. DR InterPro; IPR009065; FERM. DR InterPro; IPR008954; Moesin. DR InterPro; IPR011993; PH_type. DR Pfam; PF00373; Band_41; 1. DR Pfam; PF00769; ERM; 1. DR PIRSF; PIRSF002305; ERM; 1. DR PRINTS; PR00935; BAND41. DR PRINTS; PR00661; ERMFAMILY. DR SMART; SM00295; B41; 1. DR PROSITE; PS00660; FERM_1; 1. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; 1. KW Cell shape; Cytoskeleton; Direct protein sequencing; Membrane; KW Phosphorylation; Structural protein. FT INIT_MET 0 0 FT CHAIN 1 580 Ezrin. FT /FTId=PRO_0000219407. FT DOMAIN 1 294 FERM. FT REGION 243 580 Interaction with PACE1 (By similarity). FT MOD_RES 145 145 Phosphotyrosine (by PDGFR) (By FT similarity). FT MOD_RES 353 353 Phosphotyrosine (by PDGFR) (By FT similarity). SQ SEQUENCE 580 AA; 68629 MW; ECD663E5C200FAA3 CRC64; PKPINVRVTT MDAELEFAIQ PNTTGKQLFD QVVKTIGLRE VWYFGLQYVD NKGFPTWLKL DKKVSAQEVR KESPLQFKFR AKFYPEDVAE ELIQDITQKL FFLQVKEGIL SDEIYCPPET AVLLGSYAVQ AKFGDYNKEL HKAGYLGSER LIPQRVMDQH KLTRDQWEDR IQVWHAEHRG MLKDSAMLEY LKIAQDLEMY GINYFEIKNK KGTDLWLGVD ALGLNIYEKD DKLTPKIGFP WSEIRNISFN DKKFVIKPID KKAPDFVFYA PRLRINKRIL QLCMGNHELY MRRRKPDTIE VQQMKAQARE EKHQKQLERQ QLETEKKRRE TVEREKEQMM REKEELMLRL QDYEEKTRKA EKELSDQIQR ALKLEEERKR AQEEAGRLEA DRLAALRAKE ELERQAADQI KSQEQLATEL AEYTAKIALL EEARRRKENE VEEWQLRAKE AQDDLVKTRE ELHLVMTAPP PPPVYEPVNY HVHEGPQEEG TELSAELSSE GILDDRNEEK RITEAEKNER VQRQLMTLTS ELSQARDENK RTHNDIIHNE NMRQGRDKYK TLRQIRQGNT KQRIDEFEAM // ID EZRI_HUMAN STANDARD; PRT; 585 AA. AC P15311; P23714; Q96CU8; Q9NSJ4; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 2. DT 18-APR-2006, entry version 68. DE Ezrin (p81) (Cytovillin) (Villin-2). GN Name=VIL2; 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 PARTIAL PROTEIN SEQUENCE. RX MEDLINE=90076135; PubMed=2591371; RA Gould K.L., Bretscher A., Esch F.S., Hunter T.; RT "cDNA cloning and sequencing of the protein-tyrosine kinase substrate, RT ezrin, reveals homology to band 4.1."; RL EMBO J. 8:4133-4142(1989). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Placenta; RX MEDLINE=89380299; PubMed=2674140; RA Turunen O., Winqvist R., Pakkanen R., Grzeschik K.-H., Wahlstroem T., RA Vaheri A.; RT "Cytovillin, a microvillar Mr 75,000 protein. cDNA sequence, RT prokaryotic expression, and chromosomal localization."; RL J. Biol. Chem. 264:16727-16732(1989). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-531. RC TISSUE=Melanoma; RG The German cDNA consortium; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-531. RC TISSUE=Colon; 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 [5] RP PROTEIN SEQUENCE OF 171-179 AND 342-349. RX MEDLINE=96311348; PubMed=8713105; DOI=10.1006/bbrc.1996.1082; RA Egerto