E41L5_RAT
ID E41L5_RAT Reviewed; 731 AA.
AC Q5FVG2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Band 4.1-like protein 5;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000312|RGD:1311366};
GN Name=Epb41l5; Synonyms=Epb4.1l5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT complex.";
RL Exp. Cell Res. 313:3959-3970(2007).
CC -!- FUNCTION: Plays a role in the formation and organization of tight
CC junctions during the establishment of polarity in epithelial cells.
CC {ECO:0000250|UniProtKB:Q9HCM4}.
CC -!- SUBUNIT: Component of a complex composed of PALS1, CRB1 and EPB41L5 (By
CC similarity). Within the complex, interacts (via FERM domain) with PALS1
CC (via HOOK domain) and with CRB1 (via intracellular domain) (By
CC similarity). Interacts with CRB2 (via intracellular domain) (By
CC similarity). Interacts with CRB3 (via intracellular domain) (By
CC similarity). {ECO:0000250|UniProtKB:Q9HCM4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC junction, adherens junction {ECO:0000250|UniProtKB:Q8BGS1}. Cell
CC membrane {ECO:0000250|UniProtKB:Q8BGS1}; Peripheral membrane protein
CC {ECO:0000305}. Photoreceptor inner segment
CC {ECO:0000269|PubMed:17920587}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5FVG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5FVG2-2; Sequence=VSP_033042, VSP_033043, VSP_033044;
CC -!- TISSUE SPECIFICITY: Expressed in the outer limiting membrane, retinal
CC pigment epithelium, outer nuclear layer and outer plexiform layer of
CC the retina (at protein level). {ECO:0000269|PubMed:17920587}.
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DR EMBL; AABR03085414; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03085531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03086343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC090012; AAH90012.1; -; mRNA.
DR RefSeq; NP_001012023.1; NM_001012023.1. [Q5FVG2-2]
DR AlphaFoldDB; Q5FVG2; -.
DR SMR; Q5FVG2; -.
DR STRING; 10116.ENSRNOP00000045431; -.
DR iPTMnet; Q5FVG2; -.
DR PhosphoSitePlus; Q5FVG2; -.
DR PaxDb; Q5FVG2; -.
DR PRIDE; Q5FVG2; -.
DR Ensembl; ENSRNOT00000042862; ENSRNOP00000045431; ENSRNOG00000002538. [Q5FVG2-2]
DR Ensembl; ENSRNOT00000111356; ENSRNOP00000089466; ENSRNOG00000002538. [Q5FVG2-1]
DR GeneID; 304733; -.
DR KEGG; rno:304733; -.
DR CTD; 57669; -.
DR RGD; 1311366; Epb41l5.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000156332; -.
DR HOGENOM; CLU_003623_5_1_1; -.
DR InParanoid; Q5FVG2; -.
DR OrthoDB; 241659at2759; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:Q5FVG2; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Bgee; ENSRNOG00000002538; Expressed in lung and 18 other tissues.
DR ExpressionAtlas; Q5FVG2; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0032587; C:ruffle membrane; ISO:RGD.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR GO; GO:0031032; P:actomyosin structure organization; ISO:RGD.
DR GO; GO:0003383; P:apical constriction; ISO:RGD.
DR GO; GO:0048318; P:axial mesoderm development; ISO:RGD.
DR GO; GO:0048319; P:axial mesoderm morphogenesis; ISO:RGD.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
DR GO; GO:0007398; P:ectoderm development; ISO:RGD.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; ISO:RGD.
DR GO; GO:0007492; P:endoderm development; ISO:RGD.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISO:RGD.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0070986; P:left/right axis specification; ISO:RGD.
DR GO; GO:0007498; P:mesoderm development; ISO:RGD.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; ISO:RGD.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISO:RGD.
DR GO; GO:0032091; P:negative regulation of protein binding; ISO:RGD.
DR GO; GO:0001839; P:neural plate morphogenesis; ISO:RGD.
DR GO; GO:0048339; P:paraxial mesoderm development; ISO:RGD.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:RGD.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISO:RGD.
DR GO; GO:0070201; P:regulation of establishment of protein localization; ISO:RGD.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; ISO:RGD.
DR GO; GO:0001756; P:somitogenesis; ISO:RGD.
DR GO; GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; ISO:RGD.
DR GO; GO:0009826; P:unidimensional cell growth; ISO:RGD.
DR CDD; cd14473; FERM_B-lobe; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR030694; Band4.1-like5.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280:SF15; PTHR23280:SF15; 2.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Reference proteome.
FT CHAIN 1..731
FT /note="Band 4.1-like protein 5"
FT /id="PRO_0000330356"
FT DOMAIN 43..327
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 29..119
FT /note="Required for interaction with CRB1"
FT /evidence="ECO:0000250|UniProtKB:Q9HCM4"
FT REGION 356..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 384..393
FT /note="GEVWPCSTGS -> ASTAKPDDLG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033042"
FT VAR_SEQ 447..504
FT /note="PLSIDLLNSPDLLETTIGDVTRPSDTSAPFPAPDDVNVATMSHELEELRADC
FT ETLKDD -> SATSDRCQRGGHQWNPRALPPPQTAYRNYTDFVHEHNVKNAGAHHDAHL
FT AGRAAMTDI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033043"
FT VAR_SEQ 505..731
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033044"
SQ SEQUENCE 731 AA; 81718 MW; FB21417F2172D7FD CRC64;
MLSFLRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDAK SVITCRVSLL DGTDVSVDLP
KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLECPFDTAV QLAAYNLQAE LGDYDLAEHS
PELVSEFRFV PTQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
DGNDYSLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KGSHRSGFIR LGSRFRYSGK TEYQTTKTNK
ARRSTSFERR PSKRYSRRTL QVKGEVWPCS TGSVHNASAQ NNDSQQAWGM KSPVPVTSFS
SSGPVLVETE NLPQNSAADQ HDRKRLPLSI DLLNSPDLLE TTIGDVTRPS DTSAPFPAPD
DVNVATMSHE LEELRADCET LKDDTEKLKQ LNTEQNILPS LRPAIDINVN SQEEVVKLTE
KCLNNAIESP GLNTVRVPPD FKSNILKAQV EAVHKATRED SLLTHKNASV QDAATNSTVF
NENNMPLCKD SLTPVHGTTA DSDSVLKDAT DELDALLLSL TENLMDHTVT PQVSSSSMIT
PRWIIPQNST ISNGLAGYGV SLTGTEGCNQ KDGFSLISPP APFLVDAVTS SAPPLPGDSA
LKQKCLLTTE L
