E41L5_MOUSE
ID E41L5_MOUSE Reviewed; 731 AA.
AC Q8BGS1; Q3TJG0; Q69ZG8; Q8BSC9; Q99KZ8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Band 4.1-like protein 5;
DE AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000312|MGI:MGI:103006};
GN Name=Epb41l5; Synonyms=Epb4.1l5, Kiaa1548;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Skin, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-455 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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:0000269|PubMed:17920587}. Cell
CC junction, adherens junction {ECO:0000269|PubMed:17920587}. Cell
CC membrane {ECO:0000269|PubMed:17920587}; Peripheral membrane protein
CC {ECO:0000305}. Photoreceptor inner segment
CC {ECO:0000250|UniProtKB:Q5FVG2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BGS1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BGS1-2; Sequence=VSP_033040, VSP_033041;
CC Name=3;
CC IsoId=Q8BGS1-3; Sequence=VSP_033039;
CC -!- TISSUE SPECIFICITY: In the retina, expressed at the outer limiting
CC membrane, retinal pigment epithelium, outer nuclear layer and outer
CC plexiform layer (at protein level) (PubMed:17920587). Also detected in
CC the inner segments (at protein level) (PubMed:17920587). Expressed at
CC the basolateral and apical sides of the mesonephric tubules in the
CC kidney (at protein level) (PubMed:17920587).
CC {ECO:0000269|PubMed:17920587}.
CC -!- DEVELOPMENTAL STAGE: At 10.5 dpc, strongly expressed in the developing
CC neural tube and optic vesicle, as well as in the branchial arches and
CC kidney (PubMed:17920587). In the developing kidney, detected in the
CC mesonephrotic tubules (PubMed:17920587). At 11.5 dpc, expressed along
CC the entire cranial-caudal length of the developing neural tube,
CC including the anterior forebrain and the posterior spinal cord
CC (PubMed:17920587). Always restricted to the ventricular layer, where
CC proliferative cells are located (PubMed:17920587). Conversely, not
CC detected in postmitotic neural compartments (PubMed:17920587). In the
CC developing lung, at 11.5 dpc, expressed in the internal endodermal
CC layer and in particular in the nascent bronchial tips
CC (PubMed:17920587). At 12.5 dpc, expressed in the optic vesicle,
CC detected mainly in the retinal layer (PubMed:17920587). The retinal
CC pigment epithelium shows only background levels (PubMed:17920587). At
CC 15.5 dpc expressed at the basolateral side of the plasma membrane in
CC brain, spinal cord, kidney, testis, intestine, skin, and muscles
CC (PubMed:17920587). {ECO:0000269|PubMed:17920587}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32476.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK173198; BAD32476.1; ALT_INIT; mRNA.
DR EMBL; AK034676; BAC28794.1; -; mRNA.
DR EMBL; AK044959; BAC32159.1; -; mRNA.
DR EMBL; AK044996; BAC32177.1; -; mRNA.
DR EMBL; AK079301; BAC37601.1; -; mRNA.
DR EMBL; AK136125; BAE22832.1; -; mRNA.
DR EMBL; AK161141; BAE36211.1; -; mRNA.
DR EMBL; AK167449; BAE39535.1; -; mRNA.
DR EMBL; BC003937; AAH03937.1; -; mRNA.
DR EMBL; BC011476; AAH11476.1; -; mRNA.
DR CCDS; CCDS15226.1; -. [Q8BGS1-1]
DR CCDS; CCDS48339.1; -. [Q8BGS1-2]
DR RefSeq; NP_001106887.1; NM_001113416.1. [Q8BGS1-2]
DR RefSeq; NP_663481.2; NM_145506.4. [Q8BGS1-1]
DR RefSeq; XP_006529460.1; XM_006529397.1. [Q8BGS1-1]
DR RefSeq; XP_006529461.1; XM_006529398.1. [Q8BGS1-1]
DR RefSeq; XP_006529463.1; XM_006529400.1. [Q8BGS1-2]
DR AlphaFoldDB; Q8BGS1; -.
DR SMR; Q8BGS1; -.
DR BioGRID; 230501; 1.
DR IntAct; Q8BGS1; 3.
DR STRING; 10090.ENSMUSP00000128374; -.
DR iPTMnet; Q8BGS1; -.
DR PhosphoSitePlus; Q8BGS1; -.
DR jPOST; Q8BGS1; -.
DR MaxQB; Q8BGS1; -.
DR PaxDb; Q8BGS1; -.
DR PeptideAtlas; Q8BGS1; -.
DR PRIDE; Q8BGS1; -.
DR ProteomicsDB; 277538; -. [Q8BGS1-1]
DR ProteomicsDB; 277539; -. [Q8BGS1-2]
DR ProteomicsDB; 277540; -. [Q8BGS1-3]
DR Antibodypedia; 33383; 136 antibodies from 27 providers.
DR Ensembl; ENSMUST00000027632; ENSMUSP00000027632; ENSMUSG00000026383. [Q8BGS1-2]
DR Ensembl; ENSMUST00000052404; ENSMUSP00000058966; ENSMUSG00000026383. [Q8BGS1-1]
DR Ensembl; ENSMUST00000163147; ENSMUSP00000128374; ENSMUSG00000026383. [Q8BGS1-3]
DR Ensembl; ENSMUST00000191046; ENSMUSP00000140227; ENSMUSG00000026383. [Q8BGS1-2]
DR GeneID; 226352; -.
DR KEGG; mmu:226352; -.
DR UCSC; uc007ciw.2; mouse. [Q8BGS1-1]
DR UCSC; uc007cix.2; mouse. [Q8BGS1-2]
DR UCSC; uc011wqs.1; mouse. [Q8BGS1-3]
DR CTD; 57669; -.
DR MGI; MGI:103006; Epb41l5.
DR VEuPathDB; HostDB:ENSMUSG00000026383; -.
DR eggNOG; KOG3530; Eukaryota.
DR GeneTree; ENSGT00940000156332; -.
DR HOGENOM; CLU_003623_5_1_1; -.
DR InParanoid; Q8BGS1; -.
DR OMA; ATSDCCQ; -.
DR OrthoDB; 241659at2759; -.
DR PhylomeDB; Q8BGS1; -.
DR TreeFam; TF319780; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 226352; 1 hit in 39 CRISPR screens.
DR ChiTaRS; Epb41l5; mouse.
DR PRO; PR:Q8BGS1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BGS1; protein.
DR Bgee; ENSMUSG00000026383; Expressed in secondary oocyte and 191 other tissues.
DR ExpressionAtlas; Q8BGS1; baseline and differential.
DR Genevisible; Q8BGS1; MM.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0031252; C:cell leading edge; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IDA:MGI.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; IDA:MGI.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:MGI.
DR GO; GO:0003383; P:apical constriction; IDA:MGI.
DR GO; GO:0048318; P:axial mesoderm development; IMP:MGI.
DR GO; GO:0048319; P:axial mesoderm morphogenesis; IMP:MGI.
DR GO; GO:0000904; P:cell morphogenesis involved in differentiation; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:MGI.
DR GO; GO:0007398; P:ectoderm development; IMP:MGI.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IMP:MGI.
DR GO; GO:0007492; P:endoderm development; IMP:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0070986; P:left/right axis specification; IMP:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:MGI.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:MGI.
DR GO; GO:0001839; P:neural plate morphogenesis; IMP:MGI.
DR GO; GO:0048339; P:paraxial mesoderm development; IMP:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:MGI.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:MGI.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:MGI.
DR GO; GO:0032092; P:positive regulation of protein binding; IDA:MGI.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IMP:MGI.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IDA:MGI.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI.
DR GO; GO:0001756; P:somitogenesis; IMP:MGI.
DR GO; GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; IMP:MGI.
DR GO; GO:0009826; P:unidimensional cell growth; IDA:MGI.
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 Methylation; Reference proteome.
FT CHAIN 1..731
FT /note="Band 4.1-like protein 5"
FT /id="PRO_0000330355"
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 352..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 393
FT /note="G -> GRFSSLLYS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_033039"
FT VAR_SEQ 445..504
FT /note="CLPLSVDLLNSPDLLETTIGDVTRTSETSAPFPAPDTINVATRSNELEEFKA
FT ECETLKDD -> WLSATSDRCQRGGNQWNPRALPPPQTAYRNYTDFVHEHNVKNAGAHH
FT DAQLSGRAAMTEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033040"
FT VAR_SEQ 505..731
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033041"
FT CONFLICT 113
FT /note="P -> H (in Ref. 2; BAE39535)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="D -> Y (in Ref. 2; BAC28794)"
FT /evidence="ECO:0000305"
FT MOD_RES Q8BGS1-2:455
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
SQ SEQUENCE 731 AA; 81636 MW; 77348A1F68EF596A CRC64;
MLSFLRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDAK SIITCRVSLL DGTDVSVDLP
KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLECPFDTAV QLAAYNLQAE LGDYDLAEHS
PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
DGNDYSLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK
ARRSTSFERR PSKRYSRRTL QMKASTTQPE DLGVLNASAQ KSDSQQAWGV MSPVPVTSSS
SCGAVQVEIE NLPQTSATEQ HDRKCLPLSV DLLNSPDLLE TTIGDVTRTS ETSAPFPAPD
TINVATRSNE LEEFKAECET LKDDTEKLKQ LETEQTILPS LRPTIDINVN SQEEVVKLTE
KCLNNAIENP ALNAVKVPPD FKSNILKAQV EAVHKVTRED SLLTHKNASV QDAATNSTAF
NENDVPVCKD SLTPVHGTAA DSASVLKDAT DELDALLLSL TENLMDHTVT PQVSSPSMIT
PRWIIPQSAT ISNGLAGYGA SLAGTDECSQ KDGFSLISPP APFLVDAVTS SAPPLPEDST
LKQKCLLTTE L
