ID   E41L5_BOVIN             Reviewed;         502 AA.
AC   Q58CU2;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Band 4.1-like protein 5;
DE   AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000250|UniProtKB:Q9HCM4};
GN   Name=EPB41L5;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION WITH CRB1, 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)
CC       (PubMed:17920587). Interacts with CRB2 (via intracellular domain) (By
CC       similarity). Interacts with CRB3 (via intracellular domain) (By
CC       similarity). {ECO:0000250|UniProtKB:Q9HCM4,
CC       ECO:0000269|PubMed:17920587}.
CC   -!- INTERACTION:
CC       Q58CU2; P82279: CRB1; Xeno; NbExp=2; IntAct=EBI-26451934, EBI-1048648;
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:0000250|UniProtKB:Q5FVG2}.
CC   -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level).
CC       {ECO:0000269|PubMed:17920587}.
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DR   EMBL; BT021855; AAX46702.1; -; mRNA.
DR   EMBL; BC105257; AAI05258.1; -; mRNA.
DR   RefSeq; NP_001030461.1; NM_001035384.1.
DR   AlphaFoldDB; Q58CU2; -.
DR   SMR; Q58CU2; -.
DR   IntAct; Q58CU2; 1.
DR   STRING; 9913.ENSBTAP00000053352; -.
DR   PaxDb; Q58CU2; -.
DR   PRIDE; Q58CU2; -.
DR   Ensembl; ENSBTAT00000024277; ENSBTAP00000024277; ENSBTAG00000018236.
DR   GeneID; 530941; -.
DR   KEGG; bta:530941; -.
DR   CTD; 57669; -.
DR   VEuPathDB; HostDB:ENSBTAG00000018236; -.
DR   VGNC; VGNC:28525; EPB41L5.
DR   eggNOG; KOG3530; Eukaryota.
DR   GeneTree; ENSGT00940000156332; -.
DR   HOGENOM; CLU_003623_1_0_1; -.
DR   InParanoid; Q58CU2; -.
DR   OMA; ATSDCCQ; -.
DR   OrthoDB; 241659at2759; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000018236; Expressed in thyroid gland and 102 other tissues.
DR   ExpressionAtlas; Q58CU2; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   GO; GO:0031032; P:actomyosin structure organization; IBA:GO_Central.
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; 1.
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   Cell junction; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..502
FT                   /note="Band 4.1-like protein 5"
FT                   /id="PRO_0000330353"
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          359..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          430..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        433..447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCM4"
SQ   SEQUENCE   502 AA;  57169 MW;  91375805DC641A92 CRC64;
     MLSFFRRTLG RRSMRKQAEK DRLREAQRAA THIPAAGDAR AVITCRVSLL 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 KNSHRSGFIR LGSRFRYSGK TEYQTTKTNK
     ARRSTSFERR PSKRYSRRTL QVKASTGKPE ELSVHNNVSA QSNGSQQAWG VRSTVPVIPS
     GPVVVEVENL PKSPGADQHD KKWLSAAGDR SQRGGNQWDT RALSPPHPAP RNYPAFVHEH
     NVKNAGAQQN AHFPGPAAMT DI