ID   E41L5_CANLF             Reviewed;         505 AA.
AC   Q9MYU8;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 103.
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; Synonyms=BE37;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Thyroid;
RA   Pichon B., Christophe D.;
RT   "Cloning of the cDNA encoding protein Band 4.1-like 5, a new member of the
RT   Band 4.1 family of proteins.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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:0000250|UniProtKB:Q5FVG2}.
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DR   EMBL; AJ401272; CAB96753.1; -; mRNA.
DR   RefSeq; NP_001002952.1; NM_001002952.1.
DR   AlphaFoldDB; Q9MYU8; -.
DR   SMR; Q9MYU8; -.
DR   STRING; 9612.ENSCAFP00000007253; -.
DR   PaxDb; Q9MYU8; -.
DR   Ensembl; ENSCAFT00040013060; ENSCAFP00040011304; ENSCAFG00040006786.
DR   GeneID; 403419; -.
DR   KEGG; cfa:403419; -.
DR   CTD; 57669; -.
DR   eggNOG; KOG3530; Eukaryota.
DR   InParanoid; Q9MYU8; -.
DR   OrthoDB; 241659at2759; -.
DR   Reactome; R-CFA-6794361; Neurexins and neuroligins.
DR   Proteomes; UP000002254; Unplaced.
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   2: Evidence at transcript level;
KW   Cell junction; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..505
FT                   /note="Band 4.1-like protein 5"
FT                   /id="PRO_0000330354"
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          357..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         39
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9HCM4"
SQ   SEQUENCE   505 AA;  57911 MW;  94B7F2DDFF409859 CRC64;
     MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP
     KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
     KFYSSEPNNL REELTRYLFV LQLKQDILSG KLECPFDTAV QLAAYNLQAE LGDYDLAEHS
     PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
     DGNDYSLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKNK LTLVVVEDDV QGKEQEHTFV
     FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK
     ARRSTSFERR PSKRYSRRTL QMKASTAKPE ELSVHNNVST QSNGSQQAWS VRSTLPVIPS
     VPSGPVLAEI ENLPRNPGSN QYDRKWVSAA SDCCQRGGNQ WNTRALSPPQ PAHRNYTDFV
     HEHNVKNTGV HHDVHFPGHA AMTEI