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Database: UniProt
Entry: A0A3Q7UK57_VULVU
LinkDB: A0A3Q7UK57_VULVU
Original site: A0A3Q7UK57_VULVU 
ID   A0A3Q7UK57_VULVU        Unreviewed;       753 AA.
AC   A0A3Q7UK57;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Band 4.1-like protein 5 {ECO:0000256|ARBA:ARBA00023841};
DE   AltName: Full=Erythrocyte membrane protein band 4.1-like 5 {ECO:0000256|ARBA:ARBA00030226};
GN   Name=EPB41L5 {ECO:0000313|RefSeq:XP_025873557.1};
OS   Vulpes vulpes (Red fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX   NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025873557.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025873557.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025873557.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025873557.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: Plays a role in the formation and organization of tight
CC       junctions during the establishment of polarity in epithelial cells.
CC       {ECO:0000256|ARBA:ARBA00023750}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}. Photoreceptor inner segment
CC       {ECO:0000256|ARBA:ARBA00004437}.
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DR   RefSeq; XP_025873557.1; XM_026017772.1.
DR   AlphaFoldDB; A0A3Q7UK57; -.
DR   KEGG; vvp:112934352; -.
DR   OrthoDB; 3682543at2759; -.
DR   Proteomes; UP000286640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
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   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13186; FERM_C_NBL4_NBL5; 1.
DR   CDD; cd17205; FERM_F1_EPB41L5; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
DR   InterPro; IPR014847; FA.
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; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF15; BAND 4.1-LIKE PROTEIN 5; 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; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000286640}.
FT   DOMAIN          43..327
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          352..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..407
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   753 AA;  84498 MW;  3ED43FD18640A782 CRC64;
     MLSFFRRTLG RRSMRKHAEK ERLREAQRAA THIPAAGDSK SIITCRVSLL DGTDVSVDLP
     KKAKGQELFD QIMYHLDLIE SDYFGLRFMD SAQVAHWLDG TKSIKKQVKI GSPYCLHLRV
     KFYSSEPNNL REELTRYLFV LQLKQDILSG KLECPFDIAV QLAAYNLQAE LGDYDLAEHS
     PELVSEFRFV PIQTEEMELA IFEKWKEYRG QTPAQAETNY LNKAKWLEMY GVDMHVVKAR
     DGNDYSLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKNK LTLVVVEDDD QGKEQEHTFV
     FRLDHPKACK HLWKCAVEHH AFFRLRGPVQ KSSHRSGFIR LGSRFRYSGK TEYQTTKTNK
     ARRSTSFERR PSKRYSRRTL QMKASTAKPE ELSVHNNVST QSNGSQQAWG VRSTLPVIPS
     VPSGPVLAEI ENLPRNPGSN QYDRKCLPLN IDLLDSPDLL ETTIDDVIGA PDTLEIAQAP
     DEVNIITRQT GLEGTKEECG TLKDASQKLK HLEMESSPLP SPRPNIDVNI NNQTYFKSTI
     YGCSGGKEET WAVIRTEEVM KLTEKCLNNA IESPGVNARR VPPDLKSNIL KAQVEAVHKV
     TREDSLLSHK NSNVQDAAAN SDILNENNVP FPEDSLALMH TTPATNGSVL KDATDELDAL
     LLSLTENLMD HTVTPQVSST SMITPRWIVP QSGVLSNGLE GLCLAEKEEH GNREVVSLIS
     PPGPFLVDAV TSSVPTLAGE TVLKQKCLLT TEL
//
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