ID A0A4W2F233_BOBOX Unreviewed; 726 AA.
AC A0A4W2F233;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-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|Ensembl:ENSBIXP00000043459.1};
OS Bos indicus x Bos taurus (Hybrid cattle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=30522 {ECO:0000313|Ensembl:ENSBIXP00000043459.1, ECO:0000313|Proteomes:UP000314981};
RN [1] {ECO:0000313|Proteomes:UP000314981, ECO:0000313|Proteomes:UP000429181}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Low W.Y., Tearle R., Bickhart D.M., Rosen B.D., Koren S., Rhie A.,
RA Hiendleder S., Phillippy A.M., Smith T.P.L., Williams J.L.;
RT "Haplotype-resolved cattle genomes.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBIXP00000043459.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 30522.A0A4W2F233; -.
DR Ensembl; ENSBIXT00000042172.1; ENSBIXP00000043459.1; ENSBIXG00000027570.1.
DR Ensembl; ENSBIXT00005003304.1; ENSBIXP00005006986.1; ENSBIXG00005001310.1.
DR GeneTree; ENSGT00940000156332; -.
DR Proteomes; UP000314981; Chromosome 2.
DR Proteomes; UP000429181; Chromosome 2.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0032587; C:ruffle membrane; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0031032; P:actomyosin structure organization; IEA:Ensembl.
DR GO; GO:0003383; P:apical constriction; IEA:Ensembl.
DR GO; GO:0048319; P:axial mesoderm morphogenesis; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0007398; P:ectoderm development; IEA:Ensembl.
DR GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
DR GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0070986; P:left/right axis specification; IEA:Ensembl.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IEA:Ensembl.
DR GO; GO:0022408; P:negative regulation of cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0001839; P:neural plate morphogenesis; IEA:Ensembl.
DR GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0051894; P:positive regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:Ensembl.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; IEA:Ensembl.
DR GO; GO:0006931; P:substrate-dependent cell migration, cell attachment to substrate; IEA:Ensembl.
DR GO; GO:0009826; P:unidimensional cell growth; IEA:Ensembl.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13186; FERM_C_NBL4_NBL5; 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:UP000314981}.
FT DOMAIN 43..327
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 359..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 80751 MW; 1B5CD440B839FEDE 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 KKCLPLKLDL LDSPDLLETT INEVAGAPDT MDTSQAPGEV
STATRQAGLE GPEGECRTFI DASEKLKHLE MENSPVPAPH PNVDVNINNQ EEVVKLTEKC
LNNAIDSPAL NTRRVPPDLK SNILKAQVEA VQKVTREDRV LSHKNASVQD ASTDSAELNE
NTVPVRGDSL ALMQTTPAES GSALKDATDE LDALLLSLTE NLLDHTTIPQ VSSTSVITPR
WIVPQSTVLP NGLAGNGFSL TGKEGLGSRE LISPPAPFLV DAVTSSAPAS AGEATLKQKC
LLTTEL
//
