ID A0A1L8EVD0_XENLA Unreviewed; 752 AA.
AC A0A1L8EVD0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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.L {ECO:0000313|RefSeq:XP_018089555.1,
GN ECO:0000313|RefSeq:XP_018089556.1, ECO:0000313|RefSeq:XP_041431435.1,
GN ECO:0000313|Xenbase:XB-GENE-962306};
GN Synonyms=epb4.1l5 {ECO:0000313|RefSeq:XP_018089556.1,
GN ECO:0000313|RefSeq:XP_041431435.1}, epb41l5
GN {ECO:0000313|RefSeq:XP_018089556.1,
GN ECO:0000313|RefSeq:XP_041431435.1}, lulu
GN {ECO:0000313|RefSeq:XP_018089555.1, ECO:0000313|RefSeq:XP_018089556.1,
GN ECO:0000313|RefSeq:XP_041431435.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018089555.1};
RN [1] {ECO:0000313|RefSeq:XP_018089555.1, ECO:0000313|RefSeq:XP_018089556.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018089555.1,
RC ECO:0000313|RefSeq:XP_018089556.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018089555.1,
RC ECO:0000313|RefSeq:XP_018089556.1};
RG RefSeq;
RL Submitted (APR-2022) 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_018089555.1; XM_018234066.2.
DR RefSeq; XP_018089556.1; XM_018234067.2.
DR RefSeq; XP_041431435.1; XM_041575501.1.
DR STRING; 8355.A0A1L8EVD0; -.
DR PaxDb; 8355-A0A1L8EVD0; -.
DR GeneID; 379926; -.
DR AGR; Xenbase:XB-GENE-962306; -.
DR CTD; 379926; -.
DR Xenbase; XB-GENE-962306; epb41l5.L.
DR OMA; GRDENEY; -.
DR OrthoDB; 3682543at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 379926; Expressed in lung and 19 other cell types or tissues.
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:UP000186698}.
FT DOMAIN 43..327
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 350..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 752 AA; 84649 MW; DF20814F6441C4D1 CRC64;
MLSFFRRTLG RRSMRRHAEK ERLREAQRAT THIPAAGDTR SIITCRVSLL DGSDVSVDLP
KKAEGQELFE QIMYHLDLIE KDYFGLQFMD SAQVPHWLDN TKSIKKQVKI GPPYCLHLRV
KFYSSEPNNL REELTRYLFV LQLKQDILSG KLDCSFDTAV QLAAYSLQGE LGDYDPAEHT
PDLVSEFRFI PTQSEEFEFA VLGKWKDFRG QTPAEAETNY LNKAKWLEMY GVDMHMVKAR
DDNDYQLGLT PTGVLVFEGE TKIGLFFWPK ITRLDFKKSK LTLVVVEDDE QGKEQEHTFV
FKMDHPKACK HLWKCAVEHH AFFRLRSPTH KTSSRSGFIR LGSRFRYSGK TEYQTTKSSK
PRRSSSFERR PSKRYSRRTL QMRGQAQRPE FTRFQRDQPG QNKGSQQAWP SNPSVPPSGS
ALLEIQNLTR SPGAGQGDRC FVGLANSKDL LESNLDDVMT VSQGPAPLPD AITMTFTNPD
ETVLELGNLA SGTEDVTVKR NNLEADAVTT HPIWANMNIN VNNQEETVKL PEKLLNNSVE
SAGPPPVWLT TDIKSNILKA QVEAGHKLTR EDLELDDKNK TPEESSARSI TVKVNNNLST
PLSWEMPLFR DSQDPKANFF IKNVLSAERE SSRSEFPEIP PFITPPEEVV DIKSPTEDLD
NLIASLTENL IDLTDVPPKV PSYTTVTPRW LVPQSSAVSN GLLGGEMTTS NDPERLPALT
DSLDLTATPT GSVSTGDPGG LPKPKCLLTT EL
//
