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Database: UniProt
Entry: A0A1S3W5G3_ERIEU
LinkDB: A0A1S3W5G3_ERIEU
Original site: A0A1S3W5G3_ERIEU 
ID   A0A1S3W5G3_ERIEU        Unreviewed;       921 AA.
AC   A0A1S3W5G3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Band 4.1-like protein 1 isoform X5 {ECO:0000313|RefSeq:XP_016041621.1};
GN   Name=EPB41L1 {ECO:0000313|RefSeq:XP_016041621.1};
OS   Erinaceus europaeus (Western European hedgehog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Eulipotyphla; Erinaceidae; Erinaceinae;
OC   Erinaceus.
OX   NCBI_TaxID=9365 {ECO:0000313|Proteomes:UP000079721, ECO:0000313|RefSeq:XP_016041621.1};
RN   [1] {ECO:0000313|RefSeq:XP_016041621.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_016041621.1; XM_016186135.1.
DR   AlphaFoldDB; A0A1S3W5G3; -.
DR   CTD; 2036; -.
DR   OrthoDB; 5391231at2759; -.
DR   Proteomes; UP000079721; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030866; P:cortical actin cytoskeleton organization; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13184; FERM_C_4_1_family; 1.
DR   CDD; cd17201; FERM_F1_EPB41L1; 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; IPR008379; Band_4.1_C.
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; IPR007477; SAB_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR   PANTHER; PTHR23280:SF24; BAND 4.1-LIKE PROTEIN 1; 1.
DR   Pfam; PF05902; 4_1_CTD; 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   Pfam; PF04382; SAB; 1.
DR   PIRSF; PIRSF002304; Membrane_skeletal_4_1; 2.
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   Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW   Reference proteome {ECO:0000313|Proteomes:UP000079721}.
FT   DOMAIN          97..378
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..727
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..538
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        547..571
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..691
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..712
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   921 AA;  102513 MW;  0DEC9DA67FCF4AB8 CRC64;
     MTTETGPDSD VKKAQEEAPQ QPEAAAAATT PVTPIGHGHL EANSNEKHPP QQDARPMEQS
     LDMEEKDYSE ADGLSERTTP SKAQKSPQKI AKKYKSTICR VTLLDASEYE CEVEKHGRGQ
     VLFDLVCEHL NLLEKDYFGL TFCDADSQKN WLDPSKEIKK QIRSSPWNFA FTVKFYPPDP
     AQLTEDITRY YLCLQLRADI ITGRLPCSFV THALLGSYAV QAELGDYDTE EHVGNYVSEL
     RFAPNQTREL EERIMELHKT YRGMTPGEAE IHFLENAKKL SMYGVDLHHA KDSEGIDIML
     GVCANGLLIY RDRLRINRFA WPKILKISYK RSNFYIKIRP GEYEQFESTI GFKLPNHRSA
     KRLWKVCIEH HTFFRLVSPE PPPKGFLVMG SKFRYSGRTQ AQTRQASALI DRPAPFFERS
     SSKRYTMSRS LDGAEFSRPA SVSENHDSGP DGDKLEEDGE SGGRRSEAEE GEVRTPTKIK
     DLKPEQETTP RHKQEFLDKP EDVLLKHQAS INELKRTLKE PNSKLIHRDR DWERERRLPS
     SPASPSPKGT PEKASESQMT QDSSQQDLAP EPGTATGLEV LTQKSLTASP ERAGLREGSE
     EKVKLPRPRA PESDTGDEDQ DQERDAVFLK DNHLAIERKC SSITVSSTSS LEAEVDFTVI
     GDYHGSAFED FSRSLPELDQ DKSDSETEGL VFSHDLNKGV SSHDDESGGI EDSPDRGACS
     TPDMPQFEPV KTETMTVSSL AIRKKIEPEA ILQTRVAAVD TTQAASGQQV DGAAPGGKEF
     MTTTPSITTE TISTTMDNSL KSGKGAAAMI PGPQTVATEI RSLSPIIGKD VLTSTYGATA
     ETLSTSTTTH VTKTVKGGFS ETRIEKRIII TGDEDVDQDQ ALALAIKEAK LQHPDMLVTK
     AVVYRETDPS PEERDKKPQE S
//
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