GenomeNet

Database: UniProt
Entry: A0A3Q7T7W6_VULVU
LinkDB: A0A3Q7T7W6_VULVU
Original site: A0A3Q7T7W6_VULVU 
ID   A0A3Q7T7W6_VULVU        Unreviewed;      1553 AA.
AC   A0A3Q7T7W6;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Band 4.1-like protein 1 isoform X8 {ECO:0000313|RefSeq:XP_025865558.1};
GN   Name=EPB41L1 {ECO:0000313|RefSeq:XP_025865558.1};
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_025865558.1};
RN   [1]
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (JAN-2019) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_025865558.1}
RP   IDENTIFICATION.
RC   STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025865558.1};
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_025865558.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_025865558.1; XM_026009773.1.
DR   Proteomes; UP000286640; 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   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:UP000286640}.
FT   DOMAIN          100..381
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          1..67
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          517..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          747..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1019..1132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1213..1321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1371..1421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        450..504
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..541
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        812..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        842..857
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..872
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        926..940
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1116..1132
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1309
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1371..1385
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1553 AA;  171062 MW;  086919AADD8000BC CRC64;
     MTTETGPDSE VKKAQEEAPQ QPEAAATAAA TTPVTPAGHG GHPEANSNEK HPPQQDTRPA
     EQSLDMEEKG YGEADGLSER TTPSRAQKSP QKIAKKYKSA ICRVTLLDAS EYECEVEKHG
     RGQVLFDLVC EHLNLLEKDY FGLTFCDADS QKNWLDPSKE IKKQIRSSPW NFAFTVKFYP
     PDPAQLTEDI TRYYLCLQLR ADIITGRLPC SFVTHALLGS YAVQAELGDY DAEEHIGNYV
     SELRFAPNQT RELEERIMEL HKTYRGMTPG EAEIHFLENA KKLSMYGVDL HHAKDSEGID
     IMLGVCANGL LIYRDRLRIN RFAWPKILKI SYKRSNFYIK IRPGEYEQFE STIGFKLPNH
     RSAKRLWKVC IEHHTFFRLV SPEPPPKGFL VMGSKFRYSG RTQAQTRQAS ALIDRPAPFF
     ERSSSKRYTM SRSLDGAEFS RPASVSENHD TGPDGDKPEE DGESGGRRSE AEEGEVRTPT
     KIKELKPEQE TTPRHKQEFL DKPEDVLLKH QASINELKRT LKEPNSKLIH RDRDWERERR
     LPSSPASPSP KGTPEKANES QRTQDTSPQD LAPEPGTATG WEVFTQKSLA ASPEGSEHWV
     FIEREYTRPE ERLKVATTQQ EGSKTGLEDI LADGRLSKVD VLVDKFKVEV ATEETVGVRR
     AKTQQQGRMI ASPEDFESVW EEGPWVRKGP GGASLAAGCT PAENLLEGSQ LRVGTGEAAI
     KKRWISGGQL EGQMELRKEL EEFQAWGRPA ASGSRSAEAD VPSPASDKGG LQSFLLDPAQ
     SEARGDSSDE TEPSFAERSF YLNYGEKDSE DQVLPPPLEK REEHSDALPV DDTRLELSDK
     LTESSELISL DLQDSAAASS RNKDEEGKTH TASLEEGAGS PKNHGRPDGL EASVEQLGKG
     PSPEQTFAED WEEAGRGVEG ECSHPASKIG TEEKAEKNPP TGWKNHSPHR GGGMCPDLPA
     CTLPQAIPPN DVRKPAKPDR SNFLPQDRGL VHIQTGEPAM EDRKASAFLQ MEVIAPLPAS
     PGPFQAQAAP EETFPSPAPR GSGEPLQLWD RDPFGEQSPV FPKHAHPLKE SPEPKDRIGP
     LVTPDGGERR APPVASRKPR FVSEEAEGAV PPSGKQREMT SFQARGQEGS LEDISKTSVA
     NKIRIFETHG AETRRASQGE TRALINELSS EASTGQVEQQ RNKLLDLGFV QLQPPGDFTG
     PKATHSSVMP LATRHFREDT SHQEGCTEPV SPDSGCETAL EETPGGAGHN KSGDAVREEK
     HISNLAANPP GKGGHLRFAS PLGPQRAGLR EGSEEKVKPP RPRAPESDTG DEDQDQERDA
     VFLKDNHLAI ERKCSSITVS STSSLEAEVD FTVIGDYHGS AFEDFSRSLP ELDRDKSDSE
     TEGLVFSRDL SKGGPSQEDE SGGIEDSPDR GACATPDMPQ FEPVKTETMT VSSLAIRKKI
     EPEAVLQTRI TTMDTTQQVD GTAPGGKESI TTAPSITTET ISTTMTVKGG FSETRIEKRI
     IITGDEDVDQ DQALALAIKE AKLQHPDMLV TKAVVYRETD PSPEDRDRKP QES
//
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