ID W5PFI7_SHEEP Unreviewed; 1069 AA.
AC W5PFI7;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Vinculin {ECO:0000256|ARBA:ARBA00014125};
DE AltName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
GN Name=VCL {ECO:0000313|Ensembl:ENSOARP00000009202.1};
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940 {ECO:0000313|Ensembl:ENSOARP00000009202.1, ECO:0000313|Proteomes:UP000002356};
RN [1] {ECO:0000313|Ensembl:ENSOARP00000009202.1, ECO:0000313|Proteomes:UP000002356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Texel {ECO:0000313|Ensembl:ENSOARP00000009202.1,
RC ECO:0000313|Proteomes:UP000002356};
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2] {ECO:0000313|Ensembl:ENSOARP00000009202.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Actin filament (F-actin)-binding protein involved in cell-
CC matrix adhesion and cell-cell adhesion. Regulates cell-surface E-
CC cadherin expression and potentiates mechanosensing by the E-cadherin
CC complex. May also play important roles in cell morphology and
CC locomotion. {ECO:0000256|ARBA:ARBA00024757}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}. Cell membrane, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004278}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004278}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004278}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004413}. Cell projection, podosome
CC {ECO:0000256|ARBA:ARBA00004188}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000256|ARBA:ARBA00008376}.
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DR EMBL; AMGL01071517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AMGL01071519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5PFI7; -.
DR SMR; W5PFI7; -.
DR STRING; 9940.ENSOARP00000009202; -.
DR PaxDb; 9940-ENSOARP00000009202; -.
DR Ensembl; ENSOART00000009336.1; ENSOARP00000009202.1; ENSOARG00000008576.1.
DR eggNOG; KOG3681; Eukaryota.
DR HOGENOM; CLU_012338_0_0_1; -.
DR OMA; ANNLCEL; -.
DR Proteomes; UP000002356; Chromosome 25.
DR Bgee; ENSOARG00000008576; Expressed in thyroid gland and 55 other cell types or tissues.
DR ExpressionAtlas; W5PFI7; baseline.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 2.
DR Gene3D; 1.20.120.810; Vinculin, Vh2 four-helix bundle; 3.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR46180; VINCULIN; 1.
DR PANTHER; PTHR46180:SF1; VINCULIN; 1.
DR Pfam; PF01044; Vinculin; 2.
DR PRINTS; PR00806; VINCULIN.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 6.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 2.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889};
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000002356};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 788..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 289..316
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 790..804
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1069 AA; 116697 MW; 489F8640A5AB4770 CRC64;
MPPAFIKVEN ACTKLVQAAQ MLQSDPYSVP ARDYLIDGSR GILSGTSDLL LTFDEAEVRK
IIRVCKGILE YLTVAEVVET MEDLVTYTKN LGPGMTKMAK MIDERQQELT HQEHRVMLVN
SMNTVKELLP VLISAMKIFV TTKNSKNQGI EEALKNRNFT VEKMSAEINE IIRVLQLTSW
DEDAWASKKD TEAMKRALAS IDSKLNQAKG WLRDPNASPG DAGEQAIRQI LDEAGKVGEL
CAGKERREIL GTCKMLGQMT DQVADLRASR GQGASPVAMQ KAQQVSQGLD VLTAKVENAA
RKLEAMTNSK QSIAKKIDAA QNWLADPNGG PEGEEQIRGA LAEARKIAEL CDDPKERDDI
LRSLGEISAL TSKLGDLRRQ GKGDSPEARA LAKQVATALQ NLQTKTNRAV ANSRPAKAAV
HLEGKIEQAQ RWIDNPTVDD RGVGTGQAAI RGLVAEGHRL ANVMMGPYRQ DLLAQCDRVD
QLTAQLADLA ARGEGESPQA RALASQLQDS LKDLKARMQE AMTQEVSDVF SDTTTPIKLL
AVAATAPPDA PNREEVFDER AANFENHSGR LGATAEKAAA VGTANKSTVE GIQASVKTAR
ELTPQVVSAA RILLRNPGNQ AAYEHFETMK NQWIDNVEKM TGLVDEAIDT KSLLDASEEA
IKKDLDKCKV AMANIQPQML VAGATSIARR ANRILLVAKR EVENSEDPKF REAVKAASDE
LSKTISPMVV DAKAVAGNIS DPGLQKSFLD SGYRILGAVA KVREAFQPQE PDFPPPPPDL
EQLRLTDELA PPKPPLPEGE VPPPRPPPPE EKDEEFPEQK AGEVINQPMM MAARQLHDEA
RKWSSKPSTK PGNPAAKVGI SVVAEAEAAD AVGFPVPPDM EDDYEPELLL MPSNQPVNQP
ILAAAQSLHR EATKWSSKGN DIIAAAKRMA LLMAEMSRLV RGGSGTKRAL IQCAKDIAKA
SDEVTRLAKE VAKQCTDKRI RTNLLQVCER IPTISTQLKI LSTVKATMLG RTNISDEESE
QATEMLVHNA QNLMQSVKET VREAEAASIK IRTDAGFTLR WVRKTPWYQ
//
