ID M3XW73_MUSPF Unreviewed; 1134 AA.
AC M3XW73;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Vinculin {ECO:0000256|ARBA:ARBA00014125};
DE AltName: Full=Metavinculin {ECO:0000256|ARBA:ARBA00033411};
GN Name=VCL {ECO:0000313|Ensembl:ENSMPUP00000003323.1,
GN ECO:0000313|RefSeq:XP_004769427.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000003323.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000003323.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004769427.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004769427.1};
RG RefSeq;
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; AEYP01073171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073172; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073177; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01073180; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004769427.1; XM_004769370.3.
DR STRING; 9669.ENSMPUP00000003323; -.
DR Ensembl; ENSMPUT00000003388.1; ENSMPUP00000003323.1; ENSMPUG00000003355.1.
DR GeneID; 101679725; -.
DR KEGG; mpuf:101679725; -.
DR CTD; 7414; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_012338_0_0_1; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 2908505at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0043034; C:costamere; IEA:Ensembl.
DR GO; GO:0005916; C:fascia adherens; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:Ensembl.
DR GO; GO:0061826; C:podosome ring; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045294; F:alpha-catenin binding; IEA:Ensembl.
DR GO; GO:0002162; F:dystroglycan binding; IEA:Ensembl.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0034333; P:adherens junction assembly; IEA:Ensembl.
DR GO; GO:0043297; P:apical junction assembly; IEA:Ensembl.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEA:Ensembl.
DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR GO; GO:0030334; P:regulation of cell migration; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IEA:Ensembl.
DR GO; GO:1904702; P:regulation of protein localization to adherens junction; IEA:Ensembl.
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; 7.
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:UP000000715};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REGION 858..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 859..873
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 123893 MW; 109F0E807861FDE5 CRC64;
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNSKN QGIEEALKNR NFTVEKMSAE
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPSAS PGDAGEQAIR
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALTEARKIAE
LCDDPKERDD ILRSLGEISA LTSKLADLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTRMQEA MTQEVSDVFS
DTTTPIKLLA VAATAPPDAP SREEVFDERA ANFEHHSGRL GATAEKAAAV GTANKATVEG
IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK
SLLDASEEAI KKDLDKCKVA MANIQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP
DFPPPPPDLE QLRLADELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
AARQLHDEAR KWSSKPGNRA AEVGVGVVAE ADAADAVGFP VPPDMEDDFE PELLLMPSNQ
PVNQPILAAA QSLHREATKW SSKGNDIIAA AKRMALLMAE MSRLVRGGSG TKRALIQCAK
DIAKASDEVT RLAKEVAKQC TDKRIRTNLL QVCERIPTIS TQLKILSTVK ATMLGRTNIS
DEESEQATEM LVHNAQNLMQ SVKETVREAE AASIKIRTDA GFTLRWVRKT PWYQ
//
