VINC_XENLA
ID VINC_XENLA Reviewed; 235 AA.
AC Q04615;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Vinculin;
DE AltName: Full=Metavinculin;
DE Flags: Fragment;
GN Name=vcl;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=8425604; DOI=10.1016/0014-5793(93)81274-4;
RA Strasser P., Gimona M., Herzog M., Geiger B., Small J.V.;
RT "Variable and constant regions in the C-terminus of vinculin and
RT metavinculin. Cloning and expression of fragments in E. coli.";
RL FEBS Lett. 317:189-194(1993).
CC -!- FUNCTION: Involved in cell adhesion. May be involved in the attachment
CC of the actin-based microfilaments to the plasma membrane.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- SUBUNIT: Exhibits self-association properties.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12003};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q64727}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Metavinculin;
CC IsoId=Q04615-1; Sequence=Displayed;
CC Name=1; Synonyms=Vinculin;
CC IsoId=Q04615-2; Sequence=VSP_006733;
CC -!- PTM: Phosphorylated on serines, threonines and tyrosines.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- PTM: Acetylated by myristic acid and/or palmitic acid.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- MISCELLANEOUS: [Isoform 2]: Differs from vinculin by the insertion of a
CC 68 residues domain near the C-terminus.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; Z19541; CAA79601.1; -; mRNA.
DR PIR; S29508; S29508.
DR AlphaFoldDB; Q04615; -.
DR SMR; Q04615; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR PANTHER; PTHR46180; PTHR46180; 1.
DR Pfam; PF01044; Vinculin; 1.
DR SUPFAM; SSF47220; SSF47220; 1.
PE 2: Evidence at transcript level;
KW Actin-binding; Alternative splicing; Cell adhesion; Cell junction;
KW Cell membrane; Cytoplasm; Cytoskeleton; Lipoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN <1..235
FT /note="Vinculin"
FT /id="PRO_0000064256"
FT VAR_SEQ 7..84
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:8425604"
FT /id="VSP_006733"
FT NON_TER 1
SQ SEQUENCE 235 AA; 26150 MW; 7B545A46E290147E CRC64;
KWSSKSPGNY DYPAPQGREA VISEVEQAQE EEEEEASVEF ALSSDIEDDY EPELLLVPEG
QPVNQPMLAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA
KDIAKASDEV TKLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI
SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWARK TPWYQ
