VINC_PIG
ID VINC_PIG Reviewed; 1135 AA.
AC P26234; Q8WMK3;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Vinculin;
DE AltName: Full=Metavinculin;
GN Name=VCL;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Longissimus muscle;
RA Ponsuksili S., Wimmers K., Schmoll F., Schellander K.;
RT "Analysis of porcine vinculin gene as a candidate gene for carcass
RT traits.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 2-21; 244-260; 496-512 AND 852-1006.
RX PubMed=3142762; DOI=10.1002/j.1460-2075.1988.tb03076.x;
RA Gimona M., Small J.V., Moeremans M., van Damme J., Puype M.,
RA Vandekerckhove J.;
RT "Porcine vinculin and metavinculin differ by a 68-residue insert located
RT close to the carboxy-terminal part of the molecule.";
RL EMBO J. 7:2329-2334(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 912-1135 (ISOFORM 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: 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:0000250|UniProtKB:P18206}.
CC -!- SUBUNIT: Exhibits self-association properties. Part of a complex
CC composed of THSD1, PTK2/FAK1, TLN1 and VCL (By similarity). Interacts
CC with APBB1IP, NRAP and TLN1. Interacts with CTNNB1 and this interaction
CC is necessary for its localization to the cell-cell junctions and for
CC its function in regulating cell surface expression of E-cadherin (By
CC similarity). Interacts with SORBS1 (By similarity). Interacts with SYNM
CC (By similarity). Interacts with CTNNA1 (By similarity). Binds to ACTN4;
CC this interaction triggers conformational changes (By similarity).
CC {ECO:0000250|UniProtKB:P12003, ECO:0000250|UniProtKB:P18206,
CC ECO:0000250|UniProtKB:Q64727}.
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}. Note=Recruitment to cell-cell junctions
CC occurs in a myosin II-dependent manner. Interaction with CTNNB1 is
CC necessary for its localization to the cell-cell junctions.
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Metavinculin;
CC IsoId=P26234-1; Sequence=Displayed;
CC Name=1; Synonyms=Vinculin;
CC IsoId=P26234-2; Sequence=VSP_006732;
CC -!- DOMAIN: Exists in at least two conformations. When in the closed,
CC 'inactive' conformation, extensive interactions between the head and
CC tail domains prevent detectable binding to most of its ligands. It
CC takes on an 'active' conformation after cooperative and simultaneous
CC binding of two different ligands. This activation involves displacement
CC of the head-tail interactions and leads to a significant accumulation
CC of ternary complexes. The active form then binds a number of proteins
CC that have both signaling and structural roles that are essential for
CC cell adhesion. {ECO:0000250|UniProtKB:P18206}.
CC -!- DOMAIN: The N-terminal globular head (Vh) comprises of subdomains D1-
CC D4. The C-terminal tail (Vt) binds F-actin and cross-links actin
CC filaments into bundles. An intramolecular interaction between Vh and Vt
CC masks the F-actin-binding domain located in Vt. The binding of talin
CC and alpha-actinin to the D1 subdomain of vinculin induces a helical
CC bundle conversion of this subdomain, leading to the disruption of the
CC intramolecular interaction and the exposure of the cryptic F-actin-
CC binding domain of Vt. Vt inhibits actin filament barbed end elongation
CC without affecting the critical concentration of actin assembly.
CC {ECO:0000250|UniProtKB:P18206}.
CC -!- PTM: Phosphorylated; on serines, threonines and tyrosines.
CC Phosphorylation on Tyr-1134 in activated platelets affects head-tail
CC interactions and cell spreading but has no effect on actin binding nor
CC on localization to focal adhesion plaques (By similarity).
CC {ECO:0000250|UniProtKB:P12003}.
CC -!- PTM: Acetylated; mainly by myristic acid but also by a small amount of
CC palmitic acid. {ECO:0000250|UniProtKB:P12003}.
CC -!- SIMILARITY: Belongs to the vinculin/alpha-catenin family.
CC {ECO:0000305}.
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DR EMBL; AF165172; AAL50327.1; -; mRNA.
DR EMBL; Z19540; CAA79600.1; -; mRNA.
DR PIR; S29507; S29507.
DR RefSeq; NP_999099.1; NM_213934.1. [P26234-2]
DR AlphaFoldDB; P26234; -.
DR SMR; P26234; -.
DR STRING; 9823.ENSSSCP00000010997; -.
DR PaxDb; P26234; -.
DR PeptideAtlas; P26234; -.
DR PRIDE; P26234; -.
DR Ensembl; ENSSSCT00000011289; ENSSSCP00000010997; ENSSSCG00000010313. [P26234-1]
DR Ensembl; ENSSSCT00000087228; ENSSSCP00000065820; ENSSSCG00000010313. [P26234-2]
DR Ensembl; ENSSSCT00070006085; ENSSSCP00070004965; ENSSSCG00070003156. [P26234-2]
DR Ensembl; ENSSSCT00070006104; ENSSSCP00070004983; ENSSSCG00070003156. [P26234-1]
DR GeneID; 396974; -.
DR KEGG; ssc:396974; -.
DR CTD; 7414; -.
DR eggNOG; KOG3681; Eukaryota.
DR GeneTree; ENSGT01030000234543; -.
DR HOGENOM; CLU_012338_0_0_1; -.
DR InParanoid; P26234; -.
DR OMA; ANNLCEL; -.
DR OrthoDB; 270073at2759; -.
DR TreeFam; TF313686; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Reactome; R-SSC-445355; Smooth Muscle Contraction.
DR Reactome; R-SSC-5674135; MAP2K and MAPK activation.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR Proteomes; UP000008227; Chromosome 14.
DR Proteomes; UP000314985; Chromosome 14.
DR Bgee; ENSSSCG00000010313; Expressed in stomach and 44 other tissues.
DR ExpressionAtlas; P26234; baseline and differential.
DR Genevisible; P26234; SS.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISS:AgBase.
DR GO; GO:0044291; C:cell-cell contact zone; IBA:GO_Central.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0043034; C:costamere; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005916; C:fascia adherens; ISS:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0090637; C:inner dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0090636; C:outer dense plaque of desmosome; ISS:AgBase.
DR GO; GO:0005886; C:plasma membrane; ISS:AgBase.
DR GO; GO:0002102; C:podosome; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0042383; C:sarcolemma; ISS:UniProtKB.
DR GO; GO:1990357; C:terminal web; ISS:AgBase.
DR GO; GO:0005915; C:zonula adherens; ISS:AgBase.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0045294; F:alpha-catenin binding; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
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:0007155; P:cell adhesion; ISS:UniProtKB.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
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; ISS:UniProtKB.
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 InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR017997; Vinculin.
DR InterPro; IPR006077; Vinculin/catenin.
DR InterPro; IPR000633; Vinculin_CS.
DR PANTHER; PTHR46180; PTHR46180; 2.
DR Pfam; PF01044; Vinculin; 2.
DR SUPFAM; SSF47220; SSF47220; 6.
DR PROSITE; PS00663; VINCULIN_1; 1.
DR PROSITE; PS00664; VINCULIN_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; Cell adhesion;
KW Cell junction; Cell membrane; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3142762"
FT CHAIN 2..1135
FT /note="Vinculin"
FT /id="PRO_0000064254"
FT REPEAT 259..370
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 371..480
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 481..590
FT /note="3"
FT /evidence="ECO:0000255"
FT REGION 2..836
FT /note="N-terminal globular head"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 168..208
FT /note="Talin-interaction"
FT /evidence="ECO:0000250|UniProtKB:P12003"
FT REGION 259..590
FT /note="3 X 112 AA tandem repeats"
FT /evidence="ECO:0000255"
FT REGION 742..765
FT /note="Interaction with ACTN4"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 837..879
FT /note="Linker (Pro-rich)"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 858..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..1135
FT /note="C-terminal tail"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT REGION 1004..1047
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT REGION 1121..1135
FT /note="Facilitates phospholipid membrane insertion"
FT /evidence="ECO:0000250|UniProtKB:Q64727"
FT COMPBIAS 860..874
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 173
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 497
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 538
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P85972"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 605
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 673
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 722
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 810
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 823
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT MOD_RES 1134
FT /note="Phosphotyrosine; by SRC-type Tyr-kinases"
FT /evidence="ECO:0000250|UniProtKB:P18206"
FT VAR_SEQ 912..979
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_006732"
FT CONFLICT 507
FT /note="N -> H (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 902..903
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 123945 MW; 5B29A4D7DBFD19FF 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 KKDTEAMKRA LASIDSKLNQ AKGWLRDPTA SPGDAGEQAI
RQILDEAGKV GELCAGKERR EILGTCKMLG QMTDQVADLR ARGQGASPVA MQKAQQVSQG
LDVLTAKVEN AARKLEAMTN SKQSIAKKID AAQNWLADPN GGPEGEEQIR GALAEARKIA
ELCDDPKERD DILRSLGEIS ALTSKLADLR RQGKGDSPEA RALAKQVATA LQNLQTKTNR
AVANSRPAKA AVHLEGKIEQ AQRWIDNPTV DDRGVGQAAI RGLVAEGHRL ANVMMGPYRQ
DLLAKCDRVD QLTAQLADLA ARGEGESPQA RALASQLQDS LKDLKARMQE AMTQEVSDVF
SDTTTPIKLL AVAATAPPDA PNREEVFDER AANFENHSGR LGATAEKAAA VGTANKSTVE
GIQASVKTAR ELTPQVVSAA RILLRNPGNQ AAYEHFETMK NQWIDNVEKM TGLVDEAIDT
KSLLDASEEA IKKDLDKCKV AMANIQPQML VAGATSIARR ANRILLVAKR EVENSEDPKF
REAVKAASDE LSKTISPMVM DAKAVAGNIS DPGLQKSFLD SGYRILGAVA KVREAFQPQE
PDFPPPPPDL EQLRLTDELA PPKPPLPEGE VPPPRPPPPE EKDEEFPEQK AGEVINQPMM
MAARQLHDEA RKWSSKPGNP AAKVGIGVVA EADAADAVGF PVPSDMEDDY EPELLLMPSS
QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GTKRALIQCA
KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI
SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
