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Protein

Vinculin

Gene

VCL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.3 Publications

GO - Molecular functioni

  • actin filament binding Source: InterPro
  • alpha-actinin binding Source: AgBase
  • alpha-catenin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • dystroglycan binding Source: Ensembl
  • muscle alpha-actinin binding Source: AgBase
  • protein homodimerization activity Source: AgBase
  • scaffold protein binding Source: AgBase
  • structural molecule activity Source: InterPro
  • ubiquitin protein ligase binding Source: Ensembl
  • vinculin binding Source: AgBase

GO - Biological processi

Keywordsi

Molecular functionActin-binding
Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-GGA-114608 Platelet degranulation
R-GGA-445355 Smooth Muscle Contraction
R-GGA-5674135 MAP2K and MAPK activation
R-GGA-6798695 Neutrophil degranulation
SABIO-RKiP12003

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
Gene namesi
Name:VCL
Synonyms:VINC1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 6

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi100Y → F: Some reduction of phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-1134. 1 Publication1
Mutagenesisi160Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi537Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi692Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi822Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi1134Y → F: Greatly reduced phosphorylation levels in platelets. Little change in cell spreading. Complete loss of phosphorylation. No change in subcellular location nor on in vitro actin binding. 40% decrease in cell spreading; when associated with F-100. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000642552 – 1135VinculinAdd BLAST1134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei100Phosphotyrosine1 Publication1
Modified residuei537PhosphotyrosineCurated1
Modified residuei822PhosphotyrosineBy similarity1
Modified residuei1134Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1

Post-translational modificationi

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1134 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques.1 Publication
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP12003
PRIDEiP12003

PTM databases

iPTMnetiP12003

Expressioni

Tissue specificityi

Isoform Metavinculin is muscle-specific.

Gene expression databases

BgeeiENSGALG00000005079 Expressed in 11 organ(s), highest expression level in colon
ExpressionAtlasiP12003 baseline and differential

Interactioni

Subunit structurei

Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with CTNNB1 and this interaction is necessary for its localization to the cell-cell junctions and for its function in regulating cell surface expression of E-cadherin.4 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi676671, 2 interactors
DIPiDIP-35191N
ELMiP12003
IntActiP12003, 15 interactors
MINTiP12003
STRINGi9031.ENSGALP00000008131

Structurei

Secondary structure

11135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP12003
SMRiP12003
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12003

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati259 – 3691Sequence analysisAdd BLAST111
Repeati370 – 4792Sequence analysisAdd BLAST110
Repeati480 – 5893Sequence analysisAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 835N-terminal globular headBy similarityAdd BLAST834
Regioni168 – 208Talin-interaction1 PublicationAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni836 – 878Linker (Pro-rich)By similarityAdd BLAST43
Regioni879 – 1135C-terminal tailBy similarityAdd BLAST257
Regioni1004 – 1047Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1121 – 1135Facilitates phospholipid membrane insertionBy similarityAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi837 – 878Pro-richPROSITE-ProRule annotationAdd BLAST42

Domaini

Exists in at least two conformations. When in the closed, 'inactive' conformation, extensive interactions between the head and tail domains prevent detectable binding to most of its ligands. It takes on an 'active' conformation after cooperative and simultaneous binding of two different ligands. This activation involves displacement of the head-tail interactions and leads to a significant accumulation of ternary complexes. The active form then binds a number of proteins that have both signaling and structural roles that are essential for cell adhesion.By similarity
The N-terminal globular head (Vh) comprises of subdomains D1-D4. The C-terminal tail (Vt) binds F-actin and cross-links actin filaments into bundles. An intramolecular interaction between Vh and Vt masks the F-actin-binding domain located in Vt. The binding of talin and alpha-actinin to the D1 subdomain of vinculin induces a helical bundle conversion of this subdomain, leading to the disruption of the intramolecular interaction and the exposure of the cryptic F-actin-binding domain of Vt. Vt inhibits actin filament barbed end elongation without affecting the critical concentration of actin assembly.By similarity

Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00550000074411
HOGENOMiHOG000007828
HOVERGENiHBG079758
InParanoidiP12003
KOiK05700
OrthoDBiEOG091G038S
PhylomeDBiP12003

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 8 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 2 (identifier: P12003-2) [UniParc]FASTAAdd to basket
Also known as: Metavinculin

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA
60 70 80 90 100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY
110 120 130 140 150
SVPARDYLID GSRGILSGTS DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV
160 170 180 190 200
VETMEDLVTY TKNLGPGMTK MAKMIDERQQ ELTHQEHRVM LVNSMNTVKE
210 220 230 240 250
LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE INEIIRVLQL
260 270 280 290 300
TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR
310 320 330 340 350
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM
360 370 380 390 400
QKAQQVSQGL DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG
410 420 430 440 450
GSEGEEHIRG IMSEARKVAE LCEEPKERDD ILRSLGEISA LTAKLSDLRR
460 470 480 490 500
HGKGDSPEAR ALAKQIATSL QNLQSKTNRA VANTRPVKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV
660 670 680 690 700
GTANKTTVEG IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANMQPQMLV
760 770 780 790 800
AGATSIARRA NRILLVAKRE VENSEDPKFR EAVKAASDEL SKTISPMVMD
810 820 830 840 850
AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP DFPPPPPDLE
860 870 880 890 900
HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY
960 970 980 990 1000
EPELLLMPTN QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA
1010 1020 1030 1040 1050
EMSRLVRGGS GNKRALIQCA KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL
1060 1070 1080 1090 1100
LQVCERIPTI STQLKILSTV KATMLGRTNI SDEESEQATE MLVHNAQNLM
1110 1120 1130
QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
Length:1,135
Mass (Da):124,560
Last modified:January 23, 2007 - v4
Checksum:i28CC2699C9511058
GO
Isoform 1 (identifier: P12003-1) [UniParc]FASTAAdd to basket
Also known as: Vinculin

The sequence of this isoform differs from the canonical sequence as follows:
     916-984: Missing.

Show »
Length:1,066
Mass (Da):116,999
Checksum:i6F585201260BA47F
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1NYY0F1NYY0_CHICK
Vinculin
VCL
1,135Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti442 – 447TAKLSD → QLSCQI (PubMed:2497736).Curated6
Sequence conflicti442 – 447TAKLSD → QLSCQI in CAA68412 (PubMed:3117046).Curated6
Sequence conflicti701Q → H (PubMed:2497736).Curated1
Sequence conflicti701Q → H in CAA68412 (PubMed:3117046).Curated1
Sequence conflicti880E → K in CAA68412 (PubMed:3117046).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010772916 – 984Missing in isoform 1. 2 PublicationsAdd BLAST69

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04126 mRNA Translation: AAA49136.1
M87837 Genomic DNA Translation: AAA49135.1
Y00312 mRNA Translation: CAA68412.1
PIRiA31346 A29997
RefSeqiNP_990772.1, NM_205441.1 [P12003-1]
XP_015143689.1, XM_015288203.1 [P12003-2]
UniGeneiGga.15976
Gga.698

Genome annotation databases

EnsembliENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079 [P12003-2]
ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079 [P12003-1]
GeneIDi396422
KEGGigga:396422

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04126 mRNA Translation: AAA49136.1
M87837 Genomic DNA Translation: AAA49135.1
Y00312 mRNA Translation: CAA68412.1
PIRiA31346 A29997
RefSeqiNP_990772.1, NM_205441.1 [P12003-1]
XP_015143689.1, XM_015288203.1 [P12003-2]
UniGeneiGga.15976
Gga.698

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QKRX-ray1.80A/B879-1135[»]
1ST6X-ray3.10A1-1135[»]
1T01X-ray2.06A1-254[»]
1U6HX-ray2.38A1-259[»]
1XWJX-ray2.60A2-259[»]
1ZVZX-ray1.80A2-259[»]
1ZW2X-ray2.10A2-259[»]
1ZW3X-ray3.30A2-259[»]
2GDCX-ray2.74A1-266[»]
3JBIelectron microscopy8.50V879-1130[»]
3ZDLX-ray2.30A1-259[»]
4E17X-ray2.30A1-259[»]
4E18X-ray2.40A1-259[»]
6FQ4X-ray2.89A1-259[»]
ProteinModelPortaliP12003
SMRiP12003
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676671, 2 interactors
DIPiDIP-35191N
ELMiP12003
IntActiP12003, 15 interactors
MINTiP12003
STRINGi9031.ENSGALP00000008131

PTM databases

iPTMnetiP12003

Proteomic databases

PaxDbiP12003
PRIDEiP12003

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079 [P12003-2]
ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079 [P12003-1]
GeneIDi396422
KEGGigga:396422

Organism-specific databases

CTDi7414

Phylogenomic databases

eggNOGiKOG3681 Eukaryota
ENOG410XSRU LUCA
GeneTreeiENSGT00550000074411
HOGENOMiHOG000007828
HOVERGENiHBG079758
InParanoidiP12003
KOiK05700
OrthoDBiEOG091G038S
PhylomeDBiP12003

Enzyme and pathway databases

ReactomeiR-GGA-114608 Platelet degranulation
R-GGA-445355 Smooth Muscle Contraction
R-GGA-5674135 MAP2K and MAPK activation
R-GGA-6798695 Neutrophil degranulation
SABIO-RKiP12003

Miscellaneous databases

EvolutionaryTraceiP12003
PROiPR:P12003

Gene expression databases

BgeeiENSGALG00000005079 Expressed in 11 organ(s), highest expression level in colon
ExpressionAtlasiP12003 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR036723 Alpha-catenin/vinculin-like_sf
IPR017997 Vinculin
IPR006077 Vinculin/catenin
IPR000633 Vinculin_CS
PANTHERiPTHR18914 PTHR18914, 3 hits
PTHR18914:SF1 PTHR18914:SF1, 3 hits
PfamiView protein in Pfam
PF01044 Vinculin, 3 hits
SUPFAMiSSF47220 SSF47220, 8 hits
PROSITEiView protein in PROSITE
PS00663 VINCULIN_1, 1 hit
PS00664 VINCULIN_2, 3 hits
ProtoNetiSearch...

Entry informationi

Entry nameiVINC_CHICK
AccessioniPrimary (citable) accession number: P12003
Secondary accession number(s): Q91024
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: September 12, 2018
This is version 172 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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