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Protein

Vinculin

Gene

VCL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • alpha-actinin binding Source: AgBase
  • alpha-catenin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • muscle alpha-actinin binding Source: AgBase
  • protein homodimerization activity Source: AgBase
  • scaffold protein binding Source: AgBase
  • structural molecule activity Source: InterPro
  • vinculin binding Source: AgBase

GO - Biological processi

  • adherens junction assembly Source: BHF-UCL
  • apical junction assembly Source: Ensembl
  • axon extension Source: Ensembl
  • epithelial cell-cell adhesion Source: BHF-UCL
  • lamellipodium assembly Source: UniProtKB
  • morphogenesis of an epithelium Source: BHF-UCL
  • platelet aggregation Source: Ensembl
  • protein localization to cell surface Source: Ensembl
  • regulation of cell migration Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SABIO-RKP12003.

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: Unplaced

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: AgBase
  • adherens junction Source: UniProtKB
  • brush border Source: AgBase
  • cell Source: AgBase
  • cell-cell junction Source: UniProtKB
  • costamere Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • fascia adherens Source: Ensembl
  • focal adhesion Source: UniProtKB
  • inner dense plaque of desmosome Source: AgBase
  • mitochondrial inner membrane Source: UniProtKB
  • muscle tendon junction Source: AgBase
  • neuromuscular junction Source: AgBase
  • outer dense plaque of desmosome Source: AgBase
  • plasma membrane Source: AgBase
  • protein complex Source: Ensembl
  • sarcolemma Source: AgBase
  • skeletal muscle myofibril Source: AgBase
  • stress fiber Source: AgBase
  • terminal web Source: AgBase
  • Z disc Source: AgBase
  • zonula adherens Source: AgBase
Complete GO annotation...

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 residuei537PhosphotyrosineSequence analysis1
Modified residuei822PhosphotyrosineSequence analysis1
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.

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ACTN1P05094-25EBI-1039563,EBI-6049246
PXNP490245EBI-1039563,EBI-2896280
Tln1P260393EBI-1039563,EBI-1039593From a different organism.
VASPP505522EBI-1039563,EBI-748201From a different organism.

GO - Molecular functioni

  • alpha-actinin binding Source: AgBase
  • alpha-catenin binding Source: BHF-UCL
  • beta-catenin binding Source: BHF-UCL
  • cadherin binding Source: BHF-UCL
  • muscle alpha-actinin binding Source: AgBase
  • protein homodimerization activity Source: AgBase
  • scaffold protein binding Source: AgBase
  • vinculin binding Source: AgBase

Protein-protein interaction databases

BioGridi676671. 2 interactors.
DIPiDIP-35191N.
IntActiP12003. 12 interactors.
STRINGi9031.ENSGALP00000008131.

Structurei

Secondary structure

11135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 28Combined sources22
Turni29 – 32Combined sources4
Beta strandi33 – 35Combined sources3
Helixi41 – 63Combined sources23
Helixi68 – 73Combined sources6
Helixi75 – 97Combined sources23
Helixi102 – 146Combined sources45
Helixi148 – 150Combined sources3
Helixi154 – 181Combined sources28
Helixi185 – 215Combined sources31
Beta strandi218 – 221Combined sources4
Helixi222 – 249Combined sources28
Helixi253 – 255Combined sources3
Helixi256 – 275Combined sources20
Helixi277 – 285Combined sources9
Turni292 – 295Combined sources4
Helixi296 – 311Combined sources16
Helixi318 – 338Combined sources21
Turni339 – 342Combined sources4
Helixi347 – 395Combined sources49
Helixi405 – 421Combined sources17
Helixi428 – 451Combined sources24
Helixi457 – 482Combined sources26
Helixi493 – 505Combined sources13
Helixi516 – 531Combined sources16
Helixi535 – 556Combined sources22
Helixi567 – 598Combined sources32
Helixi604 – 614Combined sources11
Helixi622 – 650Combined sources29
Helixi654 – 681Combined sources28
Turni682 – 684Combined sources3
Helixi689 – 714Combined sources26
Helixi719 – 739Combined sources21
Beta strandi742 – 744Combined sources3
Turni746 – 748Combined sources3
Helixi752 – 772Combined sources21
Helixi777 – 802Combined sources26
Beta strandi803 – 806Combined sources4
Turni809 – 813Combined sources5
Helixi814 – 817Combined sources4
Turni818 – 823Combined sources6
Helixi824 – 835Combined sources12
Beta strandi887 – 890Combined sources4
Helixi892 – 895Combined sources4
Helixi897 – 909Combined sources13
Helixi987 – 1005Combined sources19
Helixi1010 – 1012Combined sources3
Helixi1013 – 1040Combined sources28
Helixi1044 – 1054Combined sources11
Helixi1057 – 1074Combined sources18
Beta strandi1075 – 1077Combined sources3
Helixi1082 – 1113Combined sources32
Helixi1121 – 1123Combined sources3

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[»]
DisProtiDP00556.
ProteinModelPortaliP12003.
SMRiP12003.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12003.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 835N-terminal globular headBy similarityAdd BLAST834
Regioni168 – 208Talin-interactionAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsAdd 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-richAdd 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).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).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

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 5 hits.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 8 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]

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

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

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

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[»]
DisProtiDP00556.
ProteinModelPortaliP12003.
SMRiP12003.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi676671. 2 interactors.
DIPiDIP-35191N.
IntActiP12003. 12 interactors.
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

SABIO-RKP12003.

Miscellaneous databases

EvolutionaryTraceiP12003.
PROiP12003.

Gene expression databases

BgeeiENSGALG00000005079.

Family and domain databases

InterProiIPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 5 hits.
PfamiPF01044. Vinculin. 3 hits.
[Graphical view]
SUPFAMiSSF47220. SSF47220. 8 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVINC_CHICK
AccessioniPrimary (citable) accession number: P12003
Secondary accession number(s): Q91024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 160 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.