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P12003 (VINC_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vinculin
Alternative name(s):
Metavinculin
Gene names
Name:VCL
Synonyms:VINC1
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length1135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.9 Ref.10

Subunit structure

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. Ref.6 Ref.7 Ref.10 Ref.12

Subcellular location

Cytoplasmcytoskeleton. Cell junctionadherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Note: Cytoplasmic face of adhesion plaques. Recruitment to cell-cell junctions occurs in a myosin II-dependent manner. Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions. Ref.9 Ref.10

Tissue specificity

Isoform Metavinculinis muscle-specific.

Domain

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. Ref.6

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. Ref.6

Post-translational modification

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. Ref.8

Acetylated; mainly by myristic acid but also by a small amount of palmitic acid. Ref.5

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandActin-binding
   PTMLipoprotein
Myristate
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction assembly

Inferred from direct assay Ref.10. Source: BHF-UCL

apical junction assembly

Inferred from electronic annotation. Source: Ensembl

epithelial cell-cell adhesion

Inferred from direct assay Ref.10. Source: BHF-UCL

lamellipodium assembly

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of an epithelium

Inferred from direct assay Ref.10. Source: BHF-UCL

protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

adherens junction

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.9. Source: UniProtKB

costamere

Inferred from sequence or structural similarity. Source: UniProtKB

fascia adherens

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

mitochondrial inner membrane

Inferred from direct assay PubMed 12615910. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalpha-catenin binding

Inferred from direct assay Ref.10. Source: BHF-UCL

beta-catenin binding

Inferred from direct assay Ref.10. Source: BHF-UCL

cadherin binding

Inferred from physical interaction Ref.10. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 7525621PubMed 8922390PubMed 7525621PubMed 8922390. Source: IntAct

structural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P12003-2)

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.
Isoform 1 (identifier: P12003-1)

Also known as: Vinculin;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 11351134Vinculin
PRO_0000064255

Regions

Repeat259 – 3691111
Repeat370 – 4791102
Repeat480 – 5891103
Region2 – 835834N-terminal globular head By similarity
Region168 – 20841Talin-interaction
Region259 – 5893313 X 112 AA tandem repeats
Region836 – 87843Linker (Pro-rich) By similarity
Region879 – 1135257C-terminal tail By similarity
Region1004 – 104744Facilitates phospholipid membrane insertion By similarity
Region1121 – 113515Facilitates phospholipid membrane insertion By similarity
Compositional bias837 – 87842Pro-rich

Amino acid modifications

Modified residue1001Phosphotyrosine Ref.8
Modified residue5371Phosphotyrosine Potential
Modified residue8221Phosphotyrosine Potential
Modified residue11341Phosphotyrosine; by SRC-type Tyr-kinases Ref.8

Natural variations

Alternative sequence916 – 98469Missing in isoform 1.
VSP_010772

Experimental info

Mutagenesis1001Y → 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. Ref.8
Mutagenesis1601Y → F: No change of phosphorylation levels in platelets. Ref.8
Mutagenesis5371Y → F: No change of phosphorylation levels in platelets. Ref.8
Mutagenesis6921Y → F: No change of phosphorylation levels in platelets. Ref.8
Mutagenesis8221Y → F: No change of phosphorylation levels in platelets. Ref.8
Mutagenesis11341Y → 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. Ref.8
Sequence conflict442 – 4476TAKLSD → QLSCQI Ref.2
Sequence conflict442 – 4476TAKLSD → QLSCQI in CAA68412. Ref.4
Sequence conflict7011Q → H Ref.2
Sequence conflict7011Q → H in CAA68412. Ref.4
Sequence conflict8801E → K in CAA68412. Ref.4

Secondary structure

.............................................................................................. 1135
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Metavinculin) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 28CC2699C9511058

FASTA1,135124,560
        10         20         30         40         50         60 
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA VSNLVRVGKE 

        70         80         90        100        110        120 
TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY SVPARDYLID GSRGILSGTS 

       130        140        150        160        170        180 
DLLLTFDEAE VRKIIRVCKG ILEYLTVAEV VETMEDLVTY TKNLGPGMTK MAKMIDERQQ 

       190        200        210        220        230        240 
ELTHQEHRVM LVNSMNTVKE LLPVLISAMK IFVTTKNTKS QGIEEALKNR NFTVEKMSAE 

       250        260        270        280        290        300 
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR 

       310        320        330        340        350        360 
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM QKAQQVSQGL 

       370        380        390        400        410        420 
DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG GSEGEEHIRG IMSEARKVAE 

       430        440        450        460        470        480 
LCEEPKERDD ILRSLGEISA LTAKLSDLRR HGKGDSPEAR ALAKQIATSL QNLQSKTNRA 

       490        500        510        520        530        540 
VANTRPVKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD 

       550        560        570        580        590        600 
LLAKCDRVDQ LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS 

       610        620        630        640        650        660 
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV GTANKTTVEG 

       670        680        690        700        710        720 
IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 

       730        740        750        760        770        780 
SLLDASEEAI KKDLDKCKVA MANMQPQMLV AGATSIARRA NRILLVAKRE VENSEDPKFR 

       790        800        810        820        830        840 
EAVKAASDEL SKTISPMVMD AKAVAGNISD PGLQKSFLDS GYRILGAVAK VREAFQPQEP 

       850        860        870        880        890        900 
DFPPPPPDLE HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM 

       910        920        930        940        950        960 
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY EPELLLMPTN 

       970        980        990       1000       1010       1020 
QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA EMSRLVRGGS GNKRALIQCA 

      1030       1040       1050       1060       1070       1080 
KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL LQVCERIPTI STQLKILSTV KATMLGRTNI 

      1090       1100       1110       1120       1130 
SDEESEQATE MLVHNAQNLM QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ 

« Hide

Isoform 1 (Vinculin) [UniParc].

Checksum: 6F585201260BA47F
Show »

FASTA1,066116,999

References

[1]"cDNA-derived sequence of chicken embryo vinculin."
Coutu M.D., Craig S.W.
Proc. Natl. Acad. Sci. U.S.A. 85:8535-8539(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[2]"Primary sequence and domain structure of chicken vinculin."
Price G.J., Jones P., Davison M.D., Patel B., Bendori R., Geiger B., Critchley D.R.
Biochem. J. 259:453-461(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Embryo.
[3]"Chicken vinculin and meta-vinculin are derived from a single gene by alternative splicing of a 207-base pair exon unique to meta-vinculin."
Byrne B.J., Kaczorowski Y.J., Coutu M.D., Craig S.W.
J. Biol. Chem. 267:12845-12850(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2).
[4]"Isolation and characterization of a vinculin cDNA from chick-embryo fibroblasts."
Price G.J., Jones P., Davison M.D., Patel B., Eperon I.C., Critchley D.R.
Biochem. J. 245:595-603(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-881.
Tissue: Embryo.
[5]"The cytoskeletal protein vinculin is acylated by myristic acid."
Kellie S., Wigglesworth N.M.
FEBS Lett. 213:428-432(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION.
[6]"Identification of a talin binding site in the cytoskeletal protein vinculin."
Jones P., Jackson P., Price G.J., Patel B., Ohanion V., Lear A.L., Critchley D.R.
J. Cell Biol. 109:2917-2927(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: TALIN INTERACTION DOMAIN.
[7]"Molecular interactions of N-RAP, a nebulin-related protein of striated muscle myotendon junctions and intercalated disks."
Luo G., Herrera A.H., Horowits R.
Biochemistry 38:6135-6143(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NRAP.
[8]"The phosphorylation of vinculin on tyrosine residues 100 and 1065, mediated by SRC kinases, affects cell spreading."
Zhang Z., Izaguirre G., Lin S.-Y., Lee H.Y., Schaefer E., Haimovich B.
Mol. Biol. Cell 15:4234-4247(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-100 AND TYR-1134, FUNCTION, MUTAGENESIS OF TYR-100; TYR-160; TYR-537; TYR-692; TYR-822 AND TYR-1134.
[9]"Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a myosin II-dependent manner."
le Duc Q., Shi Q., Blonk I., Sonnenberg A., Wang N., Leckband D., de Rooij J.
J. Cell Biol. 189:1107-1115(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Vinculin regulates cell-surface E-cadherin expression by binding to beta-catenin."
Peng X., Cuff L.E., Lawton C.D., DeMali K.A.
J. Cell Sci. 123:567-577(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
[11]"Crystal structure of the vinculin tail suggests a pathway for activation."
Bakolitsa C., de Pereda J.M., Bagshaw C.R., Critchley D.R., Liddington R.C.
Cell 99:603-613(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 881-1135 OF ISOFORM 1.
[12]"RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover."
Goult B.T., Zacharchenko T., Bate N., Tsang R., Hey F., Gingras A.R., Elliott P.R., Roberts G.C., Ballestrem C., Critchley D.R., Barsukov I.L.
J. Biol. Chem. 288:8238-8249(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-259 IN COMPLEX WITH APBB1IP, INTERACTION WITH TLN1 AND APBB1IP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04126 mRNA. Translation: AAA49136.1.
M87837 Genomic DNA. Translation: AAA49135.1.
Y00312 mRNA. Translation: CAA68412.1.
PIRA29997. A31346.
RefSeqNP_990772.1. NM_205441.1. [P12003-1]
UniGeneGga.698.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
3ZDLX-ray2.30A1-259[»]
4E17X-ray2.30A1-259[»]
4E18X-ray2.40A1-259[»]
DisProtDP00556.
ProteinModelPortalP12003.
SMRP12003. Positions 1-254.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid676671. 2 interactions.
DIPDIP-35191N.
IntActP12003. 12 interactions.
STRING9031.ENSGALP00000008131.

Proteomic databases

PaxDbP12003.
PRIDEP12003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396422.
KEGGgga:396422.

Organism-specific databases

CTD7414.

Phylogenomic databases

eggNOGNOG329927.
HOGENOMHOG000007828.
HOVERGENHBG079758.
InParanoidP12003.
KOK05700.
PhylomeDBP12003.

Family and domain databases

InterProIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERPTHR18914. PTHR18914. 1 hit.
PfamPF01044. Vinculin. 3 hits.
[Graphical view]
PRINTSPR00806. VINCULIN.
SUPFAMSSF47220. SSF47220. 8 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP12003.
NextBio20816463.
PROP12003.

Entry information

Entry nameVINC_CHICK
AccessionPrimary (citable) accession number: P12003
Secondary accession number(s): Q91024
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 137 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references