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Q64727 (VINC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. 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·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1066 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 By similarity. Ref.1

Subunit structure

Exhibits self-association properties. Interacts with APBB1IP, NRAP and TLN1. Interacts with SYNM. 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 By similarity. Interacts with SORBS1. Ref.6

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell junctionadherens junction By similarity. Cell membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell junctionfocal adhesion By similarity. 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. Co-localizes with LIMD1 in the focal adhesions By similarity.

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.

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.

Post-translational modification

Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1065 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques By similarity.

Acetylated; mainly by myristic acid but also by a small amount of palmitic acid By similarity.

Sequence similarities

Belongs to the vinculin/alpha-catenin family.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
   DomainRepeat
   LigandActin-binding
   PTMAcetylation
Lipoprotein
Palmitate
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processadherens junction assembly

Inferred from electronic annotation. Source: Ensembl

apical junction assembly

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from direct assay PubMed 12473693. Source: MGI

epithelial cell-cell adhesion

Inferred from electronic annotation. Source: Ensembl

lamellipodium assembly

Inferred from direct assay PubMed 12473693. Source: MGI

morphogenesis of an epithelium

Inferred from electronic annotation. Source: Ensembl

protein localization to cell surface

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Inferred from direct assay PubMed 12473693. Source: MGI

   Cellular_componentactin cytoskeleton

Inferred from electronic annotation. Source: InterPro

adherens junction

Inferred from direct assay PubMed 12203715. Source: MGI

cell-cell junction

Inferred from direct assay PubMed 14657280. Source: MGI

costamere

Inferred from direct assay PubMed 15128702. Source: MGI

fascia adherens

Inferred from direct assay PubMed 11732910PubMed 16481394. Source: MGI

focal adhesion

Inferred from direct assay PubMed 15883197. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 16481394. Source: MGI

protein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionstructural molecule activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 10661065Vinculin
PRO_0000064253

Regions

Repeat259 – 3691111
Repeat370 – 4791102
Repeat480 – 5891103
Region2 – 835834N-terminal globular head By similarity
Region168 – 20841Talin-interaction By similarity
Region259 – 5893313 X 112 AA tandem repeats
Region836 – 87843Linker (Pro-rich) By similarity
Region879 – 1066188C-terminal tail By similarity
Region935 – 97844Facilitates phospholipid membrane insertion
Region1052 – 106615Facilitates phospholipid membrane insertion
Compositional bias837 – 87842Pro-rich

Amino acid modifications

Modified residue1731N6-acetyllysine By similarity
Modified residue2901Phosphoserine Ref.7 Ref.9
Modified residue3461Phosphoserine By similarity
Modified residue4341Phosphoserine By similarity
Modified residue4961N6-acetyllysine By similarity
Modified residue5371Phosphotyrosine Potential
Modified residue7211Phosphoserine Ref.9
Modified residue8221Phosphotyrosine By similarity
Modified residue10651Phosphotyrosine; by SRC-type Tyr-kinases By similarity

Experimental info

Sequence conflict161V → E in AAB96843. Ref.1
Sequence conflict2151T → S in AAB96843. Ref.1
Sequence conflict3631L → V in AAB96843. Ref.1
Sequence conflict4991Q → K in BAC37033. Ref.3
Sequence conflict5011Q → R in AAB96843. Ref.1
Sequence conflict7991M → K in BAC37033. Ref.3
Sequence conflict8121G → D in AAB96843. Ref.1
Sequence conflict10441A → T in BAC37033. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q64727 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 067F1B16A5285859

FASTA1,066116,717
        10         20         30         40         50         60 
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA VSNLVRVGKE 

        70         80         90        100        110        120 
TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY SVPARDYLID GSRGILSGTS 

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

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

       250        260        270        280        290        300 
INEIIRVLQL TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR 

       310        320        330        340        350        360 
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM QKAQQVSQGL 

       370        380        390        400        410        420 
DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG GPEGEEQIRG ALAEARKIAE 

       430        440        450        460        470        480 
LCDDPKERDD ILRSLGEIAA LTSKLGDLRR QGKGDSPEAR ALAKQVATAL QNLQTKTNRA 

       490        500        510        520        530        540 
VANSRPAKAA VHLEGKIEQA QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD 

       550        560        570        580        590        600 
LLAKCDRVDQ LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS 

       610        620        630        640        650        660 
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV GTANKSTVEG 

       670        680        690        700        710        720 
IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN QWIDNVEKMT GLVDEAIDTK 

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

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

       850        860        870        880        890        900 
DFPPPPPDLE QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM 

       910        920        930        940        950        960 
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC AKDIAKASDE 

       970        980        990       1000       1010       1020 
VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST VKATMLGRTN ISDEESEQAT 

      1030       1040       1050       1060 
EMLVHNAQNL MQSVKETVRE AEAASIKIRT DAGFTLRWVR KTPWYQ 

« Hide

References

« Hide 'large scale' references
[1]"Targeted disruption of vinculin genes in F9 and embryonic stem cells changes cell morphology, adhesion, and locomotion."
Coll J.-L., Ben-Ze'ev A., Ezzell R.M., Rodriguez Fernandez J.L., Baribault H., Oshima R.G., Adamson E.D.
Proc. Natl. Acad. Sci. U.S.A. 92:9161-9165(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: 129/SvJ.
Tissue: Embryo.
[2]"Vinculin gene is non-essential in Drosophila melanogaster."
Alatortsev V.E., Kramerova I.A., Frolov M.V., Lavrov S.A., Westphal E.D.
FEBS Lett. 413:197-201(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Forelimb.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 286-300; 656-666 AND 916-924, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[6]"Ponsin/SH3P12: an l-afadin- and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions."
Mandai K., Nakanishi H., Satoh A., Takahashi K., Satoh K., Nishioka H., Mizoguchi A., Takai Y.
J. Cell Biol. 144:1001-1017(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SORBS1.
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[8]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[9]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-721, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[10]"Vinculin's C-terminal region facilitates phospholipid membrane insertion."
Wirth V.F., List F., Diez G., Goldmann W.H.
Biochem. Biophys. Res. Commun. 398:433-437(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REGION INVOLVED IN PHOSPHOLIPID MEMBRANE INSERTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L13300, L13299 Genomic DNA. Translation: AAA40557.1.
L18880 mRNA. Translation: AAB96843.1.
AK035184 mRNA. Translation: BAC28973.1.
AK077850 mRNA. Translation: BAC37033.1.
BC008520 mRNA. Translation: AAH08520.1.
BC008554 mRNA. Translation: AAH08554.1.
PIRA60965.
T10108.
RefSeqNP_033528.3. NM_009502.4.
UniGeneMm.279361.

3D structure databases

ProteinModelPortalQ64727.
SMRQ64727. Positions 1-258, 882-1063.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204506. 5 interactions.
IntActQ64727. 11 interactions.
MINTMINT-1634466.

PTM databases

PhosphoSiteQ64727.

2D gel databases

REPRODUCTION-2DPAGEQ64727.

Proteomic databases

PaxDbQ64727.
PRIDEQ64727.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
GeneID22330.
KEGGmmu:22330.
UCSCuc007skz.1. mouse.

Organism-specific databases

CTD7414.
MGIMGI:98927. Vcl.

Phylogenomic databases

eggNOGNOG329927.
GeneTreeENSGT00550000074411.
HOGENOMHOG000007828.
HOVERGENHBG079758.
InParanoidQ64727.
KOK05700.
OMAPILICSM.
OrthoDBEOG73NG2V.
PhylomeDBQ64727.
TreeFamTF313686.

Gene expression databases

BgeeQ64727.
CleanExMM_VCL.
GenevestigatorQ64727.

Family and domain databases

InterProIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERPTHR18914. PTHR18914. 1 hit.
PfamPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSPR00806. VINCULIN.
SUPFAMSSF47220. SSF47220. 6 hits.
PROSITEPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVCL. mouse.
NextBio302571.
PMAP-CutDBQ64727.
PROQ64727.
SOURCESearch...

Entry information

Entry nameVINC_MOUSE
AccessionPrimary (citable) accession number: Q64727
Secondary accession number(s): Q8BP32 expand/collapse secondary AC list , Q8BS46, Q922C5, Q922D9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 128 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot