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Q64727

- VINC_MOUSE

UniProt

Q64727 - VINC_MOUSE

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Protein

Vinculin

Gene

Vcl

Organism
Mus musculus (Mouse)
Status
Reviewed - 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 (By similarity).By similarity

GO - Molecular functioni

  1. structural molecule activity Source: InterPro

GO - Biological processi

  1. adherens junction assembly Source: Ensembl
  2. apical junction assembly Source: Ensembl
  3. cell adhesion Source: MGI
  4. epithelial cell-cell adhesion Source: Ensembl
  5. lamellipodium assembly Source: MGI
  6. morphogenesis of an epithelium Source: Ensembl
  7. protein localization to cell surface Source: Ensembl
  8. regulation of cell migration Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
Gene namesi
Name:Vcl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:98927. Vcl.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Cell junctionadherens junction By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; 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).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. adherens junction Source: MGI
  3. cell-cell junction Source: MGI
  4. costamere Source: MGI
  5. cytoplasm Source: UniProtKB
  6. extracellular vesicular exosome Source: Ensembl
  7. fascia adherens Source: MGI
  8. focal adhesion Source: UniProtKB
  9. plasma membrane Source: MGI
  10. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 10661065VinculinPRO_0000064253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731N6-acetyllysineBy similarity
Modified residuei290 – 2901Phosphoserine2 Publications
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei496 – 4961N6-acetyllysineBy similarity
Modified residuei537 – 5371PhosphotyrosineSequence Analysis
Modified residuei721 – 7211Phosphoserine1 Publication
Modified residuei822 – 8221PhosphotyrosineBy similarity
Modified residuei1065 – 10651Phosphotyrosine; by SRC-type Tyr-kinasesBy similarity

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiQ64727.
PaxDbiQ64727.
PRIDEiQ64727.

2D gel databases

REPRODUCTION-2DPAGEQ64727.

PTM databases

PhosphoSiteiQ64727.

Miscellaneous databases

PMAP-CutDBQ64727.

Expressioni

Gene expression databases

BgeeiQ64727.
CleanExiMM_VCL.
GenevestigatoriQ64727.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Arhgef1Q612103EBI-432047,EBI-641821
PXNP490244EBI-432047,EBI-2896280From a different organism.
PxnQ8VI363EBI-432047,EBI-983394
Tln1P260392EBI-432047,EBI-1039593

Protein-protein interaction databases

BioGridi204506. 6 interactions.
IntActiQ64727. 11 interactions.
MINTiMINT-1634466.

Structurei

3D structure databases

ProteinModelPortaliQ64727.
SMRiQ64727. Positions 1-258, 882-1063.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati259 – 3691111Add
BLAST
Repeati370 – 4791102Add
BLAST
Repeati480 – 5891103Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 835834N-terminal globular headBy similarityAdd
BLAST
Regioni168 – 20841Talin-interactionBy similarityAdd
BLAST
Regioni259 – 5893313 X 112 AA tandem repeatsAdd
BLAST
Regioni836 – 87843Linker (Pro-rich)By similarityAdd
BLAST
Regioni879 – 1066188C-terminal tailBy similarityAdd
BLAST
Regioni935 – 97844Facilitates phospholipid membrane insertionAdd
BLAST
Regioni1052 – 106615Facilitates phospholipid membrane insertionAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi837 – 87842Pro-richAdd
BLAST

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

eggNOGiNOG329927.
GeneTreeiENSGT00550000074411.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiQ64727.
KOiK05700.
OMAiLTHQVHR.
OrthoDBiEOG73NG2V.
PhylomeDBiQ64727.
TreeFamiTF313686.

Family and domain databases

InterProiIPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view]
PANTHERiPTHR18914. PTHR18914. 1 hit.
PfamiPF01044. Vinculin. 2 hits.
[Graphical view]
PRINTSiPR00806. VINCULIN.
SUPFAMiSSF47220. SSF47220. 6 hits.
PROSITEiPS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q64727-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVAAVQAA
60 70 80 90 100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVQ AAQMLQSDPY
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 IFVTTKNSKN QGIEEALKNR NFTVEKMSAE INEIIRVLQL
260 270 280 290 300
TSWDEDAWAS KDTEAMKRAL ASIDSKLNQA KGWLRDPNAS PGDAGEQAIR
310 320 330 340 350
QILDEAGKVG ELCAGKERRE ILGTCKMLGQ MTDQVADLRA RGQGASPVAM
360 370 380 390 400
QKAQQVSQGL DVLTAKVENA ARKLEAMTNS KQSIAKKIDA AQNWLADPNG
410 420 430 440 450
GPEGEEQIRG ALAEARKIAE LCDDPKERDD ILRSLGEIAA LTSKLGDLRR
460 470 480 490 500
QGKGDSPEAR ALAKQVATAL QNLQTKTNRA VANSRPAKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGHRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LTAQLADLAA RGEGESPQAR ALASQLQDSL KDLKAQMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV
660 670 680 690 700
GTANKSTVEG IQASVKTARE LTPQVISAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANIQPQMLV
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
QLRLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEVINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKGNDII AAAKRMALLM AEMSRLVRGG SGTKRALIQC
960 970 980 990 1000
AKDIAKASDE VTRLAKEVAK QCTDKRIRTN LLQVCERIPT ISTQLKILST
1010 1020 1030 1040 1050
VKATMLGRTN ISDEESEQAT EMLVHNAQNL MQSVKETVRE AEAASIKIRT
1060
DAGFTLRWVR KTPWYQ
Length:1,066
Mass (Da):116,717
Last modified:January 23, 2007 - v4
Checksum:i067F1B16A5285859
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161V → E in AAB96843. (PubMed:7568093)Curated
Sequence conflicti215 – 2151T → S in AAB96843. (PubMed:7568093)Curated
Sequence conflicti363 – 3631L → V in AAB96843. (PubMed:7568093)Curated
Sequence conflicti499 – 4991Q → K in BAC37033. (PubMed:16141072)Curated
Sequence conflicti501 – 5011Q → R in AAB96843. (PubMed:7568093)Curated
Sequence conflicti799 – 7991M → K in BAC37033. (PubMed:16141072)Curated
Sequence conflicti812 – 8121G → D in AAB96843. (PubMed:7568093)Curated
Sequence conflicti1044 – 10441A → T in BAC37033. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS26860.1.
PIRiA60965.
T10108.
RefSeqiNP_033528.3. NM_009502.4.
UniGeneiMm.279361.

Genome annotation databases

EnsembliENSMUST00000022369; ENSMUSP00000022369; ENSMUSG00000021823.
GeneIDi22330.
KEGGimmu:22330.
UCSCiuc007skz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS26860.1.
PIRi A60965.
T10108.
RefSeqi NP_033528.3. NM_009502.4.
UniGenei Mm.279361.

3D structure databases

ProteinModelPortali Q64727.
SMRi Q64727. Positions 1-258, 882-1063.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204506. 6 interactions.
IntActi Q64727. 11 interactions.
MINTi MINT-1634466.

PTM databases

PhosphoSitei Q64727.

2D gel databases

REPRODUCTION-2DPAGE Q64727.

Proteomic databases

MaxQBi Q64727.
PaxDbi Q64727.
PRIDEi Q64727.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022369 ; ENSMUSP00000022369 ; ENSMUSG00000021823 .
GeneIDi 22330.
KEGGi mmu:22330.
UCSCi uc007skz.1. mouse.

Organism-specific databases

CTDi 7414.
MGIi MGI:98927. Vcl.

Phylogenomic databases

eggNOGi NOG329927.
GeneTreei ENSGT00550000074411.
HOGENOMi HOG000007828.
HOVERGENi HBG079758.
InParanoidi Q64727.
KOi K05700.
OMAi LTHQVHR.
OrthoDBi EOG73NG2V.
PhylomeDBi Q64727.
TreeFami TF313686.

Miscellaneous databases

ChiTaRSi VCL. mouse.
NextBioi 302571.
PMAP-CutDB Q64727.
PROi Q64727.
SOURCEi Search...

Gene expression databases

Bgeei Q64727.
CleanExi MM_VCL.
Genevestigatori Q64727.

Family and domain databases

InterProi IPR017997. Vinculin.
IPR006077. Vinculin/catenin.
IPR000633. Vinculin_CS.
[Graphical view ]
PANTHERi PTHR18914. PTHR18914. 1 hit.
Pfami PF01044. Vinculin. 2 hits.
[Graphical view ]
PRINTSi PR00806. VINCULIN.
SUPFAMi SSF47220. SSF47220. 6 hits.
PROSITEi PS00663. VINCULIN_1. 1 hit.
PS00664. VINCULIN_2. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.

Entry informationi

Entry nameiVINC_MOUSE
AccessioniPrimary (citable) accession number: Q64727
Secondary accession number(s): Q8BP32
, Q8BS46, Q922C5, Q922D9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 133 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3