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P85972 (VINC_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 45. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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.

Subunit structure

Exhibits self-association properties. Interacts with APBB1IP, NRAP, SORBS1 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. UniProtKB P18206

Subcellular location

Cytoplasmcytoskeleton. 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. Colocalizes with LIMD1 in the focal adhesions By similarity. Ref.3

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. UniProtKB P12003

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P18206
Chain2 – 10661065Vinculin UniProtKB P18206
PRO_0000349117

Regions

Repeat259 – 3691111
Repeat370 – 4791102
Repeat480 – 5891103
Region2 – 835834N-terminal globular head By similarity
Region168 – 20841Talin-interaction By similarity UniProtKB P12003
Region259 – 5893313 X 112 AA tandem repeats
Region836 – 87843Linker (Pro-rich) By similarity
Region879 – 1066188C-terminal tail By similarity
Region935 – 97844Facilitates phospholipid membrane insertion By similarity
Region1052 – 106615Facilitates phospholipid membrane insertion By similarity
Compositional bias837 – 87842Pro-rich

Amino acid modifications

Modified residue1731N6-acetyllysine By similarity
Modified residue2901Phosphoserine Ref.2 UniProtKB P18206
Modified residue3461Phosphoserine By similarity
Modified residue4341Phosphoserine By similarity
Modified residue4961N6-acetyllysine By similarity
Modified residue7211Phosphoserine By similarity UniProtKB P18206
Modified residue8221Phosphotyrosine By similarity UniProtKB Q64727
Modified residue10651Phosphotyrosine; by SRC-type Tyr-kinases By similarity UniProtKB P12003

Sequences

Sequence LengthMass (Da)Tools
P85972 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: E0669F208E4E8A86

FASTA1,066116,615
        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 NFTVGKMSAE 

       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 LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS 

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

       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]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites."
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[3]"Proteome profile of the mature rat olfactory bulb."
Maurya D.K., Sundaram C.S., Bhargava P.
Proteomics 9:2593-2599(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH474061 Genomic DNA. Translation: EDL86258.1.
RefSeqNP_001100718.1. NM_001107248.1.
UniGeneRn.164613.

3D structure databases

ProteinModelPortalP85972.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid258242. 2 interactions.
IntActP85972. 3 interactions.
MINTMINT-6804299.

PTM databases

PhosphoSiteP85972.

2D gel databases

World-2DPAGE0004:P85972.

Proteomic databases

PaxDbP85972.
PRIDEP85972.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID305679.
KEGGrno:305679.
UCSCRGD:1311217. rat.

Organism-specific databases

CTD7414.
RGD1311217. Vcl.

Phylogenomic databases

eggNOGNOG329927.
HOGENOMHOG000007828.
HOVERGENHBG079758.
KOK05700.
PhylomeDBP85972.
TreeFamTF313686.

Gene expression databases

GenevestigatorP85972.

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

NextBio654946.
PROP85972.

Entry information

Entry nameVINC_RAT
AccessionPrimary (citable) accession number: P85972
Secondary accession number(s): A6KKR4
Entry history
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: April 16, 2014
This is version 45 of the entry and version 1 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