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P85972

- VINC_RAT

UniProt

P85972 - VINC_RAT

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Protein

Vinculin

Gene

Vcl

Organism
Rattus norvegicus (Rat)
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. Rho GTPase binding Source: RGD
  2. structural molecule activity Source: InterPro

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
VinculinBy similarity
Alternative name(s):
MetavinculinBy similarity
Gene namesi
Name:VclBy similarity
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi1311217. Vcl.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. 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. Colocalizes with LIMD1 in the focal adhesions (By similarity).By similarity

GO - Cellular componenti

  1. actin cytoskeleton Source: InterPro
  2. intercalated disc Source: BHF-UCL
  3. sarcolemma Source: BHF-UCL
  4. Z disc Source: BHF-UCL
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 – 10661065VinculinBy similarityPRO_0000349117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei173 – 1731N6-acetyllysineBy similarity
Modified residuei290 – 2901Phosphoserine1 Publication
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei496 – 4961N6-acetyllysineBy similarity
Modified residuei721 – 7211PhosphoserineBy similarity
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

PaxDbiP85972.
PRIDEiP85972.

2D gel databases

World-2DPAGE0004:P85972.

PTM databases

PhosphoSiteiP85972.

Expressioni

Gene expression databases

GenevestigatoriP85972.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi258242. 2 interactions.
IntActiP85972. 3 interactions.
MINTiMINT-6804299.

Structurei

3D structure databases

ProteinModelPortaliP85972.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati259 – 3691111Sequence AnalysisAdd
BLAST
Repeati370 – 4791102Sequence AnalysisAdd
BLAST
Repeati480 – 5891103Sequence AnalysisAdd
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 repeatsSequence AnalysisAdd
BLAST
Regioni836 – 87843Linker (Pro-rich)By similarityAdd
BLAST
Regioni879 – 1066188C-terminal tailBy similarityAdd
BLAST
Regioni935 – 97844Facilitates phospholipid membrane insertionBy similarityAdd
BLAST
Regioni1052 – 106615Facilitates phospholipid membrane insertionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi837 – 87842Pro-richSequence AnalysisAdd
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.Sequence Analysis

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG329927.
HOGENOMiHOG000007828.
HOVERGENiHBG079758.
InParanoidiP85972.
KOiK05700.
PhylomeDBiP85972.
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.

P85972-1 [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 NFTVGKMSAE 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
LAAQLADLAA RGEGESPQAR ALASQLQDSL KDLKTQMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPPDAP NREEVFDERA ANFENHSGRL GATAEKAAAV
660 670 680 690 700
GAANKSTVEG 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):116,615
Last modified:September 2, 2008 - v1
Checksum:iE0669F208E4E8A86
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474061 Genomic DNA. Translation: EDL86258.1.
RefSeqiNP_001100718.1. NM_001107248.1.
UniGeneiRn.164613.

Genome annotation databases

GeneIDi305679.
KEGGirno:305679.
UCSCiRGD:1311217. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CH474061 Genomic DNA. Translation: EDL86258.1 .
RefSeqi NP_001100718.1. NM_001107248.1.
UniGenei Rn.164613.

3D structure databases

ProteinModelPortali P85972.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 258242. 2 interactions.
IntActi P85972. 3 interactions.
MINTi MINT-6804299.

PTM databases

PhosphoSitei P85972.

2D gel databases

World-2DPAGE 0004:P85972.

Proteomic databases

PaxDbi P85972.
PRIDEi P85972.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 305679.
KEGGi rno:305679.
UCSCi RGD:1311217. rat.

Organism-specific databases

CTDi 7414.
RGDi 1311217. Vcl.

Phylogenomic databases

eggNOGi NOG329927.
HOGENOMi HOG000007828.
HOVERGENi HBG079758.
InParanoidi P85972.
KOi K05700.
PhylomeDBi P85972.
TreeFami TF313686.

Miscellaneous databases

NextBioi 654946.
PROi P85972.

Gene expression databases

Genevestigatori P85972.

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. 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.

Entry informationi

Entry nameiVINC_RAT
AccessioniPrimary (citable) accession number: P85972
Secondary accession number(s): A6KKR4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 2, 2008
Last sequence update: September 2, 2008
Last modified: November 26, 2014
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3