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Entry version 185 (07 Oct 2020)
Sequence version 4 (23 Jan 2007)
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Protein

Vinculin

Gene

VCL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.3 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActin-binding
Biological processCell adhesion

Enzyme and pathway databases

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P12003

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Vinculin
Alternative name(s):
Metavinculin
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:VCL
Synonyms:VINC1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiGallus gallus (Chicken)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9031 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi100Y → 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. 1 Publication1
Mutagenesisi160Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi537Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi692Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi822Y → F: No change of phosphorylation levels in platelets. 1 Publication1
Mutagenesisi1134Y → 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. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000642552 – 1135VinculinAdd BLAST1134

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei100Phosphotyrosine1 Publication1
Modified residuei537PhosphotyrosineCurated1
Modified residuei822PhosphotyrosineBy similarity1
Modified residuei1134Phosphotyrosine; by SRC-type Tyr-kinases1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.1 Publication
Acetylated; mainly by myristic acid but also by a small amount of palmitic acid.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Palmitate, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P12003

PRoteomics IDEntifications database

More...
PRIDEi
P12003

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P12003

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Isoform Metavinculin is muscle-specific.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSGALG00000005079, Expressed in colon and 14 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P12003, baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
676671, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-35191N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P12003

Protein interaction database and analysis system

More...
IntActi
P12003, 16 interactors

Molecular INTeraction database

More...
MINTi
P12003

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000008131

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P12003

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P12003

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati259 – 3691Sequence analysisAdd BLAST111
Repeati370 – 4792Sequence analysisAdd BLAST110
Repeati480 – 5893Sequence analysisAdd BLAST110

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 835N-terminal globular headBy similarityAdd BLAST834
Regioni168 – 208Talin-interaction1 PublicationAdd BLAST41
Regioni259 – 5893 X 112 AA tandem repeatsSequence analysisAdd BLAST331
Regioni836 – 878Linker (Pro-rich)By similarityAdd BLAST43
Regioni879 – 1135C-terminal tailBy similarityAdd BLAST257
Regioni1004 – 1047Facilitates phospholipid membrane insertionBy similarityAdd BLAST44
Regioni1121 – 1135Facilitates phospholipid membrane insertionBy similarityAdd BLAST15

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi837 – 878Pro-richPROSITE-ProRule annotationAdd BLAST42

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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
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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the vinculin/alpha-catenin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3681, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00990000203614

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012338_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P12003

KEGG Orthology (KO)

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KOi
K05700

Database for complete collections of gene phylogenies

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PhylomeDBi
P12003

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036723, Alpha-catenin/vinculin-like_sf
IPR017997, Vinculin
IPR006077, Vinculin/catenin
IPR000633, Vinculin_CS

The PANTHER Classification System

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PANTHERi
PTHR46180, PTHR46180, 2 hits

Pfam protein domain database

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Pfami
View protein in Pfam
PF01044, Vinculin, 3 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47220, SSF47220, 8 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00663, VINCULIN_1, 1 hit
PS00664, VINCULIN_2, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 2 (identifier: P12003-2) [UniParc]FASTAAdd to basket
Also known as: Metavinculin

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MPVFHTRTIE SILEPVAQQI SHLVIMHEEG EVDGKAIPDL TAPVSAVQAA
60 70 80 90 100
VSNLVRVGKE TVQTTEDQIL KRDMPPAFIK VENACTKLVR AAQMLQADPY
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 IFVTTKNTKS QGIEEALKNR NFTVEKMSAE INEIIRVLQL
260 270 280 290 300
TSWDEDAWAS KDTEAMKRAL ALIDSKMNQA KGWLRDPNAP PGDAGEQAIR
310 320 330 340 350
QILDEAGKAG ELCAGKERRE ILGTCKTLGQ MTDQLADLRA RGQGATPMAM
360 370 380 390 400
QKAQQVSQGL DLLTAKVENA ARKLEAMTNS KQAIAKKIDA AQNWLADPNG
410 420 430 440 450
GSEGEEHIRG IMSEARKVAE LCEEPKERDD ILRSLGEISA LTAKLSDLRR
460 470 480 490 500
HGKGDSPEAR ALAKQIATSL QNLQSKTNRA VANTRPVKAA VHLEGKIEQA
510 520 530 540 550
QRWIDNPTVD DRGVGQAAIR GLVAEGRRLA NVMMGPYRQD LLAKCDRVDQ
560 570 580 590 600
LAAQLADLAA RGEGESPQAR AIAAQLQDSL KDLKARMQEA MTQEVSDVFS
610 620 630 640 650
DTTTPIKLLA VAATAPSDTP NREEVFEERA ANFENHAARL GATAEKAAAV
660 670 680 690 700
GTANKTTVEG IQATVKSARE LTPQVVSAAR ILLRNPGNQA AYEHFETMKN
710 720 730 740 750
QWIDNVEKMT GLVDEAIDTK SLLDASEEAI KKDLDKCKVA MANMQPQMLV
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
HLHLTDELAP PKPPLPEGEV PPPRPPPPEE KDEEFPEQKA GEAINQPMMM
910 920 930 940 950
AARQLHDEAR KWSSKPVTVI NEAAEAGVDI DEEDDADVEF SLPSDIEDDY
960 970 980 990 1000
EPELLLMPTN QPVNQPILAA AQSLHREATK WSSKGNDIIA AAKRMALLMA
1010 1020 1030 1040 1050
EMSRLVRGGS GNKRALIQCA KDIAKASDEV TRLAKEVAKQ CTDKRIRTNL
1060 1070 1080 1090 1100
LQVCERIPTI STQLKILSTV KATMLGRTNI SDEESEQATE MLVHNAQNLM
1110 1120 1130
QSVKETVREA EAASIKIRTD AGFTLRWVRK TPWYQ
Length:1,135
Mass (Da):124,560
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i28CC2699C9511058
GO
Isoform 1 (identifier: P12003-1) [UniParc]FASTAAdd to basket
Also known as: Vinculin

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

Show »
Length:1,066
Mass (Da):116,999
Checksum:i6F585201260BA47F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti442 – 447TAKLSD → QLSCQI (PubMed:2497736).Curated6
Sequence conflicti442 – 447TAKLSD → QLSCQI in CAA68412 (PubMed:3117046).Curated6
Sequence conflicti701Q → H (PubMed:2497736).Curated1
Sequence conflicti701Q → H in CAA68412 (PubMed:3117046).Curated1
Sequence conflicti880E → K in CAA68412 (PubMed:3117046).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_010772916 – 984Missing in isoform 1. 2 PublicationsAdd BLAST69

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
J04126 mRNA Translation: AAA49136.1
M87837 Genomic DNA Translation: AAA49135.1
Y00312 mRNA Translation: CAA68412.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A31346, A29997

NCBI Reference Sequences

More...
RefSeqi
NP_990772.1, NM_205441.1 [P12003-1]
XP_015143689.1, XM_015288203.1 [P12003-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079 [P12003-2]
ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079 [P12003-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
396422

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396422

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04126 mRNA Translation: AAA49136.1
M87837 Genomic DNA Translation: AAA49135.1
Y00312 mRNA Translation: CAA68412.1
PIRiA31346, A29997
RefSeqiNP_990772.1, NM_205441.1 [P12003-1]
XP_015143689.1, XM_015288203.1 [P12003-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
3JBIelectron microscopy8.50V879-1130[»]
3ZDLX-ray2.30A1-259[»]
4E17X-ray2.30A1-259[»]
4E18X-ray2.40A1-259[»]
6FQ4X-ray2.89A1-259[»]
6NR7X-ray3.00A1-1135[»]
SMRiP12003
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi676671, 2 interactors
DIPiDIP-35191N
ELMiP12003
IntActiP12003, 16 interactors
MINTiP12003
STRINGi9031.ENSGALP00000008131

PTM databases

iPTMnetiP12003

Proteomic databases

PaxDbiP12003
PRIDEiP12003

Genome annotation databases

EnsembliENSGALT00000008145; ENSGALP00000008131; ENSGALG00000005079 [P12003-2]
ENSGALT00000061988; ENSGALP00000048583; ENSGALG00000005079 [P12003-1]
GeneIDi396422
KEGGigga:396422

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7414

Phylogenomic databases

eggNOGiKOG3681, Eukaryota
GeneTreeiENSGT00990000203614
HOGENOMiCLU_012338_0_0_1
InParanoidiP12003
KOiK05700
PhylomeDBiP12003

Enzyme and pathway databases

SABIO-RKiP12003

Miscellaneous databases

EvolutionaryTraceiP12003

Protein Ontology

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PROi
PR:P12003

Gene expression databases

BgeeiENSGALG00000005079, Expressed in colon and 14 other tissues
ExpressionAtlasiP12003, baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR036723, Alpha-catenin/vinculin-like_sf
IPR017997, Vinculin
IPR006077, Vinculin/catenin
IPR000633, Vinculin_CS
PANTHERiPTHR46180, PTHR46180, 2 hits
PfamiView protein in Pfam
PF01044, Vinculin, 3 hits
SUPFAMiSSF47220, SSF47220, 8 hits
PROSITEiView protein in PROSITE
PS00663, VINCULIN_1, 1 hit
PS00664, VINCULIN_2, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiVINC_CHICK
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P12003
Secondary accession number(s): Q91024
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: October 7, 2020
This is version 185 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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