P22458 · VTNC_RABIT

Function

function

Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcollagen-containing extracellular matrix
Cellular Componentextracellular space
Molecular Functionextracellular matrix binding
Molecular Functionheparin binding
Molecular Functionpolysaccharide binding
Molecular Functionscavenger receptor activity
Biological Processcell adhesion mediated by integrin
Biological Processcell-matrix adhesion
Biological Processimmune response

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Vitronectin
  • Short names
    VN
  • Alternative names
    • Glycoprotein 66
    • S-protein
    • Serum-spreading factor

Gene names

    • Name
      VTN

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus

Accessions

  • Primary accession
    P22458

Proteomes

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, modified residue, glycosylation.

TypeIDPosition(s)Description
Signal1-19
ChainPRO_000003640020-475Vitronectin
Disulfide bond24↔28Alternate
Disulfide bond24↔40Alternate
Disulfide bond28↔58Alternate
Disulfide bond38↔40Alternate
Disulfide bond38↔51Alternate
Disulfide bond44↔50
Disulfide bond51↔58Alternate
Modified residue69Phosphothreonine
Modified residue75Sulfotyrosine
Modified residue78Sulfotyrosine
Modified residue80Sulfotyrosine
Glycosylation87N-linked (GlcNAc...) asparagine
Glycosylation169N-linked (GlcNAc...) asparagine
Glycosylation242N-linked (GlcNAc...) asparagine
Modified residue279Sulfotyrosine
Modified residue282Sulfotyrosine
Modified residue312Phosphoserine
Modified residue394Phosphoserine

Post-translational modification

Sulfated on tyrosine residues.
N- and O-glycosylated.
It has been suggested that the active SMB domain may be permitted considerable disulfide bond heterogeneity or variability, thus two alternate disulfide patterns based on 3D structures are described with 1 disulfide bond conserved in both.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Plasma.

Interaction

Subunit

Interacts with SERPINE1/PAI1 and C1QBP (By similarity).
Monomer

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, motif, compositional bias, region, repeat.

TypeIDPosition(s)Description
Domain20-63SMB
Motif64-66Cell attachment site
Compositional bias87-108Polar residues
Region87-123Disordered
Repeat158-202Hemopexin 1
Repeat203-250Hemopexin 2
Repeat251-305Hemopexin 3
Region359-391Disordered
Compositional bias366-388Basic residues
Region366-392Glycosaminoglycan binding region
Repeat419-469Hemopexin 4

Domain

The SMB domain mediates interaction with SERPINE1/PAI1.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    475
  • Mass (Da)
    53,943
  • Last updated
    1991-08-01 v1
  • Checksum
    D5D1F31B8C2FA12D
MAPLRPIFTLALLLWVVLADQESCKDRCTEGFNANRKCQCDELCSYYQSCCADYAAECKPQVTRGDVFTMPEDEYGPYDYIEQTKDNASVHAQPESPTVGQEPTLSPDLQTEGGAEPTHEVPLEPEMETLRPEGEDLQAGTTELGTSASPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGILDPDYPRNISEGFSGIPDNVDAAFALPAHSYSGRERVYFFKGDKYWEYQFQQQPSQEECEGSSLSAVFEHFAMLHRDSWEDIFKLLFWGRPSGGARQPQFISRDWHGVPGKVDAAMAGRIYISGLTPSPSAKKQKSRRRSRKRYRSRYGRGRSQNSRRLSRSISRLWFSSEEVSLGPYNYEDYETSWLKPATSEPIQSVYFFSGDKYYRVNLRTQRVDTVNPPYPRSIAQYWLGCPAPGGQ

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict26in Ref. 2; AA sequence
Sequence conflict34-35in Ref. 2; AA sequence
Sequence conflict44in Ref. 2; AA sequence
Compositional bias87-108Polar residues
Compositional bias366-388Basic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M55442
EMBL· GenBank· DDBJ
AAA31258.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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