P22458 · VTNC_RABIT
- ProteinVitronectin
- GeneVTN
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids475 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular space | |
Molecular Function | extracellular matrix binding | |
Molecular Function | heparin binding | |
Molecular Function | polysaccharide binding | |
Molecular Function | scavenger receptor activity | |
Biological Process | cell adhesion mediated by integrin | |
Biological Process | cell-matrix adhesion | |
Biological Process | immune response |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended nameVitronectin
- Short namesVN
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Lagomorpha > Leporidae > Oryctolagus
Accessions
- Primary accessionP22458
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MAPLRPIFTLALLLWVVLA | ||||||
Chain | PRO_0000036400 | 20-475 | Vitronectin | |||
Sequence: DQESCKDRCTEGFNANRKCQCDELCSYYQSCCADYAAECKPQVTRGDVFTMPEDEYGPYDYIEQTKDNASVHAQPESPTVGQEPTLSPDLQTEGGAEPTHEVPLEPEMETLRPEGEDLQAGTTELGTSASPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGILDPDYPRNISEGFSGIPDNVDAAFALPAHSYSGRERVYFFKGDKYWEYQFQQQPSQEECEGSSLSAVFEHFAMLHRDSWEDIFKLLFWGRPSGGARQPQFISRDWHGVPGKVDAAMAGRIYISGLTPSPSAKKQKSRRRSRKRYRSRYGRGRSQNSRRLSRSISRLWFSSEEVSLGPYNYEDYETSWLKPATSEPIQSVYFFSGDKYYRVNLRTQRVDTVNPPYPRSIAQYWLGCPAPGGQ | ||||||
Disulfide bond | 24↔28 | Alternate | ||||
Sequence: CKDRC | ||||||
Disulfide bond | 24↔40 | Alternate | ||||
Sequence: CKDRCTEGFNANRKCQC | ||||||
Disulfide bond | 28↔58 | Alternate | ||||
Sequence: CTEGFNANRKCQCDELCSYYQSCCADYAAEC | ||||||
Disulfide bond | 38↔40 | Alternate | ||||
Sequence: CQC | ||||||
Disulfide bond | 38↔51 | Alternate | ||||
Sequence: CQCDELCSYYQSCC | ||||||
Disulfide bond | 44↔50 | |||||
Sequence: CSYYQSC | ||||||
Disulfide bond | 51↔58 | Alternate | ||||
Sequence: CADYAAEC | ||||||
Modified residue | 69 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 75 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 78 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 80 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Glycosylation | 87 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 169 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 242 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 279 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 282 | Sulfotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 312 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 394 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Plasma.
Structure
Family & Domains
Features
Showing features for domain, motif, compositional bias, region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-63 | SMB | ||||
Sequence: DQESCKDRCTEGFNANRKCQCDELCSYYQSCCADYAAECKPQVT | ||||||
Motif | 64-66 | Cell attachment site | ||||
Sequence: RGD | ||||||
Compositional bias | 87-108 | Polar residues | ||||
Sequence: NASVHAQPESPTVGQEPTLSPD | ||||||
Region | 87-123 | Disordered | ||||
Sequence: NASVHAQPESPTVGQEPTLSPDLQTEGGAEPTHEVPL | ||||||
Repeat | 158-202 | Hemopexin 1 | ||||
Sequence: GKPFDAFTDLKNGSLFAFRGQYCYELDETAVRPGYPKLIQDVWGI | ||||||
Repeat | 203-250 | Hemopexin 2 | ||||
Sequence: EGPIDAAFTRINCQGKTYLFKGSQYWRFEDGILDPDYPRNISEGFSGI | ||||||
Repeat | 251-305 | Hemopexin 3 | ||||
Sequence: PDNVDAAFALPAHSYSGRERVYFFKGDKYWEYQFQQQPSQEECEGSSLSAVFEHF | ||||||
Region | 359-391 | Disordered | ||||
Sequence: LTPSPSAKKQKSRRRSRKRYRSRYGRGRSQNSR | ||||||
Compositional bias | 366-388 | Basic residues | ||||
Sequence: KKQKSRRRSRKRYRSRYGRGRSQ | ||||||
Region | 366-392 | Glycosaminoglycan binding region | ||||
Sequence: KKQKSRRRSRKRYRSRYGRGRSQNSRR | ||||||
Repeat | 419-469 | Hemopexin 4 | ||||
Sequence: TSWLKPATSEPIQSVYFFSGDKYYRVNLRTQRVDTVNPPYPRSIAQYWLGC |
Domain
The SMB domain mediates interaction with SERPINE1/PAI1.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length475
- Mass (Da)53,943
- Last updated1991-08-01 v1
- ChecksumD5D1F31B8C2FA12D
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 26 | in Ref. 2; AA sequence | ||||
Sequence: D → G | ||||||
Sequence conflict | 34-35 | in Ref. 2; AA sequence | ||||
Sequence: AN → SD | ||||||
Sequence conflict | 44 | in Ref. 2; AA sequence | ||||
Sequence: C → P | ||||||
Compositional bias | 87-108 | Polar residues | ||||
Sequence: NASVHAQPESPTVGQEPTLSPD | ||||||
Compositional bias | 366-388 | Basic residues | ||||
Sequence: KKQKSRRRSRKRYRSRYGRGRSQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M55442 EMBL· GenBank· DDBJ | AAA31258.1 EMBL· GenBank· DDBJ | mRNA |