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Protein

Vitronectin

Gene

VTN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.
Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.

GO - Molecular functioni

GO - Biological processi

  • cell adhesion Source: ProtInc
  • cell adhesion mediated by integrin Source: BHF-UCL
  • cell-matrix adhesion Source: UniProtKB
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • immune response Source: ProtInc
  • liver regeneration Source: Ensembl
  • negative regulation of blood coagulation Source: BHF-UCL
  • negative regulation of endopeptidase activity Source: BHF-UCL
  • oligodendrocyte differentiation Source: Ensembl
  • positive regulation of cell-substrate adhesion Source: Ensembl
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of receptor-mediated endocytosis Source: BHF-UCL
  • positive regulation of smooth muscle cell migration Source: BHF-UCL
  • positive regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • positive regulation of wound healing Source: BHF-UCL
  • protein polymerization Source: Ensembl
  • regulation of complement activation Source: Reactome
  • smooth muscle cell-matrix adhesion Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000109072-MONOMER.
ReactomeiR-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP04004.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitronectin
Short name:
VN
Alternative name(s):
S-protein
Serum-spreading factor
V75
Cleaved into the following 3 chains:
Gene namesi
Name:VTN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12724. VTN.

Subcellular locationi

GO - Cellular componenti

  • alphav-beta3 integrin-vitronectin complex Source: BHF-UCL
  • basement membrane Source: Ensembl
  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • Golgi lumen Source: Ensembl
  • rough endoplasmic reticulum lumen Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76. 1 Publication1
Mutagenesisi69T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76. 1 Publication1
Mutagenesisi76T → A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69. 1 Publication1
Mutagenesisi76T → E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69. 1 Publication1

Organism-specific databases

DisGeNETi7448.
OpenTargetsiENSG00000109072.
PharmGKBiPA37335.

Chemistry databases

ChEMBLiCHEMBL1075314.
DrugBankiDB00054. Abciximab.

Polymorphism and mutation databases

BioMutaiVTN.
DMDMi139653.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
ChainiPRO_000003639420 – 478VitronectinAdd BLAST459
ChainiPRO_000003639520 – 398Vitronectin V65 subunitAdd BLAST379
PeptideiPRO_000003639620 – 63Somatomedin-BAdd BLAST44
ChainiPRO_0000036397399 – 478Vitronectin V10 subunitAdd BLAST80

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 40PROSITE-ProRule annotation
Disulfide bondi24 ↔ 28PROSITE-ProRule annotation1 Publication
Disulfide bondi28 ↔ 58PROSITE-ProRule annotation
Disulfide bondi38 ↔ 51PROSITE-ProRule annotation
Disulfide bondi38 ↔ 40PROSITE-ProRule annotation1 Publication
Disulfide bondi44 ↔ 50PROSITE-ProRule annotation1 Publication
Disulfide bondi51 ↔ 58PROSITE-ProRule annotation1 Publication
Modified residuei69Phosphothreonine; by CK2; in vitro1 Publication1
Modified residuei75Sulfotyrosine1 Publication1
Modified residuei76Phosphothreonine; by CK2; in vitro1 Publication1
Modified residuei78Sulfotyrosine1 Publication1
Glycosylationi86N-linked (GlcNAc...) (complex)5 Publications1
Modified residuei130PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Glycosylationi169N-linked (GlcNAc...)3 Publications1
Glycosylationi242N-linked (GlcNAc...) (complex)4 Publications1
Modified residuei282SulfotyrosineSequence analysis1
Disulfide bondi293 ↔ 430PROSITE-ProRule annotation1 Publication
Modified residuei312PhosphoserineCombined sources1 Publication1
Modified residuei397Phosphoserine; by PKA2 Publications1
Modified residuei417SulfotyrosineSequence analysis1
Modified residuei420SulfotyrosineSequence analysis1

Post-translational modificationi

Sulfated on 2 tyrosine residues.2 Publications
N- and O-glycosylated.By similarity
Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.1 Publication
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.
Phosphorylation sites are present in the extracellular medium.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei398 – 399Cleavage2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

EPDiP04004.
MaxQBiP04004.
PaxDbiP04004.
PeptideAtlasiP04004.
PRIDEiP04004.

2D gel databases

DOSAC-COBS-2DPAGEP04004.
SWISS-2DPAGEP04004.

PTM databases

iPTMnetiP04004.
PhosphoSitePlusiP04004.
UniCarbKBiP04004.

Miscellaneous databases

PMAP-CutDBP04004.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000109072.
CleanExiHS_VTN.
ExpressionAtlasiP04004. baseline and differential.
GenevisibleiP04004. HS.

Organism-specific databases

HPAiCAB016695.
CAB016765.
HPA060933.

Interactioni

Subunit structurei

Exists in two forms: a single chain 75 kDa form (V75) and a clipped form composed of two chains (65 kDa and 10 kDa) (V65+V10) which are held together by a disulfide bond. Interacts with SERPINE1/PAI1, insulin and C1QBP.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
C1QBPQ070218EBI-1036653,EBI-347528
GOPCQ9HD263EBI-1036653,EBI-349832
lphA0A024A2C97EBI-1036653,EBI-12498321From a different organism.

GO - Molecular functioni

  • integrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113287. 118 interactors.
DIPiDIP-36566N.
IntActiP04004. 35 interactors.
MINTiMINT-4999753.
STRINGi9606.ENSP00000226218.

Structurei

Secondary structure

1478
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi22 – 24Combined sources3
Turni25 – 29Combined sources5
Beta strandi32 – 34Combined sources3
Beta strandi36 – 39Combined sources4
Helixi44 – 47Combined sources4
Turni51 – 53Combined sources3
Helixi54 – 57Combined sources4
Beta strandi65 – 68Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OC0X-ray2.28B20-70[»]
1S4GNMR-A20-70[»]
1SSUNMR-A20-70[»]
2JQ8NMR-A20-66[»]
3BT1X-ray2.80B21-60[»]
3BT2X-ray2.50B21-60[»]
4K24X-ray4.50B21-60[»]
ProteinModelPortaliP04004.
SMRiP04004.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04004.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini20 – 63SMBPROSITE-ProRule annotationAdd BLAST44
Repeati158 – 202Hemopexin 1Add BLAST45
Repeati203 – 250Hemopexin 2Add BLAST48
Repeati251 – 305Hemopexin 3Add BLAST55
Repeati419 – 472Hemopexin 4Add BLAST54

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni362 – 395Heparin-bindingAdd BLAST34

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi64 – 66Cell attachment site3

Domaini

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.

Sequence similaritiesi

Contains 4 hemopexin repeats.Curated
Contains 1 SMB (somatomedin-B) domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00530000063751.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP04004.
KOiK06251.
OMAiLFWGRSS.
OrthoDBiEOG091G0817.
PhylomeDBiP04004.
TreeFamiTF332780.

Family and domain databases

CDDicd00094. HX. 1 hit.
Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
SSF90188. SSF90188. 1 hit.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04004-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC
60 70 80 90 100
CTDYTAECKP QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS
110 120 130 140 150
DLQAQSKGNP EQTPVLKPEE EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP
160 170 180 190 200
AEEELCSGKP FDAFTDLKNG SLFAFRGQYC YELDEKAVRP GYPKLIRDVW
210 220 230 240 250
GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP RNISDGFDGI
260 270 280 290 300
PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA
310 320 330 340 350
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM
360 370 380 390 400
AGRIYISGMA PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT
410 420 430 440 450
WLSLFSSEES NLGANNYDDY RMDWLVPATC EPIQSVFFFS GDKYYRVNLR
460 470
TRRVDTVDPP YPRSIAQYWL GCPAPGHL
Length:478
Mass (Da):54,306
Last modified:October 23, 1986 - v1
Checksum:i0D6DB5591CBFEF45
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti50C → N AA sequence (PubMed:631332).Curated1
Sequence conflicti225S → N (PubMed:3004934).Curated1
Sequence conflicti225S → N (PubMed:2447940).Curated1
Sequence conflicti366A → T in CAA26933 (PubMed:3004934).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_012983122A → S.1 PublicationCorresponds to variant rs2227741dbSNPEnsembl.1
Natural variantiVAR_012984268R → Q.1 PublicationCorresponds to variant rs2227723dbSNPEnsembl.1
Natural variantiVAR_012985400T → M.2 PublicationsCorresponds to variant rs704dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03168 mRNA. Translation: CAA26933.1. Sequence problems.
X05006 Genomic DNA. Translation: CAA28659.1. Sequence problems.
AK312968 mRNA. Translation: BAG35807.1.
AF382388 Genomic DNA. Translation: AAK60270.1.
BC005046 mRNA. Translation: AAH05046.1.
CCDSiCCDS11229.1.
PIRiA29744. SGHU1V.
RefSeqiNP_000629.3. NM_000638.3.
UniGeneiHs.2257.

Genome annotation databases

EnsembliENST00000226218; ENSP00000226218; ENSG00000109072.
GeneIDi7448.
KEGGihsa:7448.
UCSCiuc002hbc.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03168 mRNA. Translation: CAA26933.1. Sequence problems.
X05006 Genomic DNA. Translation: CAA28659.1. Sequence problems.
AK312968 mRNA. Translation: BAG35807.1.
AF382388 Genomic DNA. Translation: AAK60270.1.
BC005046 mRNA. Translation: AAH05046.1.
CCDSiCCDS11229.1.
PIRiA29744. SGHU1V.
RefSeqiNP_000629.3. NM_000638.3.
UniGeneiHs.2257.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OC0X-ray2.28B20-70[»]
1S4GNMR-A20-70[»]
1SSUNMR-A20-70[»]
2JQ8NMR-A20-66[»]
3BT1X-ray2.80B21-60[»]
3BT2X-ray2.50B21-60[»]
4K24X-ray4.50B21-60[»]
ProteinModelPortaliP04004.
SMRiP04004.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113287. 118 interactors.
DIPiDIP-36566N.
IntActiP04004. 35 interactors.
MINTiMINT-4999753.
STRINGi9606.ENSP00000226218.

Chemistry databases

ChEMBLiCHEMBL1075314.
DrugBankiDB00054. Abciximab.

PTM databases

iPTMnetiP04004.
PhosphoSitePlusiP04004.
UniCarbKBiP04004.

Polymorphism and mutation databases

BioMutaiVTN.
DMDMi139653.

2D gel databases

DOSAC-COBS-2DPAGEP04004.
SWISS-2DPAGEP04004.

Proteomic databases

EPDiP04004.
MaxQBiP04004.
PaxDbiP04004.
PeptideAtlasiP04004.
PRIDEiP04004.

Protocols and materials databases

DNASUi7448.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000226218; ENSP00000226218; ENSG00000109072.
GeneIDi7448.
KEGGihsa:7448.
UCSCiuc002hbc.4. human.

Organism-specific databases

CTDi7448.
DisGeNETi7448.
GeneCardsiVTN.
HGNCiHGNC:12724. VTN.
HPAiCAB016695.
CAB016765.
HPA060933.
MIMi193190. gene.
neXtProtiNX_P04004.
OpenTargetsiENSG00000109072.
PharmGKBiPA37335.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00530000063751.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP04004.
KOiK06251.
OMAiLFWGRSS.
OrthoDBiEOG091G0817.
PhylomeDBiP04004.
TreeFamiTF332780.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000109072-MONOMER.
ReactomeiR-HSA-2129379. Molecules associated with elastic fibres.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000170. Syndecan interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-977606. Regulation of Complement cascade.
SIGNORiP04004.

Miscellaneous databases

EvolutionaryTraceiP04004.
GeneWikiiVitronectin.
GenomeRNAii7448.
PMAP-CutDBP04004.
PROiP04004.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000109072.
CleanExiHS_VTN.
ExpressionAtlasiP04004. baseline and differential.
GenevisibleiP04004. HS.

Family and domain databases

CDDicd00094. HX. 1 hit.
Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
SSF90188. SSF90188. 1 hit.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiVTNC_HUMAN
AccessioniPrimary (citable) accession number: P04004
Secondary accession number(s): B2R7G0, P01141, Q9BSH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: November 30, 2016
This is version 206 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.