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Protein

Vitronectin

Gene

VTN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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: BHF-UCL
  • cell migration Source: UniProtKB
  • cell proliferation 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

Keywordsi

Molecular functionHeparin-binding
Biological processCell adhesion

Enzyme and pathway databases

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

EuPathDBiHostDB:ENSG00000109072.13
HGNCiHGNC:12724 VTN
MIMi193190 gene
neXtProtiNX_P04004

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; Source: COMPARTMENTS

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) asparagine5 Publications1
Modified residuei130PhosphoserineCombined sources1
Modified residuei137PhosphoserineCombined sources1
Glycosylationi169N-linked (GlcNAc...) asparagine3 Publications1
Glycosylationi242N-linked (GlcNAc...) (complex) asparagine4 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-2DPAGEiP04004
SWISS-2DPAGEiP04004

PTM databases

GlyConnecti625
iPTMnetiP04004
PhosphoSitePlusiP04004
UniCarbKBiP04004

Miscellaneous databases

PMAP-CutDBiP04004

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

Show more details

GO - Molecular functioni

  • identical protein binding Source: Ensembl
  • integrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113287, 121 interactors
CORUMiP04004
DIPiDIP-36566N
ELMiP04004
IntActiP04004, 60 interactors
MINTiP04004
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.

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

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

Family and domain databases

CDDicd00094 HX, 1 hit
Gene3Di2.110.10.10, 2 hits
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR036024 Somatomedin_B-like_dom_sf
IPR020436 Somatomedin_B_chordata
IPR001212 Somatomedin_B_dom
PfamiView protein in Pfam
PF00045 Hemopexin, 4 hits
PF01033 Somatomedin_B, 1 hit
PRINTSiPR00022 SOMATOMEDINB
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00201 SO, 1 hit
SUPFAMiSSF50923 SSF50923, 3 hits
SSF90188 SSF90188, 1 hit
PROSITEiView protein in PROSITE
PS00024 HEMOPEXIN, 2 hits
PS51642 HEMOPEXIN_2, 4 hits
PS00524 SMB_1, 1 hit
PS50958 SMB_2, 1 hit

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 → S1 PublicationCorresponds to variant dbSNP:rs2227741Ensembl.1
Natural variantiVAR_012984268R → Q1 PublicationCorresponds to variant dbSNP:rs2227723Ensembl.1
Natural variantiVAR_012985400T → M2 PublicationsCorresponds to variant dbSNP:rs704Ensembl.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

Similar proteinsi

Entry informationi

Entry nameiVTNC_HUMAN
AccessioniPrimary (citable) accession number: P04004
Secondary accession number(s): B2R7G0, P01141, Q9BSH7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 23, 1986
Last sequence update: October 23, 1986
Last modified: April 25, 2018
This is version 218 of the entry and version 1 of the sequence. See 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health