[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2414098 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki S., Oldberg A., Hayman E.G., Pierschbacher M.D., Ruoslahti E.; "Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin."; EMBO J. 4:2519-2524(1985).
[2]	SEQUENCE REVISION. Suzuki S., Oldberg A., Hayman E.G., Pierschbacher M.D., Ruoslahti E.; Submitted (JUN-1986) to the PIR data bank.
[3]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=3004934 [NCBI, ExPASy, EBI, Israel, Japan] Jenne D.E., Stanley K.K.; "Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion."; EMBO J. 4:3153-3157(1985).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1021/bi00395a024; PubMed=2447940 [NCBI, ExPASy, EBI, Israel, Japan] Jenne D.E., Stanley K.K.; "Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the 'pexin' family and a model for their evolution."; Biochemistry 26:6735-6742(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-122; GLN-268 AND MET-400. SeattleSNPs program for genomic applications; Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-400. TISSUE=Lung; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[7]	PROTEIN SEQUENCE OF 20-63. DOI=10.1016/0014-5793(78)80132-X; PubMed=631332 [NCBI, ExPASy, EBI, Israel, Japan] Fryklund L., Sievertsson H.; "Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity."; FEBS Lett. 87:55-60(1978).
[8]	PROTEIN SEQUENCE OF 20-44, AND INTERACTION WITH SERPINE1/PAI1. DOI=10.1016/0167-4838(94)90166-X; PubMed=7522053 [NCBI, ExPASy, EBI, Israel, Japan] Sigurdardottir O., Wiman B.; "Identification of a PAI-1 binding site in vitronectin."; Biochim. Biophys. Acta 1208:104-110(1994).
[9]	PROTEIN SEQUENCE OF 360-368, AND INTERACTION WITH INSULIN. DOI=10.1016/0014-4827(91)90351-T; PubMed=1709100 [NCBI, ExPASy, EBI, Israel, Japan] Yaoi Y., Hashimoto K., Takahara K., Kato I.; "Insulin binds to type V collagen with retention of mitogenic activity."; Exp. Cell Res. 194:180-185(1991).
[10]	PROTEIN SEQUENCE OF 393-400, AND PHOSPHORYLATION AT SER-397. PubMed=2448300 [NCBI, ExPASy, EBI, Israel, Japan] McGuire E.A., Peacock M.E., Inhorn R.C., Siegel N.R., Tollefsen D.M.; "Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain."; J. Biol. Chem. 263:1942-1945(1988).
[11]	PROTEIN SEQUENCE OF 399-413. TISSUE=Plasma; Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.; Submitted (JUN-1992) to UniProtKB.
[12]	SULFATION. PubMed=2479556 [NCBI, ExPASy, EBI, Israel, Japan] Jenne D.E., Hille A., Stanley K.K., Huttner W.B.; "Sulfation of two tyrosine-residues in human complement S-protein (vitronectin)."; Eur. J. Biochem. 185:391-395(1989).
[13]	PHOSPHORYLATION AT SER-397. DOI=10.1016/0014-5793(90)81159-L; PubMed=1696913 [NCBI, ExPASy, EBI, Israel, Japan] Chain D., Korc-Grodzicki B., Kreizman T., Shaltiel S.; "The phosphorylation of the two-chain form of vitronectin by protein kinase A is heparin dependent."; FEBS Lett. 269:221-225(1990).
[14]	INTERACTION WITH SERPINE1/PAI1. PubMed=1704366 [NCBI, ExPASy, EBI, Israel, Japan] Seiffert D., Loskutoff D.J.; "Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin."; J. Biol. Chem. 266:2824-2830(1991).
[15]	PHOSPHORYLATION AT THR-69 AND THR-76, AND MUTAGENESIS OF THR-69 AND THR-76. DOI=10.1074/jbc.273.38.24805; PubMed=9733784 [NCBI, ExPASy, EBI, Israel, Japan] Seger D., Gechtman Z., Shaltiel S.; "Phosphorylation of vitronectin by casein kinase II. Identification of the sites and their promotion of cell adhesion and spreading."; J. Biol. Chem. 273:24805-24813(1998).
[16]	DISULFIDE BONDS IN SOMATOMEDIN-B. DOI=10.1074/jbc.M200354200; PubMed=12019263 [NCBI, ExPASy, EBI, Israel, Japan] Kamikubo Y., Okumura Y., Loskutoff D.J.; "Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin."; J. Biol. Chem. 277:27109-27119(2002).
[17]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1002/pmic.200300556; PubMed=14760718 [NCBI, ExPASy, EBI, Israel, Japan] Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.; "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."; Proteomics 4:454-465(2004).
[18]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.; "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."; J. Proteome Res. 4:2070-2080(2005).
[19]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASS SPECTROMETRY. TISSUE=Pituitary; DOI=10.1007/s11102-006-8916-x; PubMed=16807684 [NCBI, ExPASy, EBI, Israel, Japan] Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; "Phosphoproteomic analysis of the human pituitary."; Pituitary 9:109-120(2006).
[21]	SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312, GLYCOSYLATION AT ASN-86, AND MASS SPECTROMETRY. DOI=10.1038/nmeth1056; PubMed=17558413 [NCBI, ExPASy, EBI, Israel, Japan] Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.; "Determination of the sites of tyrosine O-sulfation in peptides and proteins."; Nat. Methods 4:583-588(2007).
[22]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[23]	X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 22-58 IN COMPLEX WITH SERPINE1/PAI1. DOI=10.1038/nsb943; PubMed=12808446 [NCBI, ExPASy, EBI, Israel, Japan] Zhou A., Huntington J.A., Pannu N.S., Carrell R.W., Read R.J.; "How vitronectin binds PAI-1 to modulate fibrinolysis and cell migration."; Nat. Struct. Biol. 10:541-544(2003).

Comments

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.
FUNCTION: Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity.
SUBUNIT: 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 and insulin.
INTERACTION:
P05121:SERPINE1; NbExp=1; IntAct=EBI-1036653, EBI-953978;
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Plasma.
DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin.
PTM: Sulfated on 2 tyrosine residues.
PTM: N- and O-glycosylated (By similarity).
PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and spreading.
PTM: 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.
SIMILARITY: Contains 4 hemopexin-like domains.
SIMILARITY: Contains 1 SMB (somatomedin-B) domain.
WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/vtn/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X03168; CAA26933.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05006; CAA28659.1; ALT_SEQ; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF382388; AAK60270.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005046; AAH05046.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A29744; SGHU1V.

NP_000629.3; -.

3D structure databases

PDB

1OC0; X-ray; 2.28 A; B=20-70.	[ExPASy / RCSB / EBI]
1S4G; NMR; -; A=20-70.	[ExPASy / RCSB / EBI]
1SSU; NMR; -; A=20-70.	[ExPASy / RCSB / EBI]
2JQ8; NMR; -; A=20-66.	[ExPASy / RCSB / EBI]
3BT1; X-ray; 2.80 A; B=21-60.	[ExPASy / RCSB / EBI]
3BT2; X-ray; 2.50 A; B=21-60.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1OC0; -.
1S4G; -.
1SSU; -.
2JQ8; -.
3BT1; -.
3BT2; -.

ModBase

P04004.

Protein-protein interaction databases

IntAct

P04004; -.

PTM databases

GlycoSuiteDB

P04004; -.

PhosphoSite

P04004; -.

2D gel databases

SWISS-2DPAGE

P04004; -.

DOSAC-COBS-2DPAGE

P04004; -.

Organism-specific databases

HIX0013644; -.

HGNC:12724; VTN.

VTN.

CAB016695; -.
CAB016765; -.

MIM

193190; gene. [NCBI / EBI]

PharmGKB

PA37335; -.

GeneCards

P04004.

Gene expression databases

ArrayExpress

P04004; -.

CleanEx

HS_VTN; -.

GermOnline

ENSG00000109072; Homo sapiens.

Ontologies

GO:0005615;	Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0007155;	Biological process: cell adhesion (traceable author statement from ProtInc).
GO:0006955;	Biological process: immune response (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR000585; Hemopexin.
IPR001212; Somatomedin_B.
Graphical view of domain structure.

Gene3D

G3DSA:2.110.10.10; Hemopexin; 2.

Pfam

PF00045; Hemopexin; 4.
PF01033; Somatomedin_B; 1.
Pfam graphical view of domain structure.

PRINTS

PR00022; SOMATOMEDINB.

SMART

SM00120; HX; 4.
SM00201; SO; 1.
SMART graphical view of domain structure.

PROSITE

PS00024; HEMOPEXIN; 2.
PS00524; SMB_1; 1.
PS50958; SMB_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

P04004; -.

Genome annotation databases

Ensembl

ENSG00000109072; Homo sapiens. [Contig view]

GeneID

7448; -.

KEGG

hsa:7448; -.

Phylogenomic databases

HOGENOM

P04004; -.

HOVERGEN

P04004; -.

Other

DB00013; Urokinase.

P04004; -.

29166; -.

VTN; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell adhesion; Direct protein sequencing; Glycoprotein; Heparin-binding; Phosphoprotein; Polymorphism; Repeat; Secreted; Signal; Sulfation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 19`	`19`
`CHAIN`	`20 478`	`459`	`Vitronectin.`	`PRO_0000036394`
`CHAIN`	`20 398`	`379`	`Vitronectin V65 subunit.`	`PRO_0000036395`
`PEPTIDE`	`20 63`	`44`	`Somatomedin-B.`	`PRO_0000036396`
`CHAIN`	`399 478`	`80`	`Vitronectin V10 subunit.`	`PRO_0000036397`
`DOMAIN`	`20 63`	`44`	`SMB.`
`DOMAIN`	`161 204`	`44`	`Hemopexin-like 1.`
`DOMAIN`	`206 252`	`47`	`Hemopexin-like 2.`
`DOMAIN`	`254 304`	`51`	`Hemopexin-like 3.`
`DOMAIN`	`425 472`	`48`	`Hemopexin-like 4.`
`REGION`	`362 395`	`34`	`Heparin-binding.`
`MOTIF`	`64 66`	`3`	`Cell attachment site.`
`SITE`	`398 399`	`2`	`Cleavage.`
`MOD_RES`	`69 69`		`Phosphothreonine; by CK2; in vitro.`
`MOD_RES`	`75 75`		`Sulfotyrosine.`
`MOD_RES`	`76 76`		`Phosphothreonine; by CK2; in vitro.`
`MOD_RES`	`78 78`		`Sulfotyrosine.`
`MOD_RES`	`171 171`		`Phosphoserine.`
`MOD_RES`	`282 282`		`Sulfotyrosine (Potential).`
`MOD_RES`	`312 312`		`Phosphoserine.`
`MOD_RES`	`397 397`		`Phosphoserine; by PKA.`
`MOD_RES`	`417 417`		`Sulfotyrosine (Potential).`
`MOD_RES`	`420 420`		`Sulfotyrosine (Potential).`
`CARBOHYD`	`86 86`		`N-linked (GlcNAc...).`
`CARBOHYD`	`169 169`		`N-linked (GlcNAc...).`
`CARBOHYD`	`242 242`		`N-linked (GlcNAc...).`
`DISULFID`	`24 40`		`Alternate (By similarity).`
`DISULFID`	`24 28`		`Alternate.`
`DISULFID`	`28 58`		`Alternate (By similarity).`
`DISULFID`	`38 51`		`Alternate (By similarity).`
`DISULFID`	`38 40`		`Alternate.`
`DISULFID`	`44 50`
`DISULFID`	`51 58`		`Alternate.`
`DISULFID`	`293 430`
`VARIANT`	`122 122`	`1`	`A -> S.`	`VAR_012983`
`VARIANT`	`268 268`	`1`	`R -> Q (in dbSNP:rs2227723 [NCBI]).`	`VAR_012984`
`VARIANT`	`400 400`	`1`	`T -> M (in dbSNP:rs704 [NCBI]).`	`VAR_012985`
`MUTAGEN`	`69 69`		`T->A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-76.`
`MUTAGEN`	`69 69`		`T->E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-76.`
`MUTAGEN`	`76 76`		`T->A: Abolishes phosphorylation by CK2 and inhibits adhesion and spreading; when associated with A-69.`
`MUTAGEN`	`76 76`		`T->E: Abolishes phosphorylation by CK2 and enhances adhesion and spreading; when associated with E-69.`
`CONFLICT`	`50 50`		`C -> N (in Ref. 7; AA sequence).`
`CONFLICT`	`225 225`		`S -> N (in Ref. 3 and 4).`
`CONFLICT`	`366 366`		`A -> T (in Ref. 3; CAA26933).`
`STRAND`	`36 39`	`4`
`HELIX`	`44 47`	`4`
`HELIX`	`54 57`	`4`
`STRAND`	`65 68`	`4`

Sequence information

Length: 478 AA [This is the length of the unprocessed precursor]

Molecular weight: 54306 Da [This is the MW of the unprocessed precursor]

CRC64: 0D6DB5591CBFEF45 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC CTDYTAECKP 

        70         80         90        100        110        120 
QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS DLQAQSKGNP EQTPVLKPEE 

       130        140        150        160        170        180 
EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP AEEELCSGKP FDAFTDLKNG SLFAFRGQYC 

       190        200        210        220        230        240 
YELDEKAVRP GYPKLIRDVW GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP 

       250        260        270        280        290        300 
RNISDGFDGI PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA 

       310        320        330        340        350        360 
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM AGRIYISGMA 

       370        380        390        400        410        420 
PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT WLSLFSSEES NLGANNYDDY 

       430        440        450        460        470 
RMDWLVPATC EPIQSVFFFS GDKYYRVNLR TRRVDTVDPP YPRSIAQYWL GCPAPGHL

P04004 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools