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Vitronectin (VN) (S-protein) (Serum-spreading factor) (V75) [Cleaved into: Vitronectin V65 subunit; Vitronectin V10 subunit; Somatomedin-B]

 VTNC_HUMAN              Reviewed;         478 AA.
P04004; B2R7G0; P01141; Q9BSH7;
23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
23-OCT-1986, sequence version 1.
30-AUG-2017, entry version 212.
RecName: Full=Vitronectin;
Short=VN;
AltName: Full=S-protein;
AltName: Full=Serum-spreading factor;
AltName: Full=V75;
Contains:
RecName: Full=Vitronectin V65 subunit;
Contains:
RecName: Full=Vitronectin V10 subunit;
Contains:
RecName: Full=Somatomedin-B;
Flags: Precursor;
Name=VTN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2414098;
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;
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].
PubMed=2447940; DOI=10.1021/bi00395a024;
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 [LARGE SCALE MRNA].
TISSUE=Mammary gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-122; GLN-268 AND
MET-400.
SeattleSNPs variation discovery resource;
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-400.
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
PROTEIN SEQUENCE OF 20-63.
PubMed=631332; DOI=10.1016/0014-5793(78)80132-X;
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).
[9]
PROTEIN SEQUENCE OF 20-44, AND INTERACTION WITH SERPINE1/PAI1.
PubMed=7522053; DOI=10.1016/0167-4838(94)90166-X;
Sigurdardottir O., Wiman B.;
"Identification of a PAI-1 binding site in vitronectin.";
Biochim. Biophys. Acta 1208:104-110(1994).
[10]
PROTEIN SEQUENCE OF 360-368, AND INTERACTION WITH INSULIN.
PubMed=1709100; DOI=10.1016/0014-4827(91)90351-T;
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).
[11]
PROTEIN SEQUENCE OF 393-400, AND PHOSPHORYLATION AT SER-397.
PubMed=2448300;
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).
[12]
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.
[13]
SULFATION.
PubMed=2479556; DOI=10.1111/j.1432-1033.1989.tb15127.x;
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).
[14]
PHOSPHORYLATION AT SER-397.
PubMed=1696913; DOI=10.1016/0014-5793(90)81159-L;
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).
[15]
INTERACTION WITH SERPINE1/PAI1.
PubMed=1704366;
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).
[16]
INTERACTION WITH C1QBP.
PubMed=8900153; DOI=10.1074/jbc.271.43.26739;
Lim B.L., Reid K.B., Ghebrehiwet B., Peerschke E.I., Leigh L.A.,
Preissner K.T.;
"The binding protein for globular heads of complement C1q, gC1qR.
Functional expression and characterization as a novel vitronectin
binding factor.";
J. Biol. Chem. 271:26739-26744(1996).
[17]
PHOSPHORYLATION AT THR-69 AND THR-76, AND MUTAGENESIS OF THR-69 AND
THR-76.
PubMed=9733784; DOI=10.1074/jbc.273.38.24805;
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).
[18]
DISULFIDE BONDS IN SOMATOMEDIN-B.
PubMed=12019263; DOI=10.1074/jbc.M200354200;
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).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
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).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
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).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pituitary;
PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
"Phosphoproteomic analysis of the human pituitary.";
Pituitary 9:109-120(2006).
[22]
SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312,
GLYCOSYLATION AT ASN-86, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17558413; DOI=10.1038/nmeth1056;
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
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).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
GLYCOSYLATION AT ASN-86 AND ASN-242.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-137 AND
SER-312, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[29]
X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 22-58 IN COMPLEX WITH
SERPINE1/PAI1.
PubMed=12808446; DOI=10.1038/nsb943;
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).
-!- 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, insulin and C1QBP.
{ECO:0000269|PubMed:12808446, ECO:0000269|PubMed:1704366,
ECO:0000269|PubMed:1709100, ECO:0000269|PubMed:7522053,
ECO:0000269|PubMed:8900153}.
-!- INTERACTION:
Q07021:C1QBP; NbExp=8; IntAct=EBI-1036653, EBI-347528;
P75358:gapA (xeno); NbExp=3; IntAct=EBI-1036653, EBI-2259469;
Q9HD26:GOPC; NbExp=3; IntAct=EBI-1036653, EBI-349832;
P75167:gpmI (xeno); NbExp=2; IntAct=EBI-1036653, EBI-2259565;
P78007:ldh (xeno); NbExp=3; IntAct=EBI-1036653, EBI-2260877;
A0A024A2C9:lph (xeno); NbExp=7; IntAct=EBI-1036653, EBI-12498321;
P75390:pdhA (xeno); NbExp=3; IntAct=EBI-1036653, EBI-2259629;
P75391:pdhB (xeno); NbExp=3; IntAct=EBI-1036653, EBI-2259621;
P78031:pyk (xeno); NbExp=3; IntAct=EBI-1036653, EBI-2259473;
P75611:tkt (xeno); NbExp=3; IntAct=EBI-1036653, EBI-12654979;
-!- 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.
{ECO:0000269|PubMed:17558413, ECO:0000269|PubMed:2479556}.
-!- PTM: N- and O-glycosylated. {ECO:0000250}.
-!- PTM: Phosphorylation on Thr-69 and Thr-76 favors cell adhesion and
spreading. {ECO:0000269|PubMed:9733784}.
-!- 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.
-!- PTM: Phosphorylation sites are present in the extracellular
medium.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/vtn/";
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EMBL; X03168; CAA26933.1; ALT_SEQ; mRNA.
EMBL; X05006; CAA28659.1; ALT_SEQ; Genomic_DNA.
EMBL; AK312968; BAG35807.1; -; mRNA.
EMBL; AF382388; AAK60270.1; -; Genomic_DNA.
EMBL; BC005046; AAH05046.1; -; mRNA.
CCDS; CCDS11229.1; -.
PIR; A29744; SGHU1V.
RefSeq; NP_000629.3; NM_000638.3.
UniGene; Hs.2257; -.
PDB; 1OC0; X-ray; 2.28 A; B=20-70.
PDB; 1S4G; NMR; -; A=20-70.
PDB; 1SSU; NMR; -; A=20-70.
PDB; 2JQ8; NMR; -; A=20-66.
PDB; 3BT1; X-ray; 2.80 A; B=21-60.
PDB; 3BT2; X-ray; 2.50 A; B=21-60.
PDB; 4K24; X-ray; 4.50 A; B=21-60.
PDBsum; 1OC0; -.
PDBsum; 1S4G; -.
PDBsum; 1SSU; -.
PDBsum; 2JQ8; -.
PDBsum; 3BT1; -.
PDBsum; 3BT2; -.
PDBsum; 4K24; -.
ProteinModelPortal; P04004; -.
SMR; P04004; -.
BioGrid; 113287; 121.
DIP; DIP-36566N; -.
ELM; P04004; -.
IntAct; P04004; 44.
MINT; MINT-4999753; -.
STRING; 9606.ENSP00000226218; -.
ChEMBL; CHEMBL1075314; -.
DrugBank; DB00054; Abciximab.
iPTMnet; P04004; -.
PhosphoSitePlus; P04004; -.
UniCarbKB; P04004; -.
BioMuta; VTN; -.
DMDM; 139653; -.
DOSAC-COBS-2DPAGE; P04004; -.
SWISS-2DPAGE; P04004; -.
EPD; P04004; -.
MaxQB; P04004; -.
PaxDb; P04004; -.
PeptideAtlas; P04004; -.
PRIDE; P04004; -.
DNASU; 7448; -.
Ensembl; ENST00000226218; ENSP00000226218; ENSG00000109072.
GeneID; 7448; -.
KEGG; hsa:7448; -.
UCSC; uc002hbc.4; human.
CTD; 7448; -.
DisGeNET; 7448; -.
GeneCards; VTN; -.
HGNC; HGNC:12724; VTN.
HPA; CAB016695; -.
HPA; CAB016765; -.
HPA; HPA060933; -.
MIM; 193190; gene.
neXtProt; NX_P04004; -.
OpenTargets; ENSG00000109072; -.
PharmGKB; PA37335; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00530000063751; -.
HOGENOM; HOG000133161; -.
HOVERGEN; HBG002902; -.
InParanoid; P04004; -.
KO; K06251; -.
OMA; QPSQEEC; -.
OrthoDB; EOG091G0817; -.
PhylomeDB; P04004; -.
TreeFam; TF332780; -.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P04004; -.
EvolutionaryTrace; P04004; -.
GeneWiki; Vitronectin; -.
GenomeRNAi; 7448; -.
PMAP-CutDB; P04004; -.
PRO; PR:P04004; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000109072; -.
CleanEx; HS_VTN; -.
ExpressionAtlas; P04004; baseline and differential.
Genevisible; P04004; HS.
GO; GO:0071062; C:alphav-beta3 integrin-vitronectin complex; TAS:BHF-UCL.
GO; GO:0005604; C:basement membrane; IEA:Ensembl.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005796; C:Golgi lumen; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0048237; C:rough endoplasmic reticulum lumen; IEA:Ensembl.
GO; GO:0005518; F:collagen binding; IEA:Ensembl.
GO; GO:0050840; F:extracellular matrix binding; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0035987; P:endodermal cell differentiation; IDA:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0030195; P:negative regulation of blood coagulation; IC:BHF-UCL.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IDA:BHF-UCL.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; IDA:BHF-UCL.
GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IDA:BHF-UCL.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; TAS:BHF-UCL.
GO; GO:0090303; P:positive regulation of wound healing; IC:BHF-UCL.
GO; GO:0051258; P:protein polymerization; IEA:Ensembl.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0061302; P:smooth muscle cell-matrix adhesion; IDA:BHF-UCL.
CDD; cd00094; HX; 1.
Gene3D; 2.110.10.10; -; 2.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR020436; Somatomedin_B_chordata.
InterPro; IPR001212; Somatomedin_B_dom.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF01033; Somatomedin_B; 1.
PRINTS; PR00022; SOMATOMEDINB.
SMART; SM00120; HX; 4.
SMART; SM00201; SO; 1.
SUPFAM; SSF50923; SSF50923; 3.
SUPFAM; SSF90188; SSF90188; 1.
PROSITE; PS00024; HEMOPEXIN; 2.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00524; SMB_1; 1.
PROSITE; PS50958; SMB_2; 1.
1: Evidence at protein level;
3D-structure; Cell adhesion; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Heparin-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; Secreted; Signal; Sulfation.
SIGNAL 1 19 {ECO:0000269|PubMed:631332,
ECO:0000269|PubMed:7522053}.
CHAIN 20 478 Vitronectin.
/FTId=PRO_0000036394.
CHAIN 20 398 Vitronectin V65 subunit.
/FTId=PRO_0000036395.
PEPTIDE 20 63 Somatomedin-B.
/FTId=PRO_0000036396.
CHAIN 399 478 Vitronectin V10 subunit.
/FTId=PRO_0000036397.
DOMAIN 20 63 SMB. {ECO:0000255|PROSITE-
ProRule:PRU00350}.
REPEAT 158 202 Hemopexin 1.
REPEAT 203 250 Hemopexin 2.
REPEAT 251 305 Hemopexin 3.
REPEAT 419 472 Hemopexin 4.
REGION 362 395 Heparin-binding.
MOTIF 64 66 Cell attachment site.
SITE 398 399 Cleavage.
MOD_RES 69 69 Phosphothreonine; by CK2; in vitro.
{ECO:0000269|PubMed:9733784}.
MOD_RES 75 75 Sulfotyrosine.
{ECO:0000269|PubMed:17558413}.
MOD_RES 76 76 Phosphothreonine; by CK2; in vitro.
{ECO:0000269|PubMed:9733784}.
MOD_RES 78 78 Sulfotyrosine.
{ECO:0000269|PubMed:17558413}.
MOD_RES 130 130 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 282 282 Sulfotyrosine. {ECO:0000255}.
MOD_RES 312 312 Phosphoserine.
{ECO:0000244|PubMed:16807684,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:17558413}.
MOD_RES 397 397 Phosphoserine; by PKA.
{ECO:0000269|PubMed:1696913,
ECO:0000269|PubMed:2448300}.
MOD_RES 417 417 Sulfotyrosine. {ECO:0000255}.
MOD_RES 420 420 Sulfotyrosine. {ECO:0000255}.
CARBOHYD 86 86 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17558413,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
CARBOHYD 169 169 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 242 242 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218}.
DISULFID 24 40 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 24 28 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:12019263}.
DISULFID 28 58 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 38 51 {ECO:0000255|PROSITE-ProRule:PRU00350}.
DISULFID 38 40 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:12019263}.
DISULFID 44 50 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:12019263}.
DISULFID 51 58 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:12019263}.
DISULFID 293 430 {ECO:0000255|PROSITE-ProRule:PRU00350,
ECO:0000269|PubMed:12019263}.
VARIANT 122 122 A -> S (in dbSNP:rs2227741).
{ECO:0000269|Ref.6}.
/FTId=VAR_012983.
VARIANT 268 268 R -> Q (in dbSNP:rs2227723).
{ECO:0000269|Ref.6}.
/FTId=VAR_012984.
VARIANT 400 400 T -> M (in dbSNP:rs704).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.6}.
/FTId=VAR_012985.
MUTAGEN 69 69 T->A: Abolishes phosphorylation by CK2
and inhibits adhesion and spreading; when
associated with A-76.
{ECO:0000269|PubMed:9733784}.
MUTAGEN 69 69 T->E: Abolishes phosphorylation by CK2
and enhances adhesion and spreading; when
associated with E-76.
{ECO:0000269|PubMed:9733784}.
MUTAGEN 76 76 T->A: Abolishes phosphorylation by CK2
and inhibits adhesion and spreading; when
associated with A-69.
{ECO:0000269|PubMed:9733784}.
MUTAGEN 76 76 T->E: Abolishes phosphorylation by CK2
and enhances adhesion and spreading; when
associated with E-69.
{ECO:0000269|PubMed:9733784}.
CONFLICT 50 50 C -> N (in Ref. 8; AA sequence).
{ECO:0000305}.
CONFLICT 225 225 S -> N (in Ref. 3 and 4). {ECO:0000305}.
CONFLICT 366 366 A -> T (in Ref. 3; CAA26933).
{ECO:0000305}.
STRAND 22 24 {ECO:0000244|PDB:1S4G}.
TURN 25 29 {ECO:0000244|PDB:1SSU}.
STRAND 32 34 {ECO:0000244|PDB:1S4G}.
STRAND 36 39 {ECO:0000244|PDB:1OC0}.
HELIX 44 47 {ECO:0000244|PDB:1OC0}.
TURN 51 53 {ECO:0000244|PDB:1S4G}.
HELIX 54 57 {ECO:0000244|PDB:1OC0}.
STRAND 65 68 {ECO:0000244|PDB:1S4G}.
SEQUENCE 478 AA; 54306 MW; 0D6DB5591CBFEF45 CRC64;
MAPLRPLLIL ALLAWVALAD QESCKGRCTE GFNVDKKCQC DELCSYYQSC CTDYTAECKP
QVTRGDVFTM PEDEYTVYDD GEEKNNATVH EQVGGPSLTS DLQAQSKGNP EQTPVLKPEE
EAPAPEVGAS KPEGIDSRPE TLHPGRPQPP AEEELCSGKP FDAFTDLKNG SLFAFRGQYC
YELDEKAVRP GYPKLIRDVW GIEGPIDAAF TRINCQGKTY LFKGSQYWRF EDGVLDPDYP
RNISDGFDGI PDNVDAALAL PAHSYSGRER VYFFKGKQYW EYQFQHQPSQ EECEGSSLSA
VFEHFAMMQR DSWEDIFELL FWGRTSAGTR QPQFISRDWH GVPGQVDAAM AGRIYISGMA
PRPSLAKKQR FRHRNRKGYR SQRGHSRGRN QNSRRPSRAT WLSLFSSEES NLGANNYDDY
RMDWLVPATC EPIQSVFFFS GDKYYRVNLR TRRVDTVDPP YPRSIAQYWL GCPAPGHL


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