[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=BALB/c; TISSUE=Liver; DOI=10.1016/0378-1119(93)90113-H; PubMed=7505250 [NCBI, ExPASy, EBI, Israel, Japan] Seiffert D., Poenninger J., Binder B.R.; "Organization of the gene encoding mouse vitronectin."; Gene 134:303-304(1993).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=1719529 [NCBI, ExPASy, EBI, Israel, Japan] Seiffert D., Keeton M., Eguchi Y., Sawdey M., Loskutoff D.J.; "Detection of vitronectin mRNA in tissues and cells of the mouse."; Proc. Natl. Acad. Sci. U.S.A. 88:9402-9406(1991).
[3]	NUCLEOTIDE SEQUENCE. STRAIN=BALB/c; TISSUE=Liver; Ehrlich H.J., Richter B., von der Ahe D., Preissner K.T.; "Primary structure of vitronectins and homology with other proteins."; (In) Preissner K.T., Rosenblatt S., Kost C., Wegerhoff J., Mosher D.F. (eds.); Biology of vitronectins, pp.1-1, Elsevier, Amsterdam (1996).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Liver; Lai D.-Z.; "Construction of a robust CHO cell-line for biopharmaceutical production."; Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Retina; 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).
[6]	PROTEIN SEQUENCE OF 20-44. DOI=10.1016/0167-4838(92)90417-C; PubMed=1372829 [NCBI, ExPASy, EBI, Israel, Japan] Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H., Matsumoto I., Seno N., Hayashi M.; "Vitronectin diversity in evolution but uniformity in ligand binding and size of the core polypeptide."; Biochim. Biophys. Acta 1120:1-10(1992).
[7]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0604559; PubMed=17330941 [NCBI, ExPASy, EBI, Israel, Japan] Bernhard O.K., Kapp E.A., Simpson R.J.; "Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."; J. Proteome Res. 6:987-995(2007).

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.
SUBUNIT: Interacts with SERPINE1/PAI1 and insulin (By similarity).
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 (By similarity).
PTM: Sulfated on 2 tyrosine residues (By similarity).
PTM: N- and O-glycosylated (By similarity).
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.

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

X72091; CAA50981.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M77123; AAA40558.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X63003; CAA44732.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF440693; AAL34534.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018521; AAH18521.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S19894; SGMSV.

NP_035837.1; -.

3D structure databases

HSSP

P04004; 1OC0. [HSSP ENTRY / PDB]

P29788; 20-70.

PTM databases

P29788; -.

Organism-specific databases

MGI

MGI:98940; Vtn.

Gene expression databases

ArrayExpress

P29788; -.

CleanEx

MM_VTN; -.

GermOnline

ENSMUSG00000017344; Mus musculus.

Ontologies

GO:0005578;	Cellular component: proteinaceous extracellular matrix (inferred from direct assay from MGI).
GO:0003824;	Molecular function: catalytic activity (inferred from electronic annotation from InterPro).
GO:0008201;	Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0046872;	Molecular function: metal ion binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007160;	Biological process: cell-matrix adhesion (inferred from direct assay from MGI).
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).

Genome annotation databases

Ensembl

ENSMUSG00000017344; Mus musculus. [Contig view]

GeneID

22370; -.

KEGG

mmu:22370; -.

Phylogenomic databases

HOGENOM

P29788; -.

HOVERGEN

P29788; -.

Other

NextBio

302703; -.

SOURCE

Vtn; Mus musculus.

UniRef

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

Keywords

Cell adhesion; Direct protein sequencing; Glycoprotein; Heparin-binding; Phosphoprotein; 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_0000036398`
`DOMAIN`	`20 63`	`44`	`SMB.`
`DOMAIN`	`160 203`	`44`	`Hemopexin-like 1.`
`DOMAIN`	`205 251`	`47`	`Hemopexin-like 2.`
`DOMAIN`	`253 303`	`51`	`Hemopexin-like 3.`
`DOMAIN`	`426 473`	`48`	`Hemopexin-like 4.`
`REGION`	`366 399`	`34`	`Heparin-binding (By similarity).`
`MOTIF`	`64 66`	`3`	`Cell attachment site.`
`MOD_RES`	`75 75`		`Sulfotyrosine (Potential).`
`MOD_RES`	`78 78`		`Sulfotyrosine (Potential).`
`MOD_RES`	`80 80`		`Sulfotyrosine (Potential).`
`MOD_RES`	`170 170`		`Phosphoserine (By similarity).`
`MOD_RES`	`278 278`		`Sulfotyrosine (Potential).`
`MOD_RES`	`281 281`		`Sulfotyrosine (Potential).`
`MOD_RES`	`311 311`		`Phosphoserine (By similarity).`
`MOD_RES`	`398 398`		`Phosphoserine; by PKA (By similarity).`
`MOD_RES`	`416 416`		`Sulfotyrosine (Potential).`
`MOD_RES`	`419 419`		`Sulfotyrosine (Potential).`
`MOD_RES`	`421 421`		`Sulfotyrosine (Potential).`
`CARBOHYD`	`86 86`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`168 168`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`241 241`		`N-linked (GlcNAc...).`
`DISULFID`	`24 40`		`Alternate (By similarity).`
`DISULFID`	`24 28`		`Alternate (By similarity).`
`DISULFID`	`28 58`		`Alternate (By similarity).`
`DISULFID`	`38 51`		`Alternate (By similarity).`
`DISULFID`	`38 40`		`Alternate (By similarity).`
`DISULFID`	`44 50`		`By similarity.`
`DISULFID`	`51 58`		`Alternate (By similarity).`
`DISULFID`	`292 431`		`By similarity.`
`CONFLICT`	`179 180`		`CY -> RC (in Ref. 4; AAL34534).`
`CONFLICT`	`281 281`		`Y -> H (in Ref. 4; AAL34534).`
`CONFLICT`	`369 369`		`K -> P (in Ref. 4; AAL34534).`
`CONFLICT`	`383 384`		`Missing (in Ref. 2; AAA40558).`
`CONFLICT`	`416 416`		`Y -> K (in Ref. 2; AAA40558).`

Sequence information

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

Molecular weight: 54849 Da [This is the MW of the unprocessed precursor]

CRC64: EB0C772F8BD6A166 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC CADYMEQCKP 

        70         80         90        100        110        120 
QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP GDLNPRTDGT LKPTAFLDPE 

       130        140        150        160        170        180 
EQPSTPAPKV EQQEEILRPD TTDQGTPEFP EEELCSGKPF DAFTDLKNGS LFAFRGQYCY 

       190        200        210        220        230        240 
ELDETAVRPG YPKLIQDVWG IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR 

       250        260        270        280        290        300 
NISEGFSGIP DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV 

       310        320        330        340        350        360 
FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA GRIYVTGSLS 

       370        380        390        400        410        420 
HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS IWFSLFSSEE SGLGTYNNYD 

       430        440        450        460        470 
YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL RTRRVDSVNP PYPRSIAQYW LGCPTSEK

P29788 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