[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=8982862 [NCBI, ExPASy, EBI, Israel, Japan] Yoneda A., Kojima K., Matsumoto I., Yamamoto K., Ogawa H.; "Porcine vitronectin, the most compact form of single-chain vitronectin: the smallest molecular mass among vitronectins was ascribed to deletion and substitution of base pairs, and proteolytic trimming of the peptide."; J. Biochem. 120:954-960(1996).
[2]	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).

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 (By similarity).
SUBUNIT: Monomer. Interacts with SERPINE1/PAI1 (By similarity).
SUBCELLULAR LOCATION: Secreted, extracellular space.
TISSUE SPECIFICITY: Plasma.
DOMAIN: The SMB domain mediates interaction with SERPINE1/PAI1 (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

D63145; BAA09630.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

JC5139; JC5139.

NP_999269.1; -.

3D structure databases

HSSP

P04004; 1OC0. [HSSP ENTRY / PDB]

P48819; 20-68.

PTM databases

P48819; -.

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

BLOCKS

P48819.

Genome annotation databases

GeneID

397192; -.

KEGG

ssc:397192; -.

Phylogenomic databases

HOVERGEN

P48819; -.

Other

ProtoNet

P48819.

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`	`20 459`	`440`	`Vitronectin.`	`PRO_0000036399`
`DOMAIN`	`20 63`	`44`	`SMB.`
`DOMAIN`	`138 181`	`44`	`Hemopexin-like 1.`
`DOMAIN`	`183 229`	`47`	`Hemopexin-like 2.`
`DOMAIN`	`231 281`	`51`	`Hemopexin-like 3.`
`DOMAIN`	`406 453`	`48`	`Hemopexin-like 4.`
`MOTIF`	`64 66`	`3`	`Cell attachment site (Potential).`
`MOD_RES`	`75 75`		`Sulfotyrosine (Potential).`
`MOD_RES`	`78 78`		`Sulfotyrosine (Potential).`
`MOD_RES`	`80 80`		`Sulfotyrosine (Potential).`
`MOD_RES`	`148 148`		`Phosphoserine (By similarity).`
`MOD_RES`	`289 289`		`Phosphoserine (By similarity).`
`MOD_RES`	`398 398`		`Sulfotyrosine (Potential).`
`MOD_RES`	`401 401`		`Sulfotyrosine (Potential).`
`CARBOHYD`	`87 87`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`146 146`		`N-linked (GlcNAc...) (Potential).`
`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).`
`CONFLICT`	`44 44`		`C -> L (in Ref. 2; AA sequence).`

Sequence information

Length: 459 AA [This is the length of the unprocessed precursor]

Molecular weight: 52572 Da [This is the MW of the unprocessed precursor]

CRC64: 630E134B0DC706BE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAPLRPLLML ALLAWVALAD QESCKGRCTD GFIAERKCQC DELCSYYQSC CTDYVAECKP 

        70         80         90        100        110        120 
QVTRGDVFLQ PDDEYRAYDY HEETRHNTSV QEEQRIPVLL AKTEETPVLK PEEEAPPPGP 

       130        140        150        160        170        180 
QTDDLGVPEE ELCSGKPFDA FTNLKNGSVF AFRGLYCYEL DEKAVRPGYP KLIQDVWGIK 

       190        200        210        220        230        240 
GPIDAAFTRI NCQGKTYLFK GSQYWRFDDG VLDPNYPREI SEGFKGIPDD VDAALALPAH 

       250        260        270        280        290        300 
SYSGRERVYF FKGKQYWEYV FQQQPSREEC EGSSPSDVFA HFALMQRDSW EDIFRLLFWS 

       310        320        330        340        350        360 
HSFGGAIEPR VISQDWLGLP EQVDAAMAGQ IYISGSALKP SQPKMTKSAR RSGKRYRSRR 

       370        380        390        400        410        420 
GRGRGRGHSR SQKSHRQSRS TWLPWFSSEE TGPGGYNYDD YKMDWLVPAT CEPIQSVYFF 

       430        440        450 
SGEEYYRVNL RTQRVDTVTP PYPRSIAQYW LGCPVPDQK

P48819 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