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Reviewed, UniProtKB/Swiss-Prot P48819 (VTNC_PIG)

Last modified November 25, 2008. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Vitronectin
Alternative name(s):
    Serum-spreading factor
      Short name=S-protein
Gene names
Name: VTN
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length459 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (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 structure

Monomer. Interacts with SERPINE1/PAI1 By similarity.

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma.

Domain

The SMB domain mediates interaction with SERPINE1/PAI1 By similarity.

Post-translational modification

Sulfated on 2 tyrosine residues By similarity.

N- and O-glycosylated By similarity.

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.

Sequence similarities

Contains 4 hemopexin-like domains.

Contains 1 SMB (somatomedin-B) domain.

Ontologies

Keywords

   Biological processCell adhesion
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMGlycoprotein
Phosphoprotein
Sulfation
   Technical termDirect protein sequencing

Gene Ontology (GO)

   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalytic activity

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919
Chain20 – 459440Vitronectin
PRO_0000036399

Regions

Domain20 – 6344SMB
Domain138 – 18144Hemopexin-like 1
Domain183 – 22947Hemopexin-like 2
Domain231 – 28151Hemopexin-like 3
Domain406 – 45348Hemopexin-like 4
Motif64 – 663Cell attachment site Potential

Amino acid modifications

Modified residue751Sulfotyrosine Potential
Modified residue781Sulfotyrosine Potential
Modified residue801Sulfotyrosine Potential
Modified residue1481Phosphoserine By similarity
Modified residue2891Phosphoserine By similarity
Modified residue3981Sulfotyrosine Potential
Modified residue4011Sulfotyrosine Potential
Glycosylation871N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Disulfide bond24 ↔ 40Alternate By similarity
Disulfide bond24 ↔ 28Alternate By similarity
Disulfide bond28 ↔ 58Alternate By similarity
Disulfide bond38 ↔ 51Alternate By similarity
Disulfide bond38 ↔ 40Alternate By similarity
Disulfide bond44 ↔ 50 By similarity
Disulfide bond51 ↔ 58Alternate By similarity

Experimental info

Sequence conflict441C → L AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P48819-1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 630E134B0DC706BE

FASTA45952,572
        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 

« Hide

References

[1]"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."
Yoneda A., Kojima K., Matsumoto I., Yamamoto K., Ogawa H.
J. Biochem. 120:954-960(1996) [PubMed: 8982862] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Vitronectin diversity in evolution but uniformity in ligand binding and size of the core polypeptide."
Nakashima N., Miyazaki K., Ishikawa M., Yatohgo T., Ogawa H., Uchibori H., Matsumoto I., Seno N., Hayashi M.
Biochim. Biophys. Acta 1120:1-10(1992) [PubMed: 1372829] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-44.

Cross-references

Sequence databases

D63145 mRNA. Translation: BAA09630.1.
PIRJC5139.
RefSeqNP_999269.1.
UniGeneSsc.32202

3D structure databases

HSSPHSSP built from PDB template 1OC0 based on UniProtKB P04004.
SMRP48819. Positions 20-68.
ModBaseSearch...

PTM databases

GlycoSuiteDBP48819.

Genome annotation databases

GeneID397192.
KEGGssc:397192.

Phylogenomic databases

HOVERGENP48819.

Family and domain databases

InterProIPR000585. Hemopexin.
IPR001212. Somatomedin_B.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 2 hits.
PfamPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameVTNC_PIG
AccessionPrimary (citable) accession number: P48819
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 25, 2008
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents