Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P29788 (VTNC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vitronectin

Short name=VN
Alternative name(s):
S-protein
Serum-spreading factor
Gene names
Name:Vtn
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length478 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.

Subunit structure

Interacts with SERPINE1/PAI1, insulin and C1QBP By similarity.

Subcellular location

Secretedextracellular space.

Tissue specificity

Plasma.

Domain

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin 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 repeats.

Contains 1 SMB (somatomedin-B) domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentSecreted
   DomainRepeat
Signal
   LigandHeparin-binding
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Sulfation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell adhesion mediated by integrin

Inferred from electronic annotation. Source: Ensembl

cell-matrix adhesion

Inferred from direct assay PubMed 15728191. Source: MGI

extracellular matrix organization

Inferred from direct assay PubMed 18757743. Source: MGI

immune response

Inferred from electronic annotation. Source: InterPro

negative regulation of endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell-substrate adhesion

Inferred from direct assay PubMed 18757743. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor-mediated endocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of smooth muscle cell migration

Inferred from electronic annotation. Source: Ensembl

smooth muscle cell-matrix adhesion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteinaceous extracellular matrix

Inferred from direct assay PubMed 15728191. Source: MGI

   Molecular_functionextracellular matrix binding

Inferred from direct assay PubMed 18757743. Source: MGI

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

polysaccharide binding

Inferred from electronic annotation. Source: InterPro

scavenger receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.9
Chain20 – 478459Vitronectin
PRO_0000036398

Regions

Domain20 – 6344SMB
Repeat157 – 20145Hemopexin 1
Repeat202 – 24948Hemopexin 2
Repeat250 – 30455Hemopexin 3
Repeat420 – 47354Hemopexin 4
Region366 – 39934Heparin-binding By similarity
Motif64 – 663Cell attachment site

Amino acid modifications

Modified residue691Phosphothreonine By similarity
Modified residue751Sulfotyrosine Potential
Modified residue781Sulfotyrosine Potential
Modified residue801Sulfotyrosine Potential
Modified residue2781Sulfotyrosine Potential
Modified residue2811Sulfotyrosine Potential
Modified residue3111Phosphoserine By similarity
Modified residue3981Phosphoserine; by PKA By similarity
Modified residue4161Sulfotyrosine Potential
Modified residue4191Sulfotyrosine Potential
Modified residue4211Sulfotyrosine Potential
Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation1681N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Ref.10
Disulfide bond24 ↔ 40Alternate; alternate By similarity
Disulfide bond24 ↔ 28Alternate; alternate By similarity
Disulfide bond28 ↔ 58Alternate; alternate By similarity
Disulfide bond38 ↔ 51Alternate; alternate By similarity
Disulfide bond38 ↔ 40Alternate; alternate By similarity
Disulfide bond44 ↔ 50 By similarity
Disulfide bond51 ↔ 58Alternate; alternate By similarity
Disulfide bond292 ↔ 431 By similarity

Experimental info

Sequence conflict179 – 1802CY → RC in AAL34534. Ref.4
Sequence conflict1861A → T in AAH12690. Ref.8
Sequence conflict2811Y → H in AAL34534. Ref.4
Sequence conflict3481A → T in BAB27809. Ref.5
Sequence conflict3691K → P in AAL34534. Ref.4
Sequence conflict383 – 3842Missing in AAA40558. Ref.2
Sequence conflict4161Y → K in AAA40558. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P29788 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: EB0C772F8BD6A166

FASTA47854,849
        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 

« Hide

References

« Hide 'large scale' references
[1]"Organization of the gene encoding mouse vitronectin."
Seiffert D., Poenninger J., Binder B.R.
Gene 134:303-304(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: BALB/c.
Tissue: Liver.
[2]"Detection of vitronectin mRNA in tissues and cells of the mouse."
Seiffert D., Keeton M., Eguchi Y., Sawdey M., Loskutoff D.J.
Proc. Natl. Acad. Sci. U.S.A. 88:9402-9406(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[3]"Primary structure of vitronectins and homology with other proteins."
Ehrlich H.J., Richter B., von der Ahe D., Preissner K.T.
(In) Preissner K.T., Rosenblatt S., Kost C., Wegerhoff J., Mosher D.F. (eds.); Biology of vitronectins, pp.1-1, Elsevier, Amsterdam (1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[4]"Construction of a robust CHO cell-line for biopharmaceutical production."
Lai D.-Z.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[5]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo and Gall bladder.
[6]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[7]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Salivary gland.
[9]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 20-44.
[10]"Enhanced analysis of the mouse plasma proteome using cysteine-containing tryptic glycopeptides."
Bernhard O.K., Kapp E.A., Simpson R.J.
J. Proteome Res. 6:987-995(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-241.
Strain: C57BL/6.
Tissue: Plasma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X72091 Genomic DNA. Translation: CAA50981.1.
M77123 mRNA. Translation: AAA40558.1.
X63003 mRNA. Translation: CAA44732.1.
AF440693 mRNA. Translation: AAL34534.1.
AK011736 mRNA. Translation: BAB27809.1.
AK090325 mRNA. Translation: BAC41171.1.
AL591177 Genomic DNA. Translation: CAI25547.1.
CH466556 Genomic DNA. Translation: EDL15582.1.
BC012690 mRNA. Translation: AAH12690.1.
CCDSCCDS25106.1.
PIRSGMSV. S19894.
RefSeqNP_035837.1. NM_011707.2.
UniGeneMm.3667.

3D structure databases

ProteinModelPortalP29788.
SMRP29788. Positions 20-70, 154-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP29788. 1 interaction.
MINTMINT-4121605.
STRING10090.ENSMUSP00000017488.

PTM databases

PhosphoSiteP29788.

Proteomic databases

PaxDbP29788.
PRIDEP29788.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017488; ENSMUSP00000017488; ENSMUSG00000017344.
GeneID22370.
KEGGmmu:22370.
UCSCuc007kjk.2. mouse.

Organism-specific databases

CTD7448.
MGIMGI:98940. Vtn.

Phylogenomic databases

eggNOGNOG245064.
GeneTreeENSGT00530000063751.
HOGENOMHOG000133161.
HOVERGENHBG002902.
InParanoidQ91X32.
KOK06251.
OMALLQRDSW.
OrthoDBEOG7MH0ZG.
PhylomeDBP29788.
TreeFamTF332780.

Gene expression databases

BgeeP29788.
CleanExMM_VTN.
GenevestigatorP29788.

Family and domain databases

Gene3D2.110.10.10. 3 hits.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSPR00022. SOMATOMEDINB.
SMARTSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMSSF50923. SSF50923. 3 hits.
PROSITEPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVTN. mouse.
NextBio302703.
PROP29788.
SOURCESearch...

Entry information

Entry nameVTNC_MOUSE
AccessionPrimary (citable) accession number: P29788
Secondary accession number(s): Q5SYG4 expand/collapse secondary AC list , Q8VII4, Q91X32, Q9D080
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot