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Protein

Vitronectin

Gene

Vtn

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_294181. Regulation of Complement cascade.
REACT_319261. Integrin cell surface interactions.
REACT_326610. Syndecan interactions.
REACT_332220. Molecules associated with elastic fibres.
REACT_354321. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Vitronectin
Short name:
VN
Alternative name(s):
S-protein
Serum-spreading factor
Gene namesi
Name:Vtn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:98940. Vtn.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 19191 PublicationAdd
BLAST
Chaini20 – 478459VitronectinPRO_0000036398Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi24 ↔ 40Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi24 ↔ 28Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi28 ↔ 58Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 51Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi38 ↔ 40Alternate; alternatePROSITE-ProRule annotation
Disulfide bondi44 ↔ 50PROSITE-ProRule annotation
Disulfide bondi51 ↔ 58Alternate; alternatePROSITE-ProRule annotation
Modified residuei69 – 691PhosphothreonineBy similarity
Modified residuei75 – 751SulfotyrosineSequence Analysis
Modified residuei78 – 781SulfotyrosineSequence Analysis
Modified residuei80 – 801SulfotyrosineSequence Analysis
Glycosylationi86 – 861N-linked (GlcNAc...)Sequence Analysis
Glycosylationi168 – 1681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi241 – 2411N-linked (GlcNAc...)1 Publication
Modified residuei278 – 2781SulfotyrosineSequence Analysis
Modified residuei281 – 2811SulfotyrosineSequence Analysis
Disulfide bondi292 ↔ 431PROSITE-ProRule annotation
Modified residuei311 – 3111PhosphoserineBy similarity
Modified residuei398 – 3981Phosphoserine; by PKABy similarity
Modified residuei416 – 4161SulfotyrosineSequence Analysis
Modified residuei419 – 4191SulfotyrosineSequence Analysis
Modified residuei421 – 4211SulfotyrosineSequence Analysis

Post-translational modificationi

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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Sulfation

Proteomic databases

MaxQBiP29788.
PaxDbiP29788.
PRIDEiP29788.

PTM databases

PhosphoSiteiP29788.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP29788.
CleanExiMM_VTN.
GenevisibleiP29788. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiP29788. 1 interaction.
MINTiMINT-4121605.
STRINGi10090.ENSMUSP00000017488.

Structurei

3D structure databases

ProteinModelPortaliP29788.
SMRiP29788. Positions 20-70, 154-344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 6344SMBPROSITE-ProRule annotationAdd
BLAST
Repeati157 – 20145Hemopexin 1Add
BLAST
Repeati202 – 24948Hemopexin 2Add
BLAST
Repeati250 – 30455Hemopexin 3Add
BLAST
Repeati420 – 47354Hemopexin 4Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni366 – 39934Heparin-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi64 – 663Cell attachment site

Domaini

The SMB domain mediates interaction with SERPINE1/PAI1. The heparin-binding domain mediates interaction with insulin (By similarity).By similarity

Sequence similaritiesi

Contains 4 hemopexin repeats.Curated
Contains 1 SMB (somatomedin-B) domain.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiNOG245064.
GeneTreeiENSGT00530000063751.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP29788.
KOiK06251.
OMAiLFWGRSS.
OrthoDBiEOG7MH0ZG.
PhylomeDBiP29788.
TreeFamiTF332780.

Family and domain databases

Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC
60 70 80 90 100
CADYMEQCKP QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP
110 120 130 140 150
GDLNPRTDGT LKPTAFLDPE EQPSTPAPKV EQQEEILRPD TTDQGTPEFP
160 170 180 190 200
EEELCSGKPF DAFTDLKNGS LFAFRGQYCY ELDETAVRPG YPKLIQDVWG
210 220 230 240 250
IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR NISEGFSGIP
260 270 280 290 300
DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV
310 320 330 340 350
FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA
360 370 380 390 400
GRIYVTGSLS HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS
410 420 430 440 450
IWFSLFSSEE SGLGTYNNYD YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL
460 470
RTRRVDSVNP PYPRSIAQYW LGCPTSEK
Length:478
Mass (Da):54,849
Last modified:October 1, 1996 - v2
Checksum:iEB0C772F8BD6A166
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1802CY → RC in AAL34534 (Ref. 4) Curated
Sequence conflicti186 – 1861A → T in AAH12690 (PubMed:15489334).Curated
Sequence conflicti281 – 2811Y → H in AAL34534 (Ref. 4) Curated
Sequence conflicti348 – 3481A → T in BAB27809 (PubMed:16141072).Curated
Sequence conflicti369 – 3691K → P in AAL34534 (Ref. 4) Curated
Sequence conflicti383 – 3842Missing in AAA40558 (PubMed:1719529).Curated
Sequence conflicti416 – 4161Y → K in AAA40558 (PubMed:1719529).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25106.1.
PIRiS19894. SGMSV.
RefSeqiNP_035837.1. NM_011707.2.
UniGeneiMm.3667.

Genome annotation databases

EnsembliENSMUST00000017488; ENSMUSP00000017488; ENSMUSG00000017344.
GeneIDi22370.
KEGGimmu:22370.
UCSCiuc007kjk.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS25106.1.
PIRiS19894. SGMSV.
RefSeqiNP_035837.1. NM_011707.2.
UniGeneiMm.3667.

3D structure databases

ProteinModelPortaliP29788.
SMRiP29788. Positions 20-70, 154-344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP29788. 1 interaction.
MINTiMINT-4121605.
STRINGi10090.ENSMUSP00000017488.

PTM databases

PhosphoSiteiP29788.

Proteomic databases

MaxQBiP29788.
PaxDbiP29788.
PRIDEiP29788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017488; ENSMUSP00000017488; ENSMUSG00000017344.
GeneIDi22370.
KEGGimmu:22370.
UCSCiuc007kjk.2. mouse.

Organism-specific databases

CTDi7448.
MGIiMGI:98940. Vtn.

Phylogenomic databases

eggNOGiNOG245064.
GeneTreeiENSGT00530000063751.
HOGENOMiHOG000133161.
HOVERGENiHBG002902.
InParanoidiP29788.
KOiK06251.
OMAiLFWGRSS.
OrthoDBiEOG7MH0ZG.
PhylomeDBiP29788.
TreeFamiTF332780.

Enzyme and pathway databases

ReactomeiREACT_294181. Regulation of Complement cascade.
REACT_319261. Integrin cell surface interactions.
REACT_326610. Syndecan interactions.
REACT_332220. Molecules associated with elastic fibres.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiVtn. mouse.
NextBioi302703.
PROiP29788.
SOURCEiSearch...

Gene expression databases

BgeeiP29788.
CleanExiMM_VTN.
GenevisibleiP29788. MM.

Family and domain databases

Gene3Di2.110.10.10. 3 hits.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR020436. Somatomedin_B_chordata.
IPR001212. Somatomedin_B_dom.
[Graphical view]
PfamiPF00045. Hemopexin. 4 hits.
PF01033. Somatomedin_B. 1 hit.
[Graphical view]
PRINTSiPR00022. SOMATOMEDINB.
SMARTiSM00120. HX. 4 hits.
SM00201. SO. 1 hit.
[Graphical view]
SUPFAMiSSF50923. SSF50923. 3 hits.
PROSITEiPS00024. HEMOPEXIN. 2 hits.
PS51642. HEMOPEXIN_2. 4 hits.
PS00524. SMB_1. 1 hit.
PS50958. SMB_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiVTNC_MOUSE
AccessioniPrimary (citable) accession number: P29788
Secondary accession number(s): Q5SYG4
, Q8VII4, Q91X32, Q9D080
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 153 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.