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P29788

- VTNC_MOUSE

UniProt

P29788 - VTNC_MOUSE

Protein

Vitronectin

Gene

Vtn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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

    1. extracellular matrix binding Source: MGI
    2. heparin binding Source: UniProtKB-KW
    3. polysaccharide binding Source: InterPro
    4. scavenger receptor activity Source: InterPro

    GO - Biological processi

    1. cell adhesion mediated by integrin Source: Ensembl
    2. cell-matrix adhesion Source: MGI
    3. extracellular matrix organization Source: MGI
    4. immune response Source: InterPro
    5. negative regulation of endopeptidase activity Source: Ensembl
    6. positive regulation of cell-substrate adhesion Source: MGI
    7. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
    8. positive regulation of protein binding Source: Ensembl
    9. positive regulation of receptor-mediated endocytosis Source: Ensembl
    10. positive regulation of smooth muscle cell migration Source: Ensembl
    11. smooth muscle cell-matrix adhesion Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Heparin-binding

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196644. Syndecan interactions.
    REACT_198562. Regulation of Complement cascade.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_216309. Integrin cell surface interactions.

    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: Chromosome 11

    Organism-specific databases

    MGIiMGI:98940. Vtn.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: UniProtKB-SubCell
    2. proteinaceous extracellular matrix Source: MGI

    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

    PaxDbiP29788.
    PRIDEiP29788.

    PTM databases

    PhosphoSiteiP29788.

    Expressioni

    Tissue specificityi

    Plasma.

    Gene expression databases

    BgeeiP29788.
    CleanExiMM_VTN.
    GenevestigatoriP29788.

    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, 154-345.
    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.
    InParanoidiQ91X32.
    KOiK06251.
    OMAiLLQRDSW.
    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

    MAPLRPFFIL ALVAWVSLAD QESCKGRCTQ GFMASKKCQC DELCTYYQSC    50
    CADYMEQCKP QVTRGDVFTM PEDDYWSYDY VEEPKNNTNT GVQPENTSPP 100
    GDLNPRTDGT LKPTAFLDPE EQPSTPAPKV EQQEEILRPD TTDQGTPEFP 150
    EEELCSGKPF DAFTDLKNGS LFAFRGQYCY ELDETAVRPG YPKLIQDVWG 200
    IEGPIDAAFT RINCQGKTYL FKGSQYWRFE DGVLDPGYPR NISEGFSGIP 250
    DNVDAAFALP AHRYSGRERV YFFKGKQYWE YEFQQQPSQE ECEGSSLSAV 300
    FEHFALLQRD SWENIFELLF WGRSSDGARE PQFISRNWHG VPGKVDAAMA 350
    GRIYVTGSLS HSAQAKKQKS KRRSRKRYRS RRGRGHRRSQ SSNSRRSSRS 400
    IWFSLFSSEE SGLGTYNNYD YDMDWLVPAT CEPIQSVYFF SGDKYYRVNL 450
    RTRRVDSVNP PYPRSIAQYW LGCPTSEK 478
    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. 1 PublicationCurated
    Sequence conflicti186 – 1861A → T in AAH12690. (PubMed:15489334)Curated
    Sequence conflicti281 – 2811Y → H in AAL34534. 1 PublicationCurated
    Sequence conflicti348 – 3481A → T in BAB27809. (PubMed:16141072)Curated
    Sequence conflicti369 – 3691K → P in AAL34534. 1 PublicationCurated
    Sequence conflicti383 – 3842Missing in AAA40558. (PubMed:1719529)Curated
    Sequence conflicti416 – 4161Y → K in AAA40558. (PubMed:1719529)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS25106.1.
    PIRi S19894. SGMSV.
    RefSeqi NP_035837.1. NM_011707.2.
    UniGenei Mm.3667.

    3D structure databases

    ProteinModelPortali P29788.
    SMRi P29788. Positions 20-70, 154-345.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P29788. 1 interaction.
    MINTi MINT-4121605.
    STRINGi 10090.ENSMUSP00000017488.

    PTM databases

    PhosphoSitei P29788.

    Proteomic databases

    PaxDbi P29788.
    PRIDEi P29788.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000017488 ; ENSMUSP00000017488 ; ENSMUSG00000017344 .
    GeneIDi 22370.
    KEGGi mmu:22370.
    UCSCi uc007kjk.2. mouse.

    Organism-specific databases

    CTDi 7448.
    MGIi MGI:98940. Vtn.

    Phylogenomic databases

    eggNOGi NOG245064.
    GeneTreei ENSGT00530000063751.
    HOGENOMi HOG000133161.
    HOVERGENi HBG002902.
    InParanoidi Q91X32.
    KOi K06251.
    OMAi LLQRDSW.
    OrthoDBi EOG7MH0ZG.
    PhylomeDBi P29788.
    TreeFami TF332780.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196644. Syndecan interactions.
    REACT_198562. Regulation of Complement cascade.
    REACT_198998. Molecules associated with elastic fibres.
    REACT_216309. Integrin cell surface interactions.

    Miscellaneous databases

    ChiTaRSi VTN. mouse.
    NextBioi 302703.
    PROi P29788.
    SOURCEi Search...

    Gene expression databases

    Bgeei P29788.
    CleanExi MM_VTN.
    Genevestigatori P29788.

    Family and domain databases

    Gene3Di 2.110.10.10. 3 hits.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR020436. Somatomedin_B_chordata.
    IPR001212. Somatomedin_B_dom.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 4 hits.
    PF01033. Somatomedin_B. 1 hit.
    [Graphical view ]
    PRINTSi PR00022. SOMATOMEDINB.
    SMARTi SM00120. HX. 4 hits.
    SM00201. SO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50923. SSF50923. 3 hits.
    PROSITEi PS00024. HEMOPEXIN. 2 hits.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00524. SMB_1. 1 hit.
    PS50958. SMB_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 144 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