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P28654

- PGS2_MOUSE

UniProt

P28654 - PGS2_MOUSE

Protein

Decorin

Gene

Dcn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Dec 1992)
      Previous versions | rss
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    Functioni

    May affect the rate of fibrils formation.

    GO - Molecular functioni

    1. extracellular matrix binding Source: MGI
    2. glycosaminoglycan binding Source: MGI

    GO - Biological processi

    1. aging Source: Ensembl
    2. kidney development Source: Ensembl
    3. peptide cross-linking via chondroitin 4-sulfate glycosaminoglycan Source: MGI
    4. placenta development Source: Ensembl
    5. response to lipopolysaccharide Source: Ensembl
    6. response to mechanical stimulus Source: Ensembl
    7. skeletal muscle tissue development Source: Ensembl
    8. wound healing Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_196514. Chondroitin sulfate biosynthesis.
    REACT_196540. Dermatan sulfate biosynthesis.
    REACT_196606. ECM proteoglycans.
    REACT_198981. CS/DS degradation.
    REACT_199052. Degradation of the extracellular matrix.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Decorin
    Alternative name(s):
    Bone proteoglycan II
    PG-S2
    PG40
    Gene namesi
    Name:Dcn
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:94872. Dcn.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type VI trimer Source: Ensembl
    2. extracellular space Source: Ensembl
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Propeptidei17 – 3014PRO_0000032711Add
    BLAST
    Chaini31 – 354324DecorinPRO_0000032712Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341O-linked (Xyl...) (glycosaminoglycan)By similarity
    Disulfide bondi49 ↔ 55By similarity
    Disulfide bondi53 ↔ 62By similarity
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi308 ↔ 341By similarity

    Post-translational modificationi

    The attached glycosaminoglycan chain can be either chondroitin sulfate or dermatan sulfate depending upon the tissue of origin.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Proteoglycan

    Proteomic databases

    MaxQBiP28654.
    PaxDbiP28654.
    PRIDEiP28654.

    PTM databases

    PhosphoSiteiP28654.

    Expressioni

    Gene expression databases

    ArrayExpressiP28654.
    BgeeiP28654.
    CleanExiMM_DCN.
    GenevestigatoriP28654.

    Interactioni

    Subunit structurei

    Binds to type I and type II collagen, fibronectin and TGF-beta. Forms a ternary complex with MFAP2 and ELN. Interacts with DPT By similarity.By similarity

    Protein-protein interaction databases

    IntActiP28654. 1 interaction.
    MINTiMINT-4107388.

    Structurei

    3D structure databases

    ProteinModelPortaliP28654.
    SMRiP28654. Positions 48-350.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati68 – 8821LRR 1Add
    BLAST
    Repeati89 – 11224LRR 2Add
    BLAST
    Repeati113 – 13624LRR 3Add
    BLAST
    Repeati137 – 15721LRR 4Add
    BLAST
    Repeati158 – 18124LRR 5Add
    BLAST
    Repeati182 – 20726LRR 6Add
    BLAST
    Repeati208 – 22821LRR 7Add
    BLAST
    Repeati229 – 25224LRR 8Add
    BLAST
    Repeati253 – 27624LRR 9Add
    BLAST
    Repeati277 – 29923LRR 10Add
    BLAST
    Repeati300 – 32930LRR 11Add
    BLAST
    Repeati330 – 35425LRR 12Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi49 – 6214Cys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 12 LRR (leucine-rich) repeats.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000261690.
    HOVERGENiHBG016052.
    InParanoidiP28654.
    KOiK04660.
    OMAiPLGPVCP.
    OrthoDBiEOG76739V.
    PhylomeDBiP28654.
    TreeFamiTF334562.

    Family and domain databases

    InterProiIPR028549. Decorin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view]
    PANTHERiPTHR24369:SF5. PTHR24369:SF5. 1 hit.
    PfamiPF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002490. SLRP_I. 1 hit.
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P28654-1 [UniParc]FASTAAdd to Basket

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    MKATLIFFLL AQVSWAGPFE QRGLFDFMLE DEASGIIPYD PDNPLISMCP    50
    YRCQCHLRVV QCSDLGLDKV PWDFPPDTTL LDLQNNKITE IKEGAFKNLK 100
    DLHTLILVNN KISKISPEAF KPLVKLERLY LSKNQLKELP EKMPRTLQEL 150
    RVHENEITKL RKSDFNGLNN VLVIELGGNP LKNSGIENGA FQGLKSLSYI 200
    RISDTNITAI PQGLPTSLTE VHLDGNKITK VDAPSLKGLI NLSKLGLSFN 250
    SITVMENGSL ANVPHLRELH LDNNKLLRVP AGLAQHKYIQ VVYLHNNNIS 300
    AVGQNDFCRA GHPSRKASYS AVSLYGNPVR YWEIFPNTFR CVYVRSAIQL 350
    GNYK 354
    Length:354
    Mass (Da):39,809
    Last modified:December 1, 1992 - v1
    Checksum:iF05B5CC08DCABF6F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53929 mRNA. Translation: CAA37876.1.
    CCDSiCCDS24141.1.
    PIRiA55454.
    RefSeqiNP_001177380.1. NM_001190451.1.
    NP_031859.1. NM_007833.5.
    UniGeneiMm.56769.

    Genome annotation databases

    EnsembliENSMUST00000105287; ENSMUSP00000100924; ENSMUSG00000019929.
    ENSMUST00000163448; ENSMUSP00000131431; ENSMUSG00000019929.
    GeneIDi13179.
    KEGGimmu:13179.
    UCSCiuc007gwx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53929 mRNA. Translation: CAA37876.1 .
    CCDSi CCDS24141.1.
    PIRi A55454.
    RefSeqi NP_001177380.1. NM_001190451.1.
    NP_031859.1. NM_007833.5.
    UniGenei Mm.56769.

    3D structure databases

    ProteinModelPortali P28654.
    SMRi P28654. Positions 48-350.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P28654. 1 interaction.
    MINTi MINT-4107388.

    PTM databases

    PhosphoSitei P28654.

    Proteomic databases

    MaxQBi P28654.
    PaxDbi P28654.
    PRIDEi P28654.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000105287 ; ENSMUSP00000100924 ; ENSMUSG00000019929 .
    ENSMUST00000163448 ; ENSMUSP00000131431 ; ENSMUSG00000019929 .
    GeneIDi 13179.
    KEGGi mmu:13179.
    UCSCi uc007gwx.2. mouse.

    Organism-specific databases

    CTDi 1634.
    MGIi MGI:94872. Dcn.

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000261690.
    HOVERGENi HBG016052.
    InParanoidi P28654.
    KOi K04660.
    OMAi PLGPVCP.
    OrthoDBi EOG76739V.
    PhylomeDBi P28654.
    TreeFami TF334562.

    Enzyme and pathway databases

    Reactomei REACT_196489. A tetrasaccharide linker sequence is required for GAG synthesis.
    REACT_196514. Chondroitin sulfate biosynthesis.
    REACT_196540. Dermatan sulfate biosynthesis.
    REACT_196606. ECM proteoglycans.
    REACT_198981. CS/DS degradation.
    REACT_199052. Degradation of the extracellular matrix.

    Miscellaneous databases

    ChiTaRSi DCN. mouse.
    NextBioi 283292.
    PROi P28654.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P28654.
    Bgeei P28654.
    CleanExi MM_DCN.
    Genevestigatori P28654.

    Family and domain databases

    InterProi IPR028549. Decorin.
    IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR000372. LRR-contain_N.
    IPR016352. SLRP_I_decor/aspor/byglycan.
    [Graphical view ]
    PANTHERi PTHR24369:SF5. PTHR24369:SF5. 1 hit.
    Pfami PF13855. LRR_8. 3 hits.
    PF01462. LRRNT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002490. SLRP_I. 1 hit.
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00013. LRRNT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Naitoh Y., Suzuki S.
      Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: NIH Swiss.
      Tissue: Fibroblast.
    2. "The murine decorin. Complete cDNA cloning, genomic organization, chromosomal assignment, and expression during organogenesis and tissue differentiation."
      Scholzen T., Solursh M., Suzuki S., Reiter R., Morgan J.L., Buchberg A.M., Siracusa L.D., Iozzo R.V.
      J. Biol. Chem. 269:28270-28281(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiPGS2_MOUSE
    AccessioniPrimary (citable) accession number: P28654
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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