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Q9R001

- ATS5_MOUSE

UniProt

Q9R001 - ATS5_MOUSE

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 5

Gene

Adamts5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. May play a role in proteolytic processing mostly during the peri-implantation period.

    Catalytic activityi

    Cleaves aggrecan at the 392-Glu-|-Ala-393 site.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi209 – 2091Zinc; in inhibited formBy similarity
    Metal bindingi410 – 4101Zinc; catalyticBy similarity
    Active sitei411 – 4111PROSITE-ProRule annotation
    Metal bindingi414 – 4141Zinc; catalyticBy similarity
    Metal bindingi420 – 4201Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. metallopeptidase activity Source: MGI
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. defense response to bacterium Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199052. Degradation of the extracellular matrix.
    REACT_211817. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.225.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 5 (EC:3.4.24.-)
    Short name:
    ADAM-TS 5
    Short name:
    ADAM-TS5
    Short name:
    ADAMTS-5
    Alternative name(s):
    ADMP-2
    Aggrecanase-2
    Implantin
    Gene namesi
    Name:Adamts5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:1346321. Adamts5.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus 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 – 2121Sequence AnalysisAdd
    BLAST
    Propeptidei22 – 261240Sequence AnalysisPRO_0000029172Add
    BLAST
    Chaini262 – 930669A disintegrin and metalloproteinase with thrombospondin motifs 5PRO_0000029173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi342 ↔ 394By similarity
    Disulfide bondi371 ↔ 376By similarity
    Disulfide bondi388 ↔ 471By similarity
    Disulfide bondi426 ↔ 455By similarity
    Disulfide bondi497 ↔ 519By similarity
    Glycosylationi498 – 4981N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi508 ↔ 529By similarity
    Disulfide bondi514 ↔ 548By similarity
    Disulfide bondi542 ↔ 553By similarity
    Glycosylationi570 – 5701C-linked (Man)By similarity
    Glycosylationi573 – 5731C-linked (Man)By similarity
    Disulfide bondi579 ↔ 616By similarity
    Glycosylationi582 – 5821O-linked (Fuc...)By similarity
    Disulfide bondi583 ↔ 621By similarity
    Disulfide bondi594 ↔ 606By similarity
    Glycosylationi728 – 7281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi802 – 8021N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi807 – 8071N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity
    C- and O-glycosylated By similarity. O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation can mediate the efficient secretion of ADAMTS family members. Can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion By similarity.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PRIDEiQ9R001.

    PTM databases

    PhosphoSiteiQ9R001.

    Expressioni

    Developmental stagei

    Expressed specifically in the peri-implantation period in embryo and trophoblast and at low or undetectable level thereafter.

    Gene expression databases

    ArrayExpressiQ9R001.
    BgeeiQ9R001.
    GenevestigatoriQ9R001.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000023611.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9R001.
    SMRiQ9R001. Positions 264-797.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini267 – 476210Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini485 – 56682DisintegrinAdd
    BLAST
    Domaini567 – 62256TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini875 – 92955TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni732 – 874143SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi207 – 2148Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi41 – 466Poly-Ala
    Compositional biasi257 – 2615Poly-Arg
    Compositional biasi624 – 731108Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.
    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 2 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG302522.
    GeneTreeiENSGT00650000092972.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiB2RRX9.
    KOiK08620.
    OMAiRASCETP.
    OrthoDBiEOG7WDN1M.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013276. Pept_M12B_ADAM-TS5.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 2 hits.
    [Graphical view]
    PRINTSiPR01860. ADAMTS5.
    PR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 2 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 2 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9R001-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLEWAPLLL LLLLLSASCL SLAADSPAAA PAQDKTRQPQ AAAAAAEPDQ    50
    PQGEETRERG HLQPLAGQRR SGGLVQNIDQ LYSGGGKVGY LVYAGGRRFL 100
    LDLERDDTVG AAGSIVTAGG GLSASSGHRG HCFYRGTVDG SPRSLAVFDL 150
    CGGLDGFFAV KHARYTLKPL LRGSWAEYER IYGDGSSRIL HVYNREGFSF 200
    EALPPRASCE TPASPSGPQE SPSVHSRSRR RSALAPQLLD HSAFSPSGNA 250
    GPQTWWRRRR RSISRARQVE LLLVADSSMA RMYGRGLQHY LLTLASIANR 300
    LYSHASIENH IRLAVVKVVV LTDKDTSLEV SKNAATTLKN FCKWQHQHNQ 350
    LGDDHEEHYD AAILFTREDL CGHHSCDTLG MADVGTICSP ERSCAVIEDD 400
    GLHAAFTVAH EIGHLLGLSH DDSKFCEENF GTTEDKRLMS SILTSIDASK 450
    PWSKCTSATI TEFLDDGHGN CLLDLPRKQI LGPEELPGQT YDATQQCNLT 500
    FGPEYSVCPG MDVCARLWCA VVRQGQMVCL TKKLPAVEGT PCGKGRVCLQ 550
    GKCVDKTKKK YYSTSSHGNW GSWGPWGQCS RSCGGGVQFA YRHCNNPAPR 600
    NSGRYCTGKR AIYRSCSVTP CPPNGKSFRH EQCEAKNGYQ SDAKGVKTFV 650
    EWVPKYAGVL PADVCKLTCR AKGTGYYVVF SPKVTDGTEC RPYSNSVCVR 700
    GRCVRTGCDG IIGSKLQYDK CGVCGGDNSS CTKIIGTFNK KSKGYTDVVR 750
    IPEGATHIKV RQFKAKDQTR FTAYLALKKK TGEYLINGKY MISTSETIID 800
    INGTVMNYSG WSHRDDFLHG MGYSATKEIL IVQILATDPT KALDVRYSFF 850
    VPKKTTQKVN SVISHGSNKV GPHSTQLQWV TGPWLACSRT CDTGWHTRTV 900
    QCQDGNRKLA KGCLLSQRPS AFKQCLLKKC 930
    Length:930
    Mass (Da):101,844
    Last modified:July 27, 2011 - v2
    Checksum:i0CF1B264C782FF49
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71P → S in AAD56356. (PubMed:10464288)Curated
    Sequence conflicti76 – 761Q → H in AAD56356. (PubMed:10464288)Curated
    Sequence conflicti772 – 7721T → P in AAD56356. (PubMed:10464288)Curated
    Sequence conflicti844 – 8441D → G in AAD56356. (PubMed:10464288)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140673 mRNA. Translation: AAD56356.1.
    BC138619 mRNA. Translation: AAI38620.1.
    BC138620 mRNA. Translation: AAI38621.1.
    CCDSiCCDS28288.1.
    RefSeqiNP_035912.2. NM_011782.2.
    UniGeneiMm.112933.
    Mm.437478.

    Genome annotation databases

    EnsembliENSMUST00000023611; ENSMUSP00000023611; ENSMUSG00000022894.
    GeneIDi23794.
    KEGGimmu:23794.
    UCSCiuc007ztw.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF140673 mRNA. Translation: AAD56356.1 .
    BC138619 mRNA. Translation: AAI38620.1 .
    BC138620 mRNA. Translation: AAI38621.1 .
    CCDSi CCDS28288.1.
    RefSeqi NP_035912.2. NM_011782.2.
    UniGenei Mm.112933.
    Mm.437478.

    3D structure databases

    ProteinModelPortali Q9R001.
    SMRi Q9R001. Positions 264-797.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000023611.

    Protein family/group databases

    MEROPSi M12.225.

    PTM databases

    PhosphoSitei Q9R001.

    Proteomic databases

    PRIDEi Q9R001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023611 ; ENSMUSP00000023611 ; ENSMUSG00000022894 .
    GeneIDi 23794.
    KEGGi mmu:23794.
    UCSCi uc007ztw.1. mouse.

    Organism-specific databases

    CTDi 11096.
    MGIi MGI:1346321. Adamts5.

    Phylogenomic databases

    eggNOGi NOG302522.
    GeneTreei ENSGT00650000092972.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi B2RRX9.
    KOi K08620.
    OMAi RASCETP.
    OrthoDBi EOG7WDN1M.
    TreeFami TF331949.

    Enzyme and pathway databases

    Reactomei REACT_199052. Degradation of the extracellular matrix.
    REACT_211817. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    NextBioi 303403.
    PROi Q9R001.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9R001.
    Bgeei Q9R001.
    Genevestigatori Q9R001.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013276. Pept_M12B_ADAM-TS5.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR002870. Peptidase_M12B_N.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 2 hits.
    [Graphical view ]
    PRINTSi PR01860. ADAMTS5.
    PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 2 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 2 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 2 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."
      Hurskainen T.L., Hirohata S., Seldin M.F., Apte S.S.
      J. Biol. Chem. 274:25555-25563(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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].
      Tissue: Brain.

    Entry informationi

    Entry nameiATS5_MOUSE
    AccessioniPrimary (citable) accession number: Q9R001
    Secondary accession number(s): B2RRX9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 127 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, Reference proteome

    Documents

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

    External Data

    Dasty 3