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P97857

- ATS1_MOUSE

UniProt

P97857 - ATS1_MOUSE

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 1

Gene

Adamts1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 4 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. Has angiogenic inhibitor activity By similarity. Active metalloprotease, which may be associated with various inflammatory processes as well as development of cancer cachexia. May play a critical role in follicular rupture By similarity.By similarity

    Catalytic activityi

    Cleaves aggrecan at the 1691-Glu-|-Leu-1692 site, within the chondroitin sulfate attachment domain.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi206 – 2061Zinc; in inhibited formBy similarity
    Metal bindingi262 – 2621Calcium 1By similarity
    Metal bindingi262 – 2621Calcium 2By similarity
    Metal bindingi345 – 3451Calcium 1By similarity
    Metal bindingi345 – 3451Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi352 – 3521Calcium 1By similarity
    Metal bindingi402 – 4021Zinc; catalyticBy similarity
    Active sitei403 – 4031
    Metal bindingi406 – 4061Zinc; catalyticBy similarity
    Metal bindingi412 – 4121Zinc; catalyticBy similarity
    Metal bindingi463 – 4631Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi466 – 4661Calcium 1By similarity
    Metal bindingi466 – 4661Calcium 2By similarity

    GO - Molecular functioni

    1. heparin binding Source: MGI
    2. metalloendopeptidase activity Source: MGI
    3. protein binding Source: MGI
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. heart trabecula formation Source: MGI
    2. kidney development Source: MGI
    3. negative regulation of angiogenesis Source: MGI
    4. ovulation from ovarian follicle Source: MGI

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Heparin-binding, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM12.222.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 1 (EC:3.4.24.-)
    Short name:
    ADAM-TS 1
    Short name:
    ADAM-TS1
    Short name:
    ADAMTS-1
    Gene namesi
    Name:Adamts1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 16

    Organism-specific databases

    MGIiMGI:109249. Adamts1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: MGI
    2. cytoplasmic vesicle Source: MGI
    3. extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi403 – 4031E → Q: Loss of activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4848Sequence AnalysisAdd
    BLAST
    Propeptidei49 – 253205PRO_0000029152Add
    BLAST
    Chaini254 – 968715A disintegrin and metalloproteinase with thrombospondin motifs 1PRO_0000029153Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi334 ↔ 386By similarity
    Disulfide bondi363 ↔ 368By similarity
    Disulfide bondi380 ↔ 463By similarity
    Disulfide bondi418 ↔ 447By similarity
    Disulfide bondi489 ↔ 512By similarity
    Disulfide bondi500 ↔ 522By similarity
    Disulfide bondi507 ↔ 541By similarity
    Disulfide bondi535 ↔ 546By similarity
    Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi572 ↔ 609By similarity
    Disulfide bondi576 ↔ 614By similarity
    Disulfide bondi587 ↔ 599By similarity
    Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi783 – 7831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi946 – 9461N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.
    Glycosylated. Can be 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 mediates the efficient secretion of ADAMTS family members. Also 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

    PaxDbiP97857.
    PRIDEiP97857.

    PTM databases

    PhosphoSiteiP97857.

    Expressioni

    Inductioni

    Induced in vitro in colon adenocarcinoma cells by interleukin-1, or in vivo in kidney and heart by lipopolysaccharide. Also induced by LH stimulation in granulosa cells of preovulatory follicles.1 Publication

    Gene expression databases

    ArrayExpressiP97857.
    BgeeiP97857.
    GenevestigatoriP97857.

    Interactioni

    Protein-protein interaction databases

    BioGridi197974. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliP97857.
    SMRiP97857. Positions 257-845.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini259 – 468210Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini477 – 55983DisintegrinAdd
    BLAST
    Domaini560 – 61556TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini855 – 91157TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini912 – 96857TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni726 – 850125SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi204 – 2118Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi195 – 1995Poly-Arg
    Compositional biasi618 – 725108Cys-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 3 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG291688.
    GeneTreeiENSGT00650000092972.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiP97857.
    KOiK08617.
    OMAiCPDNNGK.
    OrthoDBiEOG7WDN1M.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR006586. ADAM_Cys-rich.
    IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013274. Pept_M12B_ADAM-TS1.
    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. 3 hits.
    [Graphical view]
    PRINTSiPR01858. ADAMTS1.
    PR01857. ADAMTSFAMILY.
    SMARTiSM00608. ACR. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 3 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 3 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P97857-1 [UniParc]FASTAAdd to Basket

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    MQPKVPLGSR KQKPCSDMGD VQRAARSRGS LSAHMLLLLL ASITMLLCAR    50
    GAHGRPTEED EELVLPSLER APGHDSTTTR LRLDAFGQQL HLKLQPDSGF 100
    LAPGFTLQTV GRSPGSEAQH LDPTGDLAHC FYSGTVNGDP GSAAALSLCE 150
    GVRGAFYLQG EEFFIQPAPG VATERLAPAV PEEESSARPQ FHILRRRRRG 200
    SGGAKCGVMD DETLPTSDSR PESQNTRNQW PVRDPTPQDA GKPSGPGSIR 250
    KKRFVSSPRY VETMLVADQS MADFHGSGLK HYLLTLFSVA ARFYKHPSIR 300
    NSISLVVVKI LVIYEEQKGP EVTSNAALTL RNFCSWQKQH NSPSDRDPEH 350
    YDTAILFTRQ DLCGSHTCDT LGMADVGTVC DPSRSCSVIE DDGLQAAFTT 400
    AHELGHVFNM PHDDAKHCAS LNGVSGDSHL MASMLSSLDH SQPWSPCSAY 450
    MVTSFLDNGH GECLMDKPQN PIKLPSDLPG TLYDANRQCQ FTFGEESKHC 500
    PDAASTCTTL WCTGTSGGLL VCQTKHFPWA DGTSCGEGKW CVSGKCVNKT 550
    DMKHFATPVH GSWGPWGPWG DCSRTCGGGV QYTMRECDNP VPKNGGKYCE 600
    GKRVRYRSCN IEDCPDNNGK TFREEQCEAH NEFSKASFGN EPTVEWTPKY 650
    AGVSPKDRCK LTCEAKGIGY FFVLQPKVVD GTPCSPDSTS VCVQGQCVKA 700
    GCDRIIDSKK KFDKCGVCGG NGSTCKKMSG IVTSTRPGYH DIVTIPAGAT 750
    NIEVKHRNQR GSRNNGSFLA IRAADGTYIL NGNFTLSTLE QDLTYKGTVL 800
    RYSGSSAALE RIRSFSPLKE PLTIQVLMVG HALRPKIKFT YFMKKKTESF 850
    NAIPTFSEWV IEEWGECSKT CGSGWQRRVV QCRDINGHPA SECAKEVKPA 900
    STRPCADLPC PHWQVGDWSP CSKTCGKGYK KRTLKCVSHD GGVLSNESCD 950
    PLKKPKHYID FCTLTQCS 968
    Length:968
    Mass (Da):105,801
    Last modified:July 27, 2011 - v4
    Checksum:i90A44F7D5262B6C5
    GO

    Sequence cautioni

    The sequence BAA11088.1 differs from that shown. Reason: Frameshift at position 7.
    The sequence BAA24501.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti335 – 3351S → N in BAA24501. (PubMed:9441751)Curated
    Sequence conflicti335 – 3351S → N in AAH40382. (PubMed:15489334)Curated
    Sequence conflicti335 – 3351S → N in AAH50834. (PubMed:15489334)Curated
    Sequence conflicti425 – 4251S → T in BAA24501. (PubMed:9441751)Curated
    Sequence conflicti425 – 4251S → T in AAH40382. (PubMed:15489334)Curated
    Sequence conflicti425 – 4251S → T in AAH50834. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001735 Genomic DNA. Translation: BAA24501.1. Different initiation.
    D67076 mRNA. Translation: BAA11088.1. Frameshift.
    AC126936 Genomic DNA. No translation available.
    BC040382 mRNA. Translation: AAH40382.1.
    BC050834 mRNA. Translation: AAH50834.1.
    CCDSiCCDS28287.1.
    PIRiT00017.
    RefSeqiNP_033751.3. NM_009621.4.
    UniGeneiMm.1421.

    Genome annotation databases

    EnsembliENSMUST00000023610; ENSMUSP00000023610; ENSMUSG00000022893.
    GeneIDi11504.
    KEGGimmu:11504.
    UCSCiuc012aho.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB001735 Genomic DNA. Translation: BAA24501.1 . Different initiation.
    D67076 mRNA. Translation: BAA11088.1 . Frameshift.
    AC126936 Genomic DNA. No translation available.
    BC040382 mRNA. Translation: AAH40382.1 .
    BC050834 mRNA. Translation: AAH50834.1 .
    CCDSi CCDS28287.1.
    PIRi T00017.
    RefSeqi NP_033751.3. NM_009621.4.
    UniGenei Mm.1421.

    3D structure databases

    ProteinModelPortali P97857.
    SMRi P97857. Positions 257-845.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197974. 1 interaction.

    Protein family/group databases

    MEROPSi M12.222.

    PTM databases

    PhosphoSitei P97857.

    Proteomic databases

    PaxDbi P97857.
    PRIDEi P97857.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000023610 ; ENSMUSP00000023610 ; ENSMUSG00000022893 .
    GeneIDi 11504.
    KEGGi mmu:11504.
    UCSCi uc012aho.1. mouse.

    Organism-specific databases

    CTDi 9510.
    MGIi MGI:109249. Adamts1.

    Phylogenomic databases

    eggNOGi NOG291688.
    GeneTreei ENSGT00650000092972.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi P97857.
    KOi K08617.
    OMAi CPDNNGK.
    OrthoDBi EOG7WDN1M.
    TreeFami TF331949.

    Miscellaneous databases

    NextBioi 278910.
    PROi P97857.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97857.
    Bgeei P97857.
    Genevestigatori P97857.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR006586. ADAM_Cys-rich.
    IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013274. Pept_M12B_ADAM-TS1.
    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. 3 hits.
    [Graphical view ]
    PRINTSi PR01858. ADAMTS1.
    PR01857. ADAMTSFAMILY.
    SMARTi SM00608. ACR. 1 hit.
    SM00209. TSP1. 3 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 3 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 3 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1 gene encoding an ADAM family protein with TSP motifs."
      Kuno K., Lizasa H., Ohno S., Matsushima K.
      Genomics 46:466-471(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    2. "Molecular cloning of a gene encoding a new type of metalloproteinase-disintegrin family protein with thrombospondin motifs as an inflammation associated gene."
      Kuno K., Kanada N., Nakashima E., Fujiki F., Ichimura F., Matsushima K.
      J. Biol. Chem. 272:556-562(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "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: Limb and Mammary gland.
    5. "ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix."
      Kuno K., Terashima Y., Matsushima K.
      J. Biol. Chem. 274:18821-18826(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF GLU-403.
    6. Cited for: FUNCTION.
    7. "Progesterone-regulated genes in the ovulation process: ADAMTS-1 and cathepsin L proteases."
      Robker R.L., Russell D.L., Espey L.L., Lydon J.P., O'Malley B.W., Richards J.S.
      Proc. Natl. Acad. Sci. U.S.A. 97:4689-4694(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiATS1_MOUSE
    AccessioniPrimary (citable) accession number: P97857
    Secondary accession number(s): E9QMN9, O54768
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 138 of the entry and version 4 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