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Q9TT93

- ATS4_BOVIN

UniProt

Q9TT93 - ATS4_BOVIN

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Protein
A disintegrin and metalloproteinase with thrombospondin motifs 4
Gene
ADAMTS4
Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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

Catalytic activityi

Glutamyl endopeptidase; bonds cleaved include 370-Thr-Glu-Gly-Glu-|-Ala-Arg-Gly-Ser-377 in the interglobular domain of mammalian aggrecan.

Cofactori

Binds 1 zinc ion per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi194 – 1941Zinc; in inhibited form By similarity
Metal bindingi361 – 3611Zinc; catalytic By similarity
Active sitei362 – 3621 By similarity
Metal bindingi365 – 3651Zinc; catalytic By similarity
Metal bindingi371 – 3711Zinc; catalytic By similarity

GO - Molecular functioni

  1. metalloendopeptidase activity Source: InterPro
  2. metallopeptidase activity Source: AgBase
  3. zinc ion binding Source: InterPro
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM12.221.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 4 (EC:3.4.24.82)
    Short name:
    ADAM-TS 4
    Short name:
    ADAM-TS4
    Short name:
    ADAMTS-4
    Alternative name(s):
    ADMP-1
    Aggrecanase-1
    Gene namesi
    Name:ADAMTS4
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell
    Complete GO annotation...

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5151 Reviewed prediction
    Add
    BLAST
    Propeptidei52 – 212161
    PRO_0000239802Add
    BLAST
    Chaini213 – 839627A disintegrin and metalloproteinase with thrombospondin motifs 4
    PRO_0000078209Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi68 – 681N-linked (GlcNAc...) Reviewed prediction
    Disulfide bondi293 ↔ 345 By similarity
    Disulfide bondi322 ↔ 327 By similarity
    Disulfide bondi339 ↔ 423 By similarity
    Disulfide bondi377 ↔ 407 By similarity
    Disulfide bondi449 ↔ 472 By similarity
    Disulfide bondi460 ↔ 482 By similarity
    Disulfide bondi467 ↔ 501 By similarity
    Disulfide bondi495 ↔ 506 By similarity
    Disulfide bondi532 ↔ 569 By similarity
    Disulfide bondi536 ↔ 574 By similarity
    Disulfide bondi547 ↔ 559 By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase By similarity.
    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.

    Keywords - PTMi

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

    Proteomic databases

    PRIDEiQ9TT93.

    Expressioni

    Inductioni

    By interleukin-1.

    Interactioni

    Subunit structurei

    Interacts with SRPX2 By similarity.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9TT93.
    SMRiQ9TT93. Positions 215-507.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini218 – 428211Peptidase M12B
    Add
    BLAST
    Domaini437 – 51983Disintegrin
    Add
    BLAST
    Domaini520 – 57556TSP type-1
    Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni686 – 839154Spacer By similarity
    Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi192 – 1998Cysteine switch By similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi247 – 2526Poly-Ala
    Compositional biasi577 – 685109Cys-rich
    Add
    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.
    Contains 1 TSP type-1 domain.

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG271890.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    KOiK07764.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    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. 1 hit.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 1 hit.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 1 hit.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9TT93-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSHMDSHPGR GLADGWLWGI QPRLLLPTVP VSGSRLVWLL LLASLLPSAW    50
    PASPLPREEE IVFPEKLNGS VLPGLGAPAR LLYRLPAFGE TLLLELEKDP 100
    GVQVEGLTVQ YLGRAPELLG GAEPGTYLTG TINGDPESVA SLHWDGGALL 150
    GVLQYRGTEL HIQPLEGGAP NSAGGPGAHI LRRKSPVSGQ GPMCNVKAPP 200
    GKPSPSPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA 250
    KAFKHPSIRN PVSLVVTRLV VLGPGEEGPQ VGPSAAQTLR SFCAWQRGLN 300
    TPDDADPGHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED 350
    DGLQSAFTAA HELGHVFSML HDNSKQCTGL NGPESTSRHV MAPVMAHVDP 400
    EEPWSPCSAR FITDFLDNGF GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ 450
    LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA 500
    CMGGRCLHVD QLQAFNVPQA GGWGPWGSWG DCSRSCGGGV QFSSRDCTRP 550
    VPRNGGKYCE GRRTRFRSCN TQDCPTGSAL TFREEQCAAY NHRTDLFKNF 600
    PGPMDWVPRY TGVAPRDQCK LTCQTRALGY YYVLDPRVAD GTPCSPDSSS 650
    VCVQGRCIHA GCDRVIGSKK KFDKCMVCGG DGSSCSKQSG SFKKFRYGYN 700
    NVVTIPAGAT HILVRQQGSP SVRSLYLALK LPDGSYALNG EYTLIPSPTD 750
    VVLPGAVSLR YSGATAASET LSGHGPLAEP LTLQVLVAGN PQNARLRYSF 800
    FVPRPRPVPS TPRPTPQDWL RRKSQILEIL RRRSWAGRK 839
    Length:839
    Mass (Da):90,280
    Last modified:June 13, 2006 - v3
    Checksum:i1B488A27DF5B96B1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF516915 mRNA. Translation: AAP47196.1.
    BC148059 mRNA. Translation: AAI48060.1.
    AF192770 mRNA. Translation: AAF07176.1.
    RefSeqiNP_858053.1. NM_181667.1.
    UniGeneiBt.15675.

    Genome annotation databases

    GeneIDi286806.
    KEGGibta:286806.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF516915 mRNA. Translation: AAP47196.1 .
    BC148059 mRNA. Translation: AAI48060.1 .
    AF192770 mRNA. Translation: AAF07176.1 .
    RefSeqi NP_858053.1. NM_181667.1.
    UniGenei Bt.15675.

    3D structure databases

    ProteinModelPortali Q9TT93.
    SMRi Q9TT93. Positions 215-507.
    ModBasei Search...

    Chemistry

    BindingDBi Q9TT93.
    ChEMBLi CHEMBL3874.

    Protein family/group databases

    MEROPSi M12.221.

    Proteomic databases

    PRIDEi Q9TT93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 286806.
    KEGGi bta:286806.

    Organism-specific databases

    CTDi 9507.

    Phylogenomic databases

    eggNOGi NOG271890.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    KOi K07764.

    Miscellaneous databases

    NextBioi 20806460.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    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. 1 hit.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 1 hit.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and characterization of bovine aggrecanase-1."
      Arai M., Anderson D., Annis B., Collins-Racie L., Corcoran C., DiBlasio-Smith E., Morris E., Dorner A., LaVallie E.
      Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Thalamus.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-531.
      Tissue: Cartilage.
    4. "n-3 fatty acids specifically modulate catabolic factors involved in articular cartilage degradation."
      Curtis C.L., Hughes C.E., Flannery C.R., Little C.B., Harwood J.L., Caterson B.
      J. Biol. Chem. 275:721-724(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 332-531.
      Tissue: Cartilage chondrocyte.
    5. Cited for: PROTEIN SEQUENCE OF 213-239; 610-615 AND 626-637.
      Tissue: Cartilage.

    Entry informationi

    Entry nameiATS4_BOVIN
    AccessioniPrimary (citable) accession number: Q9TT93
    Secondary accession number(s): A6QLR5, Q7YS95
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: June 13, 2006
    Last modified: May 14, 2014
    This is version 104 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Has sometimes been referred to as ADAMTS2.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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