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Q5RFQ8

- ATS4_PONAB

UniProt

Q5RFQ8 - ATS4_PONAB

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 4

Gene

ADAMTS4

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      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. 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 formBy similarity
    Metal bindingi361 – 3611Zinc; catalyticBy similarity
    Active sitei362 – 3621PROSITE-ProRule annotation
    Metal bindingi365 – 3651Zinc; catalyticBy similarity
    Metal bindingi371 – 3711Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: InterPro
    2. zinc ion binding Source: InterPro

    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):
    Aggrecanase-1
    Gene namesi
    Name:ADAMTS4
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5151Sequence AnalysisAdd
    BLAST
    Propeptidei52 – 212161By similarityPRO_0000239803Add
    BLAST
    Chaini213 – 837625A disintegrin and metalloproteinase with thrombospondin motifs 4PRO_0000239804Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

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

    Interactioni

    Subunit structurei

    Interacts with SRPX2.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5RFQ8.
    SMRiQ5RFQ8. Positions 215-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini218 – 428211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini437 – 51983DisintegrinAdd
    BLAST
    Domaini520 – 57556TSP type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni686 – 837152SpacerBy similarityAdd
    BLAST

    Motif

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

    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 1 TSP type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG004313.
    InParanoidiQ5RFQ8.

    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.

    Q5RFQ8-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQTGSHPGR GLAGRWLWGA QPCLLLPIVP LSWLVWLLLL LLASLLPSAR    50
    LASPLPREEE IVFPEKLNGS VLPGSGAPAR LLCRLQAFGE TLLLELEHDS 100
    GVQVEGLTVQ YLGQAPELLG GAEPGTYLTG TINGEPESVA SLHWDGGALL 150
    GVLQYRGAEL HLQPLEGGTP NSAGGPGAHI LRRKSPASGQ GPMCNVKAPL 200
    GSPSPRPRRA KRFASLSRFV ETLVVADDKM AAFHGAGLKR YLLTVMAAAA 250
    KAFKHPSIRN PVSLVVTRLV ILGSGEEGPQ VGPSAAQTLR SFCAWQRGLN 300
    TPEDSDPDHF DTAILFTRQD LCGVSTCDTL GMADVGTVCD PARSCAIVED 350
    DGLQSAYTAA HELGHVFNML HDNSKPCISL NGPLSTSRHV MAPVMAHVDP 400
    EEPWSPCSAR FITDFLDNGY GHCLLDKPEA PLHLPVTFPG KDYDADRQCQ 450
    LTFGPDSRHC PQLPPPCAAL WCSGHLNGHA MCQTKHSPWA DGTPCGPAQA 500
    CMGGRCLHMD QLQDFNIPQA GGWGPWGPWG DCSRTCGGGV QFSSRDCTRP 550
    VPRNGGKYCE GRRTRFRSCN TEDCPTGSVL TFREEQCAAY NHCTDLFKSF 600
    PGPMDWVPRY TGVAPQDQCK LTCQARALGY YYVLEPRVVD GTPCSPDSSS 650
    VCVQGRCIHA GCDRIIGSKK KFDKCMVCGG DGSGCSKQSG SFRKFRYGYN 700
    NVVTIPTGAT HILVRQQGNP GHRSIYLALK LPDGSYALNG EYTLMPSPTD 750
    VVLPGAISLR YSGATAASET LSGHGPLAQP LTLQVLVAGN PQDARLRYSF 800
    FVPRPTPSTP HPTPQDWLHR RAQILEILRR RPWVGRK 837
    Length:837
    Mass (Da):90,262
    Last modified:December 21, 2004 - v1
    Checksum:i08F5E69F65CF6B4C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857094 mRNA. Translation: CAH89399.1.
    UniGeneiPab.12192.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR857094 mRNA. Translation: CAH89399.1 .
    UniGenei Pab.12192.

    3D structure databases

    ProteinModelPortali Q5RFQ8.
    SMRi Q5RFQ8. Positions 215-507.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M12.221.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG004313.
    InParanoidi Q5RFQ8.

    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

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiATS4_PONAB
    AccessioniPrimary (citable) accession number: Q5RFQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 55 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. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3