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Q9UP79

- ATS8_HUMAN

UniProt

Q9UP79 - ATS8_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 8

Gene

ADAMTS8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Has anti-angiogenic properties.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi363 – 3631Zinc; catalyticBy similarity
    Active sitei364 – 3641PROSITE-ProRule annotation
    Metal bindingi367 – 3671Zinc; catalyticBy similarity
    Metal bindingi373 – 3731Zinc; catalyticBy similarity

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW
    2. integrin binding Source: ProtInc
    3. low-affinity phosphate transmembrane transporter activity Source: ProtInc
    4. metalloendopeptidase activity Source: InterPro
    5. metallopeptidase activity Source: ProtInc
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of cell proliferation Source: ProtInc
    2. phosphate ion transmembrane transport Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Heparin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Protein family/group databases

    MEROPSiM12.226.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 8 (EC:3.4.24.-)
    Short name:
    ADAM-TS 8
    Short name:
    ADAM-TS8
    Short name:
    ADAMTS-8
    Alternative name(s):
    METH-2
    METH-8
    Gene namesi
    Name:ADAMTS8
    Synonyms:METH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:224. ADAMTS8.

    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 – 2626Sequence AnalysisAdd
    BLAST
    Propeptidei27 – 213187By similarityPRO_0000029178Add
    BLAST
    Chaini214 – 889676A disintegrin and metalloproteinase with thrombospondin motifs 8PRO_0000029179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi294 ↔ 347By similarity
    Disulfide bondi323 ↔ 329By similarity
    Disulfide bondi341 ↔ 424By similarity
    Glycosylationi344 – 3441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi379 ↔ 408By similarity
    Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi452 ↔ 477By similarity
    Disulfide bondi463 ↔ 486By similarity
    Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi472 ↔ 507By similarity
    Glycosylationi490 – 4901N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi501 ↔ 512By similarity
    Disulfide bondi538 ↔ 575By similarity
    Disulfide bondi542 ↔ 580By similarity
    Disulfide bondi553 ↔ 565By similarity
    Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis

    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

    Proteomic databases

    PaxDbiQ9UP79.
    PRIDEiQ9UP79.

    PTM databases

    PhosphoSiteiQ9UP79.

    Expressioni

    Tissue specificityi

    Highly expressed in adult and fetal lung, lower expression in brain, placenta, heart, stomach and fetal brain and kidney.

    Gene expression databases

    BgeeiQ9UP79.
    CleanExiHS_ADAMTS8.
    GenevestigatoriQ9UP79.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000257359.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UP79.
    SMRiQ9UP79. Positions 219-809.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini219 – 429211Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 52588DisintegrinAdd
    BLAST
    Domaini526 – 58156TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini833 – 88856TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni690 – 831142SpacerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi201 – 2044Poly-Pro
    Compositional biasi583 – 689107Cys-richAdd
    BLAST

    Domaini

    The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix.

    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

    eggNOGiNOG285519.
    HOGENOMiHOG000004799.
    HOVERGENiHBG004313.
    InParanoidiQ9UP79.
    KOiK08623.
    OMAiYELDQQC.
    OrthoDBiEOG7WDN1M.
    PhylomeDBiQ9UP79.
    TreeFamiTF331949.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013277. Pept_M12B_ADAM-TS8.
    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]
    PRINTSiPR01861. ADAMTS8.
    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.

    Q9UP79-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPAPAAPRW PPLLLLLLLL LPLARGAPAR PAAGGQASEL VVPTRLPGSA    50
    GELALHLSAF GKGFVLRLAP DDSFLAPEFK IERLGGSGRA TGGERGLRGC 100
    FFSGTVNGEP ESLAAVSLCR GLSGSFLLDG EEFTIQPQGA GGSLAQPHRL 150
    QRWGPAGARP LPRGPEWEVE TGEGQRQERG DHQEDSEEES QEEEAEGASE 200
    PPPPLGATSR TKRFVSEARF VETLLVADAS MAAFYGADLQ NHILTLMSVA 250
    ARIYKHPSIK NSINLMVVKV LIVEDEKWGP EVSDNGGLTL RNFCNWQRRF 300
    NQPSDRHPEH YDTAILLTRQ NFCGQEGLCD TLGVADIGTI CDPNKSCSVI 350
    EDEGLQAAHT LAHELGHVLS MPHDDSKPCT RLFGPMGKHH VMAPLFVHLN 400
    QTLPWSPCSA MYLTELLDGG HGDCLLDAPA AALPLPTGLP GRMALYQLDQ 450
    QCRQIFGPDF RHCPNTSAQD VCAQLWCHTD GAEPLCHTKN GSLPWADGTP 500
    CGPGHLCSEG SCLPEEEVER PKPVADGGWA PWGPWGECSR TCGGGVQFSH 550
    RECKDPEPQN GGRYCLGRRA KYQSCHTEEC PPDGKSFREQ QCEKYNAYNY 600
    TDMDGNLLQW VPKYAGVSPR DRCKLFCRAR GRSEFKVFEA KVIDGTLCGP 650
    ETLAICVRGQ CVKAGCDHVV DSPRKLDKCG VCGGKGNSCR KVSGSLTPTN 700
    YGYNDIVTIP AGATNIDVKQ RSHPGVQNDG NYLALKTADG QYLLNGNLAI 750
    SAIEQDILVK GTILKYSGSI ATLERLQSFR PLPEPLTVQL LTVPGEVFPP 800
    KVKYTFFVPN DVDFSMQSSK ERATTNIIQP LLHAQWVLGD WSECSSTCGA 850
    GWQRRTVECR DPSGQASATC NKALKPEDAK PCESQLCPL 889
    Length:889
    Mass (Da):96,460
    Last modified:November 30, 2010 - v2
    Checksum:iE1767A6524BCEBAB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21L → F in AAD48081. (PubMed:10438512)Curated
    Sequence conflicti11 – 122PP → LPF in AAD48081. (PubMed:10438512)Curated
    Sequence conflicti194 – 1941E → R in AAF25806. (PubMed:10610729)Curated
    Sequence conflicti412 – 43928YLTEL…LPTGL → FSGCHLQGWIHFKYLCKCVS ELKCDLMP in AAF25806. (PubMed:10610729)CuratedAdd
    BLAST
    Sequence conflicti430 – 4301A → G in AAD48081. (PubMed:10438512)Curated
    Sequence conflicti525 – 5251A → V in AAD48081. (PubMed:10438512)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060153 mRNA. Translation: AAD48081.1.
    AP002986 Genomic DNA. No translation available.
    AF175283 mRNA. Translation: AAF25806.1.
    CCDSiCCDS41732.1.
    RefSeqiNP_008968.4. NM_007037.4.
    XP_006718821.1. XM_006718758.1.
    UniGeneiHs.271605.

    Genome annotation databases

    EnsembliENST00000257359; ENSP00000257359; ENSG00000134917.
    GeneIDi11095.
    KEGGihsa:11095.
    UCSCiuc001qgg.4. human.

    Polymorphism databases

    DMDMi313104077.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF060153 mRNA. Translation: AAD48081.1 .
    AP002986 Genomic DNA. No translation available.
    AF175283 mRNA. Translation: AAF25806.1 .
    CCDSi CCDS41732.1.
    RefSeqi NP_008968.4. NM_007037.4.
    XP_006718821.1. XM_006718758.1.
    UniGenei Hs.271605.

    3D structure databases

    ProteinModelPortali Q9UP79.
    SMRi Q9UP79. Positions 219-809.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000257359.

    Protein family/group databases

    MEROPSi M12.226.

    PTM databases

    PhosphoSitei Q9UP79.

    Polymorphism databases

    DMDMi 313104077.

    Proteomic databases

    PaxDbi Q9UP79.
    PRIDEi Q9UP79.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257359 ; ENSP00000257359 ; ENSG00000134917 .
    GeneIDi 11095.
    KEGGi hsa:11095.
    UCSCi uc001qgg.4. human.

    Organism-specific databases

    CTDi 11095.
    GeneCardsi GC11M130308.
    H-InvDB HIX0026131.
    HGNCi HGNC:224. ADAMTS8.
    MIMi 605175. gene.
    neXtProti NX_Q9UP79.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285519.
    HOGENOMi HOG000004799.
    HOVERGENi HBG004313.
    InParanoidi Q9UP79.
    KOi K08623.
    OMAi YELDQQC.
    OrthoDBi EOG7WDN1M.
    PhylomeDBi Q9UP79.
    TreeFami TF331949.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.
    REACT_201925. Degradation of the extracellular matrix.

    Miscellaneous databases

    GeneWikii ADAMTS8.
    GenomeRNAii 11095.
    NextBioi 42178.
    PROi Q9UP79.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9UP79.
    CleanExi HS_ADAMTS8.
    Genevestigatori Q9UP79.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR010294. ADAM_spacer1.
    IPR024079. MetalloPept_cat_dom.
    IPR013277. Pept_M12B_ADAM-TS8.
    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 PR01861. ADAMTS8.
    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. "METH-1, a human ortholog of ADAMTS-1, and METH-2 are members of a new family of proteins with angio-inhibitory activity."
      Vazquez F., Hastings G., Ortega M.-A., Lane T.F., Oikemus S., Lombardo M., Iruela-Arispe M.L.
      J. Biol. Chem. 274:23349-23357(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "ADAM-TS8, a novel metalloprotease of the ADAM-TS family located on mouse chromosome 9 and human chromosome 11."
      Georgiadis K.E., Hirohata S., Seldin M.F., Apte S.S.
      Genomics 62:312-315(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 194-439.

    Entry informationi

    Entry nameiATS8_HUMAN
    AccessioniPrimary (citable) accession number: Q9UP79
    Secondary accession number(s): Q9NZS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3