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O15072

- ATS3_HUMAN

UniProt

O15072 - ATS3_HUMAN

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 3

Gene

ADAMTS3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 4 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Cleaves the propeptides of type II collagen prior to fibril assembly. Does not act on types I and III collagens.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi398 – 3981Zinc; catalyticPROSITE-ProRule annotation
    Active sitei399 – 3991PROSITE-ProRule annotation
    Metal bindingi402 – 4021Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi408 – 4081Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. endopeptidase activity Source: BHF-UCL
    2. heparin binding Source: UniProtKB-KW
    3. metalloendopeptidase activity Source: UniProtKB
    4. protein binding Source: BHF-UCL
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. collagen biosynthetic process Source: BHF-UCL
    2. collagen catabolic process Source: UniProtKB
    3. collagen fibril organization Source: UniProtKB
    4. extracellular fibril organization Source: BHF-UCL
    5. extracellular matrix organization Source: Reactome
    6. positive regulation of vascular endothelial growth factor signaling pathway Source: BHF-UCL
    7. protein processing Source: BHF-UCL
    8. vascular endothelial growth factor production Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Heparin-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.220.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 3 (EC:3.4.24.-)
    Short name:
    ADAM-TS 3
    Short name:
    ADAM-TS3
    Short name:
    ADAMTS-3
    Alternative name(s):
    Procollagen II N-proteinase
    Short name:
    PC II-NP
    Procollagen II amino propeptide-processing enzyme
    Gene namesi
    Name:ADAMTS3
    Synonyms:KIAA0366
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:219. ADAMTS3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24547.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 249229By similarityPRO_0000029162Add
    BLAST
    Chaini250 – 1205956A disintegrin and metalloproteinase with thrombospondin motifs 3PRO_0000029163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi242 – 2421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi333 ↔ 382By similarity
    Glycosylationi345 – 3451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi376 ↔ 455By similarity
    Disulfide bondi415 ↔ 441By similarity
    Glycosylationi475 – 4751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi482 ↔ 507By similarity
    Disulfide bondi493 ↔ 516By similarity
    Disulfide bondi502 ↔ 535By similarity
    Disulfide bondi529 ↔ 540By similarity
    Disulfide bondi563 ↔ 600By similarity
    Disulfide bondi567 ↔ 605By similarity
    Disulfide bondi578 ↔ 590By similarity
    Glycosylationi814 – 8141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi978 ↔ 1010By similarity
    Disulfide bondi982 ↔ 1015By similarity
    Disulfide bondi993 ↔ 999By 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

    Proteomic databases

    PaxDbiO15072.
    PRIDEiO15072.

    PTM databases

    PhosphoSiteiO15072.

    Expressioni

    Tissue specificityi

    Found in cartilage and skin.

    Gene expression databases

    ArrayExpressiO15072.
    BgeeiO15072.
    CleanExiHS_ADAMTS3.
    GenevestigatoriO15072.

    Organism-specific databases

    HPAiHPA021368.
    HPA021369.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000286657.

    Structurei

    3D structure databases

    ProteinModelPortaliO15072.
    SMRiO15072. Positions 258-824.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini256 – 460205Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini470 – 55081DisintegrinAdd
    BLAST
    Domaini551 – 60656TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini845 – 90561TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini906 – 96560TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini966 – 101449TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini1015 – 105440PLACPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni713 – 844132SpacerAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi246 – 2494Poly-Arg
    Compositional biasi608 – 712105Cys-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 1 PLAC domain.PROSITE-ProRule annotation
    Contains 4 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG307411.
    HOGENOMiHOG000034222.
    HOVERGENiHBG004314.
    InParanoidiO15072.
    KOiK08619.
    OMAiAEEWEHC.
    OrthoDBiEOG76HQ0N.
    PhylomeDBiO15072.
    TreeFamiTF313537.

    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.
    IPR010909. PLAC.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF05986. ADAM_spacer1. 1 hit.
    PF01562. Pep_M12B_propep. 1 hit.
    PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 4 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 4 hits.
    [Graphical view]
    SUPFAMiSSF82895. SSF82895. 4 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    O15072-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLLSLWLIA AALVEVRTSA DGQAGNEEMV QIDLPIKRYR EYELVTPVST     50
    NLEGRYLSHT LSASHKKRSA RDVSSNPEQL FFNITAFGKD FHLRLKPNTQ 100
    LVAPGAVVEW HETSLVPGNI TDPINNHQPG SATYRIRRTE PLQTNCAYVG 150
    DIVDIPGTSV AISNCDGLAG MIKSDNEEYF IEPLERGKQM EEEKGRIHVV 200
    YKRSAVEQAP IDMSKDFHYR ESDLEGLDDL GTVYGNIHQQ LNETMRRRRH 250
    AGENDYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH 300
    INVVLVRMIM LGYAKSISLI ERGNPSRSLE NVCRWASQQQ RSDLNHSEHH 350
    DHAIFLTRQD FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET 400
    GHVLGMEHDG QGNRCGDETA MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI 450
    HSYDCLLDDP FDHDWPKLPE LPGINYSMDE QCRFDFGVGY KMCTAFRTFD 500
    PCKQLWCSHP DNPYFCKTKK GPPLDGTECA AGKWCYKGHC MWKNANQQKQ 550
    DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PMPINGGQDC PGVNFEYQLC 600
    NTEECQKHFE DFRAQQCQQR NSHFEYQNTK HHWLPYEHPD PKKRCHLYCQ 650
    SKETGDVAYM KQLVHDGTHC SYKDPYSICV RGECVKVGCD KEIGSNKVED 700
    KCGVCGGDNS HCRTVKGTFT RTPRKLGYLK MFDIPPGARH VLIQEDEASP 750
    HILAIKNQAT GHYILNGKGE EAKSRTFIDL GVEWDYNIED DIESLHTDGP 800
    LHDPVIVLII PQENDTRSSL TYKYIIHEDS VPTINSNNVI QEELDTFEWA 850
    LKSWSQCSKP CGGGFQYTKY GCRRKSDNKM VHRSFCEANK KPKPIRRMCN 900
    IQECTHPLWV AEEWEHCTKT CGSSGYQLRT VRCLQPLLDG TNRSVHSKYC 950
    MGDRPESRRP CNRVPCPAQW KTGPWSECSV TCGEGTEVRQ VLCRAGDHCD 1000
    GEKPESVRAC QLPPCNDEPC LGDKSIFCQM EVLARYCSIP GYNKLCCESC 1050
    SKRSSTLPPP YLLEAAETHD DVISNPSDLP RSLVMPTSLV PYHSETPAKK 1100
    MSLSSISSVG GPNAYAAFRP NSKPDGANLR QRSAQQAGSK TVRLVTVPSS 1150
    PPTKRVHLSS ASQMAAASFF AASDSIGASS QARTSKKDGK IIDNRRPTRS 1200
    STLER 1205
    Length:1,205
    Mass (Da):135,603
    Last modified:January 11, 2011 - v4
    Checksum:i01FA661B1C6BFF1B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti857 – 8571C → V in BAA20821. (PubMed:9205841)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti138 – 1381R → K.3 Publications
    Corresponds to variant rs788908 [ dbSNP | Ensembl ].
    VAR_055012
    Natural varianti1074 – 10741S → P.
    Corresponds to variant rs35864003 [ dbSNP | Ensembl ].
    VAR_055013

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC093790 Genomic DNA. No translation available.
    AC095056 Genomic DNA. No translation available.
    AC104814 Genomic DNA. No translation available.
    BC130287 mRNA. Translation: AAI30288.1.
    BC132735 mRNA. Translation: AAI32736.1.
    AF247668 mRNA. Translation: AAK28400.1.
    AB002364 mRNA. Translation: BAA20821.1.
    CCDSiCCDS3553.1.
    RefSeqiNP_055058.2. NM_014243.2.
    UniGeneiHs.590919.

    Genome annotation databases

    EnsembliENST00000286657; ENSP00000286657; ENSG00000156140.
    GeneIDi9508.
    KEGGihsa:9508.
    UCSCiuc003hgk.2. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC093790 Genomic DNA. No translation available.
    AC095056 Genomic DNA. No translation available.
    AC104814 Genomic DNA. No translation available.
    BC130287 mRNA. Translation: AAI30288.1 .
    BC132735 mRNA. Translation: AAI32736.1 .
    AF247668 mRNA. Translation: AAK28400.1 .
    AB002364 mRNA. Translation: BAA20821.1 .
    CCDSi CCDS3553.1.
    RefSeqi NP_055058.2. NM_014243.2.
    UniGenei Hs.590919.

    3D structure databases

    ProteinModelPortali O15072.
    SMRi O15072. Positions 258-824.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000286657.

    Protein family/group databases

    MEROPSi M12.220.

    PTM databases

    PhosphoSitei O15072.

    Proteomic databases

    PaxDbi O15072.
    PRIDEi O15072.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286657 ; ENSP00000286657 ; ENSG00000156140 .
    GeneIDi 9508.
    KEGGi hsa:9508.
    UCSCi uc003hgk.2. human.

    Organism-specific databases

    CTDi 9508.
    GeneCardsi GC04M073136.
    H-InvDB HIX0004274.
    HGNCi HGNC:219. ADAMTS3.
    HPAi HPA021368.
    HPA021369.
    MIMi 605011. gene.
    neXtProti NX_O15072.
    PharmGKBi PA24547.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG307411.
    HOGENOMi HOG000034222.
    HOVERGENi HBG004314.
    InParanoidi O15072.
    KOi K08619.
    OMAi AEEWEHC.
    OrthoDBi EOG76HQ0N.
    PhylomeDBi O15072.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_200626. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    GeneWikii ADAMTS3.
    GenomeRNAii 9508.
    NextBioi 35628.
    PROi O15072.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15072.
    Bgeei O15072.
    CleanExi HS_ADAMTS3.
    Genevestigatori O15072.

    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.
    IPR010909. PLAC.
    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. 4 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF82895. SSF82895. 4 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50900. PLAC. 1 hit.
    PS50092. TSP1. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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], VARIANT LYS-138.
    3. "Procollagen II amino propeptide processing by ADAMTS-3. Insights on dermatosparaxis."
      Fernandes R.J., Hirohata S., Engle J.M., Colige A., Cohn D.H., Eyre D.R., Apte S.S.
      J. Biol. Chem. 276:31502-31509(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-227, VARIANT LYS-138.
    4. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-1205, VARIANT LYS-138.
      Tissue: Brain.

    Entry informationi

    Entry nameiATS3_HUMAN
    AccessioniPrimary (citable) accession number: O15072
    Secondary accession number(s): A1L3U9, Q9BXZ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 146 of the entry and version 4 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

    Caution

    Has sometimes been referred to as ADAMTS4.Curated

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3