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Q769J6

- ATS13_MOUSE

UniProt

Q769J6 - ATS13_MOUSE

Protein

A disintegrin and metalloproteinase with thrombospondin motifs 13

Gene

Adamts13

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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      Entry version 84 (01 Oct 2014)
      Sequence version 1 (19 Jul 2004)
      Previous versions | rss
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    Functioni

    Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation.1 Publication

    Catalytic activityi

    Cleaves the vWF at the 842-Tyr-|-Met-843 in the A2 domain of the vWF subunit.
    The enzyme cleaves the von Willebrand factor at bond Tyr(842)-|-Met(843) within the A2 domain.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Binds 4 calcium ions.By similarity

    Enzyme regulationi

    Zinc and calcium ions cooperatively modulate enzyme activity. The cleavage of the pro-domain is not required for protease activity. Dependence on calcium for proteolytic activity is mediated by the high affinity site By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851CalciumBy similarity
    Metal bindingi175 – 1751CalciumBy similarity
    Metal bindingi184 – 1841Calcium; high affinityBy similarity
    Metal bindingi186 – 1861Calcium; high affinityBy similarity
    Metal bindingi189 – 1891Calcium; high affinityBy similarity
    Metal bindingi214 – 2141Calcium; high affinityBy similarity
    Metal bindingi226 – 2261Zinc; catalyticBy similarity
    Active sitei227 – 2271PROSITE-ProRule annotation
    Metal bindingi230 – 2301Zinc; catalyticBy similarity
    Metal bindingi236 – 2361Zinc; catalyticBy similarity
    Metal bindingi281 – 2811CalciumBy similarity
    Metal bindingi289 – 2891CalciumBy similarity

    GO - Molecular functioni

    1. endopeptidase activity Source: MGI
    2. metalloendopeptidase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. blood coagulation Source: UniProtKB-KW
    2. peptide catabolic process Source: Ensembl
    3. proteolysis Source: MGI
    4. response to interferon-gamma Source: Ensembl
    5. response to interleukin-4 Source: Ensembl
    6. response to tumor necrosis factor Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_211817. O-glycosylation of TSR domain-containing proteins.

    Protein family/group databases

    MEROPSiM12.241.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A disintegrin and metalloproteinase with thrombospondin motifs 13 (EC:3.4.24.87)
    Short name:
    ADAM-TS 13
    Short name:
    ADAM-TS13
    Short name:
    ADAMTS-13
    Alternative name(s):
    von Willebrand factor-cleaving protease
    Short name:
    vWF-CP
    Short name:
    vWF-cleaving protease
    Gene namesi
    Name:Adamts13
    Synonyms:Gm710
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2685556. Adamts13.

    Subcellular locationi

    Secreted 1 Publication
    Note: Secretion enhanced by O-fucosylation of TSP type-1 repeats.By similarity

    GO - Cellular componenti

    1. extracellular space Source: MGI
    2. proteinaceous extracellular matrix Source: InterPro

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Propeptidei34 – 7643By similarityPRO_0000247512Add
    BLAST
    Chaini77 – 14261350A disintegrin and metalloproteinase with thrombospondin motifs 13PRO_0000247513Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi148 – 1481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi157 ↔ 210By similarity
    Disulfide bondi204 ↔ 286By similarity
    Disulfide bondi246 ↔ 270By similarity
    Disulfide bondi316 ↔ 342By similarity
    Disulfide bondi327 ↔ 352By similarity
    Disulfide bondi337 ↔ 371By similarity
    Disulfide bondi365 ↔ 376By similarity
    Disulfide bondi401 ↔ 438By similarity
    Disulfide bondi405 ↔ 443By similarity
    Disulfide bondi416 ↔ 428By similarity
    Disulfide bondi488 ↔ 527By similarity
    Disulfide bondi513 ↔ 532By similarity
    Disulfide bondi537 ↔ 553By similarity
    Disulfide bondi550 ↔ 560By similarity
    Glycosylationi557 – 5571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi564 – 5641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi584 – 5841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi619 – 6191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi703 – 7031O-linked (Fuc...)By similarity
    Glycosylationi762 – 7621O-linked (Fuc...)By similarity
    Glycosylationi834 – 8341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi914 – 9141O-linked (Fuc...)By similarity
    Glycosylationi973 – 9731O-linked (Fuc...)By similarity
    Glycosylationi1033 – 10331O-linked (Fuc...)By similarity
    Glycosylationi1057 – 10571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1093 – 10931O-linked (Fuc...)By similarity

    Post-translational modificationi

    The precursor is processed by a furin endopeptidase which cleaves off the pro-domain.By similarity
    O-glycosylated By similarity. 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 ADAMTS13. May also be C-glycosylated on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and also 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

    PRIDEiQ769J6.

    PTM databases

    PhosphoSiteiQ769J6.

    Expressioni

    Tissue specificityi

    Plasma. Expression is consistently high in liver, medium in lung and spleen, low in skeletal muscle and undetectable in heart, brain, kidney and testis.2 Publications

    Developmental stagei

    Increases steadly with the age of embryo, reaching highest levels in embryonic tissues of 19 days of gestation.1 Publication

    Gene expression databases

    BgeeiQ769J6.
    GenevestigatoriQ769J6.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000099955.

    Structurei

    3D structure databases

    ProteinModelPortaliQ769J6.
    SMRiQ769J6. Positions 83-686.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 291218Peptidase M12BPROSITE-ProRule annotationAdd
    BLAST
    Domaini295 – 38894DisintegrinAdd
    BLAST
    Domaini389 – 44456TSP type-1 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini687 – 74660TSP type-1 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini747 – 81064TSP type-1 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini808 – 87164TSP type-1 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini904 – 95754TSP type-1 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini958 – 101962TSP type-1 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1020 – 107859TSP type-1 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1079 – 113759TSP type-1 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini1195 – 1302108CUB 1Add
    BLAST
    Domaini1293 – 1426134CUB 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni445 – 561117Cysteine-richAdd
    BLAST
    Regioni556 – 685130SpacerAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi503 – 5053Cell attachment siteSequence Analysis

    Domaini

    The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency.By similarity
    The globular cysteineless spacer domain adopts a jelly-roll topology, and is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction By similarity.By similarity

    Sequence similaritiesi

    Contains 2 CUB domains.Curated
    Contains 1 disintegrin domain.Curated
    Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
    Contains 8 TSP type-1 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG239882.
    GeneTreeiENSGT00750000117224.
    HOGENOMiHOG000231627.
    HOVERGENiHBG080358.
    InParanoidiA2ALB4.
    KOiK08627.
    OMAiCDMQLFG.
    PhylomeDBiQ769J6.
    TreeFamiTF313537.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR000859. CUB_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view]
    PfamiPF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 3 hits.
    [Graphical view]
    PRINTSiPR01857. ADAMTSFAMILY.
    SMARTiSM00209. TSP1. 6 hits.
    [Graphical view]
    SUPFAMiSSF49854. SSF49854. 2 hits.
    SSF82895. SSF82895. 4 hits.
    PROSITEiPS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q769J6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV     50
    SSYFGHHAAP FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE 100
    DTERYVLTNL NIGSELLRNP SLGVQFQVHL VKLITLSDSE STPNITANIT 150
    SSLMSVCEWS QTINPHDDRD PSHADLILYI TRFDLELPDG NQQVRGVTQL 200
    GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP GSGSTCKASG 250
    HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH 300
    QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS 350
    SCSRLLVPLL DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP 400
    CSRSCGGGVI TRRRWCNNPR PAFGGRACVG EDLQAKMCNT QACEKTQLEF 450
    MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ YSQGDTLCRH MCWAVGESFI 500
    VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR MDSQKVWDAC 550
    QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL 600
    AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI 650
    RGPVRDDIEI QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC 700
    SVSCGAGLRW VTYSCQDQAQ DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY 750
    WVAGDFSPCS VSCGGGLRER SLRCVETQDG FLKTLPPARC RAVAQQPAAE 800
    VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR AGDPEKPETA 850
    GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA 900
    EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW 950
    EVCRARPCPA RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK 1000
    CSPVPKPGSF EDCSPEPCPA RWKVLSLGPC SASCGLGTAT QMVACMQLDQ 1050
    GHDNEVNETF CKALVRPQAS VPCLIADCAF RWHISAWTEC SVSCGDGIQR 1100
    RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE TSSSLPHKEA 1150
    TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY 1200
    LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG 1250
    RFTWRKTCRK MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY 1300
    KECDRQLFGP RGEIVSPSLS PDGRKAGTCR VFISVAPQAR IAIRALASDM 1350
    GTASEGTNAN YVSIRDIHSL RTTTFWGQQV LYWESEGSEA ELEFSPGFLE 1400
    AHASLQGEYW TISPRTSEQD DSLALS 1426
    Length:1,426
    Mass (Da):155,357
    Last modified:July 19, 2004 - v1
    Checksum:i62E9F672B91F6772
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti354 – 3541R → H in BAC55159. (PubMed:15136581)Curated

    Polymorphismi

    Two variants (Adamts13L and Adamts13S) were isolated that differed in the insertion of an intracisternal A particle (IAP) retrotransposon including a premature stop at the position 1036. In Adamts13S the C-terminal two TSP type-1 and two CUB domains are replaced with a 16-amino acid sequence derived from the IAP, this variant exhibited vWF cleaving activities in vitro. The IAP insertion is strain-specific and is found in BALB/c, C3H/He, C57BL/6 and DBA/2 strains, but not in the 129/Sv strain.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1022 – 103716WKVLS…SCGLG → ALVWEAAPTFAVTRWR in Adamts13S.
    Add
    BLAST
    Natural varianti1038 – 1426389Missing in Adamts13S.
    Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071302 mRNA. Translation: BAC55159.2.
    AB095445 Genomic DNA. Translation: BAD04062.1.
    AB112362 mRNA. Translation: BAD18090.1.
    AL773563, AL845266 Genomic DNA. Translation: CAM23711.1.
    AL845266, AL773563 Genomic DNA. Translation: CAM24664.1.
    CCDSiCCDS15820.1.
    RefSeqiNP_001001322.1. NM_001001322.2.
    UniGeneiMm.330084.

    Genome annotation databases

    EnsembliENSMUST00000102891; ENSMUSP00000099955; ENSMUSG00000014852.
    GeneIDi279028.
    KEGGimmu:279028.
    UCSCiuc008iwp.1. mouse.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB071302 mRNA. Translation: BAC55159.2 .
    AB095445 Genomic DNA. Translation: BAD04062.1 .
    AB112362 mRNA. Translation: BAD18090.1 .
    AL773563 , AL845266 Genomic DNA. Translation: CAM23711.1 .
    AL845266 , AL773563 Genomic DNA. Translation: CAM24664.1 .
    CCDSi CCDS15820.1.
    RefSeqi NP_001001322.1. NM_001001322.2.
    UniGenei Mm.330084.

    3D structure databases

    ProteinModelPortali Q769J6.
    SMRi Q769J6. Positions 83-686.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000099955.

    Protein family/group databases

    MEROPSi M12.241.

    PTM databases

    PhosphoSitei Q769J6.

    Proteomic databases

    PRIDEi Q769J6.

    Protocols and materials databases

    DNASUi 279028.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000102891 ; ENSMUSP00000099955 ; ENSMUSG00000014852 .
    GeneIDi 279028.
    KEGGi mmu:279028.
    UCSCi uc008iwp.1. mouse.

    Organism-specific databases

    CTDi 11093.
    MGIi MGI:2685556. Adamts13.

    Phylogenomic databases

    eggNOGi NOG239882.
    GeneTreei ENSGT00750000117224.
    HOGENOMi HOG000231627.
    HOVERGENi HBG080358.
    InParanoidi A2ALB4.
    KOi K08627.
    OMAi CDMQLFG.
    PhylomeDBi Q769J6.
    TreeFami TF313537.

    Enzyme and pathway databases

    Reactomei REACT_211817. O-glycosylation of TSR domain-containing proteins.

    Miscellaneous databases

    NextBioi 393955.
    PROi Q769J6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q769J6.
    Genevestigatori Q769J6.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR000859. CUB_dom.
    IPR024079. MetalloPept_cat_dom.
    IPR001590. Peptidase_M12B.
    IPR013273. Peptidase_M12B_ADAM-TS.
    IPR000884. Thrombospondin_1_rpt.
    [Graphical view ]
    Pfami PF01421. Reprolysin. 1 hit.
    PF00090. TSP_1. 3 hits.
    [Graphical view ]
    PRINTSi PR01857. ADAMTSFAMILY.
    SMARTi SM00209. TSP1. 6 hits.
    [Graphical view ]
    SUPFAMi SSF49854. SSF49854. 2 hits.
    SSF82895. SSF82895. 4 hits.
    PROSITEi PS50215. ADAM_MEPRO. 1 hit.
    PS50092. TSP1. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of strain-specific variants of mouse Adamts13 gene encoding von Willebrand factor-cleaving protease."
      Banno F., Kaminaka K., Soejima K., Kokame K., Miyata T.
      J. Biol. Chem. 279:30896-30903(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, POLYMORPHISM.
      Strain: 129 and 129/Sv.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Cloning, expression and functional characterization of the full-length murine ADAMTS13."
      Bruno K., Voelkel D., Plaimauer B., Antoine G., Pable S., Motto D.G., Lemmerhirt H.L., Dorner F., Zimmermann K., Scheiflinger F.
      J. Thromb. Haemost. 3:1064-1073(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

    Entry informationi

    Entry nameiATS13_MOUSE
    AccessioniPrimary (citable) accession number: Q769J6
    Secondary accession number(s): A2ALB4, Q76LW1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: July 19, 2004
    Last modified: October 1, 2014
    This is version 84 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. 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