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Q769J6

- ATS13_MOUSE

UniProt

Q769J6 - ATS13_MOUSE

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Protein

A disintegrin and metalloproteinase with thrombospondin motifs 13

Gene
Adamts13, Gm710
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript leveli

Functioni

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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi85 – 851Calcium By similarity
Metal bindingi175 – 1751Calcium By similarity
Metal bindingi184 – 1841Calcium; high affinity By similarity
Metal bindingi186 – 1861Calcium; high affinity By similarity
Metal bindingi189 – 1891Calcium; high affinity By similarity
Metal bindingi214 – 2141Calcium; high affinity By similarity
Metal bindingi226 – 2261Zinc; catalytic By similarity
Active sitei227 – 2271 By similarity
Metal bindingi230 – 2301Zinc; catalytic By similarity
Metal bindingi236 – 2361Zinc; catalytic By similarity
Metal bindingi281 – 2811Calcium By similarity
Metal bindingi289 – 2891Calcium By 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
Complete GO annotation...

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

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. proteinaceous extracellular matrix Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333 Reviewed predictionAdd
BLAST
Propeptidei34 – 7643 By 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...) Reviewed prediction
Glycosylationi148 – 1481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi157 ↔ 210 By similarity
Disulfide bondi204 ↔ 286 By similarity
Disulfide bondi246 ↔ 270 By similarity
Disulfide bondi316 ↔ 342 By similarity
Disulfide bondi327 ↔ 352 By similarity
Disulfide bondi337 ↔ 371 By similarity
Disulfide bondi365 ↔ 376 By similarity
Disulfide bondi401 ↔ 438 By similarity
Disulfide bondi405 ↔ 443 By similarity
Disulfide bondi416 ↔ 428 By similarity
Disulfide bondi488 ↔ 527 By similarity
Disulfide bondi513 ↔ 532 By similarity
Disulfide bondi537 ↔ 553 By similarity
Disulfide bondi550 ↔ 560 By similarity
Glycosylationi557 – 5571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi564 – 5641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi584 – 5841N-linked (GlcNAc...) Reviewed prediction
Glycosylationi619 – 6191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi703 – 7031O-linked (Fuc...) By similarity
Glycosylationi762 – 7621O-linked (Fuc...) By similarity
Glycosylationi834 – 8341N-linked (GlcNAc...) Reviewed prediction
Glycosylationi914 – 9141O-linked (Fuc...) By similarity
Glycosylationi973 – 9731O-linked (Fuc...) By similarity
Glycosylationi1033 – 10331O-linked (Fuc...) By similarity
Glycosylationi1057 – 10571N-linked (GlcNAc...) Reviewed prediction
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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 291218Peptidase M12BAdd
BLAST
Domaini295 – 38894DisintegrinAdd
BLAST
Domaini389 – 44456TSP type-1 1Add
BLAST
Domaini687 – 74660TSP type-1 2Add
BLAST
Domaini747 – 81064TSP type-1 3Add
BLAST
Domaini808 – 87164TSP type-1 4Add
BLAST
Domaini904 – 95754TSP type-1 5Add
BLAST
Domaini958 – 101962TSP type-1 6Add
BLAST
Domaini1020 – 107859TSP type-1 7Add
BLAST
Domaini1079 – 113759TSP type-1 8Add
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 site Reviewed prediction

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.

Sequence similaritiesi

Contains 2 CUB domains.
Contains 1 disintegrin domain.
Contains 8 TSP type-1 domains.

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

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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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti354 – 3541R → H in BAC55159. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 83 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

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