Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q769J6

- ATS13_MOUSE

UniProt

Q769J6 - ATS13_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarityNote: Binds 4 Ca(2+) 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
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.

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
Complete GO annotation...

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.
ExpressionAtlasiQ769J6. baseline and differential.
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.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000231627.
HOVERGENiHBG080358.
InParanoidiQ769J6.
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

        10         20         30         40         50
MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV
60 70 80 90 100
SSYFGHHAAP FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE
110 120 130 140 150
DTERYVLTNL NIGSELLRNP SLGVQFQVHL VKLITLSDSE STPNITANIT
160 170 180 190 200
SSLMSVCEWS QTINPHDDRD PSHADLILYI TRFDLELPDG NQQVRGVTQL
210 220 230 240 250
GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP GSGSTCKASG
260 270 280 290 300
HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH
310 320 330 340 350
QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS
360 370 380 390 400
SCSRLLVPLL DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP
410 420 430 440 450
CSRSCGGGVI TRRRWCNNPR PAFGGRACVG EDLQAKMCNT QACEKTQLEF
460 470 480 490 500
MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ YSQGDTLCRH MCWAVGESFI
510 520 530 540 550
VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR MDSQKVWDAC
560 570 580 590 600
QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL
610 620 630 640 650
AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI
660 670 680 690 700
RGPVRDDIEI QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC
710 720 730 740 750
SVSCGAGLRW VTYSCQDQAQ DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY
760 770 780 790 800
WVAGDFSPCS VSCGGGLRER SLRCVETQDG FLKTLPPARC RAVAQQPAAE
810 820 830 840 850
VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR AGDPEKPETA
860 870 880 890 900
GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA
910 920 930 940 950
EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW
960 970 980 990 1000
EVCRARPCPA RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK
1010 1020 1030 1040 1050
CSPVPKPGSF EDCSPEPCPA RWKVLSLGPC SASCGLGTAT QMVACMQLDQ
1060 1070 1080 1090 1100
GHDNEVNETF CKALVRPQAS VPCLIADCAF RWHISAWTEC SVSCGDGIQR
1110 1120 1130 1140 1150
RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE TSSSLPHKEA
1160 1170 1180 1190 1200
TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY
1210 1220 1230 1240 1250
LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG
1260 1270 1280 1290 1300
RFTWRKTCRK MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY
1310 1320 1330 1340 1350
KECDRQLFGP RGEIVSPSLS PDGRKAGTCR VFISVAPQAR IAIRALASDM
1360 1370 1380 1390 1400
GTASEGTNAN YVSIRDIHSL RTTTFWGQQV LYWESEGSEA ELEFSPGFLE
1410 1420
AHASLQGEYW TISPRTSEQD DSLALS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

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 ENSGT00760000118885.
HOGENOMi HOG000231627.
HOVERGENi HBG080358.
InParanoidi Q769J6.
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.
ExpressionAtlasi Q769J6. baseline and differential.
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: November 26, 2014
This is version 86 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