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Q769J6 (ATS13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
A disintegrin and metalloproteinase with thrombospondin motifs 13

Short name=ADAM-TS 13
Short name=ADAM-TS13
Short name=ADAMTS-13
EC=3.4.24.87
Alternative name(s):
von Willebrand factor-cleaving protease
Short name=vWF-CP
Short name=vWF-cleaving protease
Gene names
Name:Adamts13
Synonyms:Gm710
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1426 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Cleaves the vWF multimers in plasma into smaller forms. Ref.3

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Binds 4 calcium ions By similarity.

Enzyme regulation

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.

Subcellular location

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

Tissue specificity

Plasma. Expression is consistently high in liver, medium in lung and spleen, low in skeletal muscle and undetectable in heart, brain, kidney and testis. Ref.1 Ref.3

Developmental stage

Increases steadly with the age of embryo, reaching highest levels in embryonic tissues of 19 days of gestation. Ref.3

Domain

The pro-domain is not required for folding or secretion and does not perform the common function of maintening enzyme latency By similarity.

The spacer domain is necessary to recognize and cleave vWF. The C-terminal TSP type-1 and CUB domains may modulate this interaction By similarity.

Post-translational modification

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.

Polymorphism

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.

Sequence similarities

Contains 2 CUB domains.

Contains 1 disintegrin domain.

Contains 1 peptidase M12B domain.

Contains 8 TSP type-1 domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333 Potential
Propeptide34 – 7643 By similarity
PRO_0000247512
Chain77 – 14261350A disintegrin and metalloproteinase with thrombospondin motifs 13
PRO_0000247513

Regions

Domain74 – 291218Peptidase M12B
Domain295 – 38894Disintegrin
Domain389 – 44456TSP type-1 1
Domain687 – 74660TSP type-1 2
Domain747 – 81064TSP type-1 3
Domain808 – 87164TSP type-1 4
Domain904 – 95754TSP type-1 5
Domain958 – 101962TSP type-1 6
Domain1020 – 107859TSP type-1 7
Domain1079 – 113759TSP type-1 8
Domain1195 – 1302108CUB 1
Domain1293 – 1426134CUB 2
Region445 – 561117Cysteine-rich
Region556 – 685130Spacer
Motif503 – 5053Cell attachment site Potential

Sites

Active site2271 By similarity
Metal binding851Calcium By similarity
Metal binding1751Calcium By similarity
Metal binding1841Calcium; high affinity By similarity
Metal binding1861Calcium; high affinity By similarity
Metal binding1891Calcium; high affinity By similarity
Metal binding2141Calcium; high affinity By similarity
Metal binding2261Zinc; catalytic By similarity
Metal binding2301Zinc; catalytic By similarity
Metal binding2361Zinc; catalytic By similarity
Metal binding2811Calcium By similarity
Metal binding2891Calcium By similarity

Amino acid modifications

Glycosylation1441N-linked (GlcNAc...) Potential
Glycosylation1481N-linked (GlcNAc...) Potential
Glycosylation5571N-linked (GlcNAc...) Potential
Glycosylation5641N-linked (GlcNAc...) Potential
Glycosylation5841N-linked (GlcNAc...) Potential
Glycosylation6191N-linked (GlcNAc...) Potential
Glycosylation7031O-linked (Fuc...) By similarity
Glycosylation7621O-linked (Fuc...) By similarity
Glycosylation8341N-linked (GlcNAc...) Potential
Glycosylation9141O-linked (Fuc...) By similarity
Glycosylation9731O-linked (Fuc...) By similarity
Glycosylation10331O-linked (Fuc...) By similarity
Glycosylation10571N-linked (GlcNAc...) Potential
Glycosylation10931O-linked (Fuc...) By similarity
Disulfide bond157 ↔ 210 By similarity
Disulfide bond204 ↔ 286 By similarity
Disulfide bond246 ↔ 270 By similarity
Disulfide bond316 ↔ 342 By similarity
Disulfide bond327 ↔ 352 By similarity
Disulfide bond337 ↔ 371 By similarity
Disulfide bond365 ↔ 376 By similarity
Disulfide bond401 ↔ 438 By similarity
Disulfide bond405 ↔ 443 By similarity
Disulfide bond416 ↔ 428 By similarity

Natural variations

Natural variant1022 – 103716WKVLS…SCGLG → ALVWEAAPTFAVTRWR in Adamts13S.
Natural variant1038 – 1426389Missing in Adamts13S.

Experimental info

Sequence conflict3541R → H in BAC55159. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q769J6 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 62E9F672B91F6772

FASTA1,426155,357
        10         20         30         40         50         60 
MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV SSYFGHHAAP 

        70         80         90        100        110        120 
FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE DTERYVLTNL NIGSELLRNP 

       130        140        150        160        170        180 
SLGVQFQVHL VKLITLSDSE STPNITANIT SSLMSVCEWS QTINPHDDRD PSHADLILYI 

       190        200        210        220        230        240 
TRFDLELPDG NQQVRGVTQL GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP 

       250        260        270        280        290        300 
GSGSTCKASG HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH 

       310        320        330        340        350        360 
QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS SCSRLLVPLL 

       370        380        390        400        410        420 
DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP CSRSCGGGVI TRRRWCNNPR 

       430        440        450        460        470        480 
PAFGGRACVG EDLQAKMCNT QACEKTQLEF MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ 

       490        500        510        520        530        540 
YSQGDTLCRH MCWAVGESFI VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR 

       550        560        570        580        590        600 
MDSQKVWDAC QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL 

       610        620        630        640        650        660 
AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI RGPVRDDIEI 

       670        680        690        700        710        720 
QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC SVSCGAGLRW VTYSCQDQAQ 

       730        740        750        760        770        780 
DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY WVAGDFSPCS VSCGGGLRER SLRCVETQDG 

       790        800        810        820        830        840 
FLKTLPPARC RAVAQQPAAE VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR 

       850        860        870        880        890        900 
AGDPEKPETA GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA 

       910        920        930        940        950        960 
EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW EVCRARPCPA 

       970        980        990       1000       1010       1020 
RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK CSPVPKPGSF EDCSPEPCPA 

      1030       1040       1050       1060       1070       1080 
RWKVLSLGPC SASCGLGTAT QMVACMQLDQ GHDNEVNETF CKALVRPQAS VPCLIADCAF 

      1090       1100       1110       1120       1130       1140 
RWHISAWTEC SVSCGDGIQR RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE 

      1150       1160       1170       1180       1190       1200 
TSSSLPHKEA TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY 

      1210       1220       1230       1240       1250       1260 
LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG RFTWRKTCRK 

      1270       1280       1290       1300       1310       1320 
MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY KECDRQLFGP RGEIVSPSLS 

      1330       1340       1350       1360       1370       1380 
PDGRKAGTCR VFISVAPQAR IAIRALASDM GTASEGTNAN YVSIRDIHSL RTTTFWGQQV 

      1390       1400       1410       1420 
LYWESEGSEA ELEFSPGFLE AHASLQGEYW TISPRTSEQD DSLALS 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS15820.1.
RefSeqNP_001001322.1. NM_001001322.2.
UniGeneMm.330084.

3D structure databases

ProteinModelPortalQ769J6.
SMRQ769J6. Positions 83-686.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000099955.

Protein family/group databases

MEROPSM12.241.

PTM databases

PhosphoSiteQ769J6.

Proteomic databases

PRIDEQ769J6.

Protocols and materials databases

DNASU279028.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102891; ENSMUSP00000099955; ENSMUSG00000014852.
GeneID279028.
KEGGmmu:279028.
UCSCuc008iwp.1. mouse.

Organism-specific databases

CTD11093.
MGIMGI:2685556. Adamts13.

Phylogenomic databases

eggNOGNOG239882.
GeneTreeENSGT00750000117224.
HOGENOMHOG000231627.
HOVERGENHBG080358.
InParanoidA2ALB4.
KOK08627.
OMACDMQLFG.
PhylomeDBQ769J6.
TreeFamTF313537.

Gene expression databases

BgeeQ769J6.
GenevestigatorQ769J6.

Family and domain databases

Gene3D3.40.390.10. 1 hit.
InterProIPR000859. CUB_dom.
IPR024079. MetalloPept_cat_dom.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. Thrombospondin_1_rpt.
[Graphical view]
PfamPF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 3 hits.
[Graphical view]
PRINTSPR01857. ADAMTSFAMILY.
SMARTSM00209. TSP1. 6 hits.
[Graphical view]
SUPFAMSSF49854. SSF49854. 2 hits.
SSF82895. SSF82895. 4 hits.
PROSITEPS50215. ADAM_MEPRO. 1 hit.
PS50092. TSP1. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio393955.
PROQ769J6.
SOURCESearch...

Entry information

Entry nameATS13_MOUSE
AccessionPrimary (citable) accession number: Q769J6
Secondary accession number(s): A2ALB4, Q76LW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot