ATS13_MOUSE
ID ATS13_MOUSE Reviewed; 1426 AA.
AC Q769J6; A2ALB4; Q76LW1;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 13;
DE Short=ADAM-TS 13;
DE Short=ADAM-TS13;
DE Short=ADAMTS-13;
DE EC=3.4.24.87 {ECO:0000269|PubMed:15869605};
DE AltName: Full=von Willebrand factor-cleaving protease;
DE Short=vWF-CP;
DE Short=vWF-cleaving protease;
DE Flags: Precursor;
GN Name=Adamts13; Synonyms=Gm710;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP POLYMORPHISM.
RC STRAIN=129, and 129/Sv; TISSUE=Liver;
RX PubMed=15136581; DOI=10.1074/jbc.m314184200;
RA Banno F., Kaminaka K., Soejima K., Kokame K., Miyata T.;
RT "Identification of strain-specific variants of mouse Adamts13 gene encoding
RT von Willebrand factor-cleaving protease.";
RL J. Biol. Chem. 279:30896-30903(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15869605; DOI=10.1111/j.1538-7836.2005.01246.x;
RA Bruno K., Voelkel D., Plaimauer B., Antoine G., Pable S., Motto D.G.,
RA Lemmerhirt H.L., Dorner F., Zimmermann K., Scheiflinger F.;
RT "Cloning, expression and functional characterization of the full-length
RT murine ADAMTS13.";
RL J. Thromb. Haemost. 3:1064-1073(2005).
CC -!- FUNCTION: Cleaves the vWF multimers in plasma into smaller forms
CC thereby controlling vWF-mediated platelet thrombus formation.
CC {ECO:0000269|PubMed:15869605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=The enzyme cleaves the von Willebrand factor at bond 842-
CC Tyr-|-Met-843 within the A2 domain.; EC=3.4.24.87;
CC Evidence={ECO:0000269|PubMed:15869605};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UNA0};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q76LX8};
CC Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:Q76LX8};
CC -!- ACTIVITY REGULATION: Zinc and calcium ions cooperatively modulate
CC enzyme activity. The cleavage of the pro-domain is not required for
CC protease activity. Dependence on calcium for proteolytic activity is
CC mediated by the high affinity site (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15136581}.
CC Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Plasma. Expression is consistently high in liver,
CC medium in lung and spleen, low in skeletal muscle and undetectable in
CC heart, brain, kidney and testis. {ECO:0000269|PubMed:15136581,
CC ECO:0000269|PubMed:15869605}.
CC -!- DEVELOPMENTAL STAGE: Increases steadly with the age of embryo, reaching
CC highest levels in embryonic tissues of 19 days of gestation.
CC {ECO:0000269|PubMed:15869605}.
CC -!- DOMAIN: The pro-domain is not required for folding or secretion and
CC does not perform the common function of maintening enzyme latency.
CC {ECO:0000250}.
CC -!- DOMAIN: The globular cysteineless spacer domain adopts a jelly-roll
CC topology, and is necessary to recognize and cleave vWF. The C-terminal
CC TSP type-1 and CUB domains may modulate this interaction (By
CC similarity). {ECO:0000250}.
CC -!- PTM: The precursor is processed by a furin endopeptidase which cleaves
CC off the pro-domain. {ECO:0000250}.
CC -!- PTM: O-glycosylated (By similarity). O-fucosylated by POFUT2 on a
CC serine or a threonine residue found within the consensus sequence C1-
CC X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
CC the first and second cysteine residue of the repeat, respectively.
CC Fucosylated repeats can then be further glycosylated by the addition of
CC a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL.
CC Fucosylation mediates the efficient secretion of ADAMTS13. May also be
CC C-glycosylated on tryptophan residues within the consensus sequence W-
CC X-X-W of the TPRs, and also N-glycosylated. These other glycosylations
CC can also facilitate secretion (By similarity). {ECO:0000250}.
CC -!- POLYMORPHISM: Two variants (Adamts13L and Adamts13S) were isolated that
CC differed in the insertion of an intracisternal A particle (IAP)
CC retrotransposon including a premature stop at the position 1036. In
CC Adamts13S the C-terminal two TSP type-1 and two CUB domains are
CC replaced with a 16-amino acid sequence derived from the IAP, this
CC variant exhibited vWF cleaving activities in vitro. The IAP insertion
CC is strain-specific and is found in BALB/c, C3H/He, C57BL/6 and DBA/2
CC strains, but not in the 129/Sv strain.
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DR EMBL; AB071302; BAC55159.2; -; mRNA.
DR EMBL; AB095445; BAD04062.1; -; Genomic_DNA.
DR EMBL; AB112362; BAD18090.1; -; mRNA.
DR EMBL; AL773563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL845266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS15820.1; -.
DR RefSeq; NP_001001322.1; NM_001001322.2.
DR RefSeq; NP_001277392.1; NM_001290463.1.
DR AlphaFoldDB; Q769J6; -.
DR SMR; Q769J6; -.
DR STRING; 10090.ENSMUSP00000099955; -.
DR MEROPS; M12.241; -.
DR GlyGen; Q769J6; 14 sites.
DR iPTMnet; Q769J6; -.
DR PhosphoSitePlus; Q769J6; -.
DR MaxQB; Q769J6; -.
DR PaxDb; Q769J6; -.
DR PRIDE; Q769J6; -.
DR Antibodypedia; 31871; 382 antibodies from 36 providers.
DR DNASU; 279028; -.
DR Ensembl; ENSMUST00000102891; ENSMUSP00000099955; ENSMUSG00000014852.
DR GeneID; 279028; -.
DR KEGG; mmu:279028; -.
DR UCSC; uc008iwp.1; mouse.
DR CTD; 11093; -.
DR MGI; MGI:2685556; Adamts13.
DR VEuPathDB; HostDB:ENSMUSG00000014852; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000158379; -.
DR InParanoid; Q769J6; -.
DR OMA; HQAHQED; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; Q769J6; -.
DR TreeFam; TF313537; -.
DR BRENDA; 3.4.24.87; 3474.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 279028; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Adamts13; mouse.
DR PRO; PR:Q769J6; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q769J6; protein.
DR Bgee; ENSMUSG00000014852; Expressed in liver and 19 other tissues.
DR ExpressionAtlas; Q769J6; baseline and differential.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0004175; F:endopeptidase activity; IMP:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
DR GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0043171; P:peptide catabolic process; ISO:MGI.
DR GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0014075; P:response to amine; IEA:Ensembl.
DR GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR Gene3D; 2.20.100.10; -; 3.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR006586; ADAM_Cys-rich.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR Pfam; PF17771; ADAM_CR_2; 1.
DR Pfam; PF19236; ADAM_CR_3; 1.
DR Pfam; PF05986; ADAM_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 6.
DR SUPFAM; SSF49854; SSF49854; 2.
DR SUPFAM; SSF82895; SSF82895; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 4.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Disulfide bond; Glycoprotein; Hemostasis; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Zinc; Zymogen.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT PROPEP 34..76
FT /evidence="ECO:0000250"
FT /id="PRO_0000247512"
FT CHAIN 77..1426
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 13"
FT /id="PRO_0000247513"
FT DOMAIN 74..291
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 295..388
FT /note="Disintegrin"
FT DOMAIN 389..444
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 687..746
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 747..810
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 808..871
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 904..957
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 958..1019
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1020..1078
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1079..1137
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1195..1302
FT /note="CUB 1"
FT DOMAIN 1293..1426
FT /note="CUB 2"
FT REGION 445..561
FT /note="Cysteine-rich"
FT REGION 556..685
FT /note="Spacer"
FT MOTIF 503..505
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT ACT_SITE 227
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000250|UniProtKB:Q76LX8"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 230
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA0"
FT BINDING 281
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT CARBOHYD 144
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 564
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 584
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 762
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 834
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 973
FT /note="O-linked (Fuc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1033
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1057
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1093
FT /note="O-linked (Fuc...) serine"
FT /evidence="ECO:0000250"
FT DISULFID 157..210
FT /evidence="ECO:0000250"
FT DISULFID 204..286
FT /evidence="ECO:0000250"
FT DISULFID 246..270
FT /evidence="ECO:0000250"
FT DISULFID 316..342
FT /evidence="ECO:0000250"
FT DISULFID 327..352
FT /evidence="ECO:0000250"
FT DISULFID 337..371
FT /evidence="ECO:0000250"
FT DISULFID 365..376
FT /evidence="ECO:0000250"
FT DISULFID 401..438
FT /evidence="ECO:0000250"
FT DISULFID 405..443
FT /evidence="ECO:0000250"
FT DISULFID 416..428
FT /evidence="ECO:0000250"
FT DISULFID 488..527
FT /evidence="ECO:0000250"
FT DISULFID 513..532
FT /evidence="ECO:0000250"
FT DISULFID 537..553
FT /evidence="ECO:0000250"
FT DISULFID 550..560
FT /evidence="ECO:0000250"
FT VARIANT 1022..1037
FT /note="WKVLSLGPCSASCGLG -> ALVWEAAPTFAVTRWR (in Adamts13S)"
FT VARIANT 1038..1426
FT /note="Missing (in Adamts13S)"
FT CONFLICT 354
FT /note="R -> H (in Ref. 1; BAC55159)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1426 AA; 155357 MW; 62E9F672B91F6772 CRC64;
MSQLCLWLTC QPCYAVSVRG ILTGAIFILG CWGLSDFQKS LLQDLEPKDV SSYFGHHAAP
FTGHPPSHLQ RLRRRRTLED ILHLELLVAV GPDVSRAHQE DTERYVLTNL NIGSELLRNP
SLGVQFQVHL VKLITLSDSE STPNITANIT SSLMSVCEWS QTINPHDDRD PSHADLILYI
TRFDLELPDG NQQVRGVTQL GGACSLSWSC LITEDTGFDL GVTIAHEIGH SFGLDHDGAP
GSGSTCKASG HVMAADGATP TGGTLEWSAC SQRQLQHLLS TGQMHCFQDP PGLQSGLTRH
QLMAQPGLYY SADDQCRVAF GSGAVACTFS REGLDVCQAL SCHTDPLDQS SCSRLLVPLL
DGTECGVEKW CSKARCRSLA ELAPVAAVHG HWSSWGPHSP CSRSCGGGVI TRRRWCNNPR
PAFGGRACVG EDLQAKMCNT QACEKTQLEF MSEQCAQTDR QPLQLSQGTA SFYHWDAAVQ
YSQGDTLCRH MCWAVGESFI VSRGDRFLDG TRCVPSGPQD DGTLSLCLLG SCRTFGCDGR
MDSQKVWDAC QVCGGDNSTC SSRNGSFTAG RAREYVTFLI VTPNMTNAHI VNRRPLFTHL
AVRIQGHYIV AGKTSISPNT TYPSLLEDYR VEYRVTLTED QLPHLEEIHI RGPVRDDIEI
QVYRRYGGEY GDLTHPDITF SYFQLKQQAA WVWTAKRGPC SVSCGAGLRW VTYSCQDQAQ
DKWVKNAQCQ GSPQPPAWQE PCVSAPCSPY WVAGDFSPCS VSCGGGLRER SLRCVETQDG
FLKTLPPARC RAVAQQPAAE VENCNSQPCP TRWEVSDPGP CMSSACEAGL DSRNVTCVSR
AGDPEKPETA GPCRTDEMSA MLEPCSRSLC SPGLGQVDNT MSLGEEAPSP VGSDKPGAQA
EHVWTPLVGL CSISCGRGLK ELYFLCMDSV LKMPVQEELC GLASKPPSRW EVCRARPCPA
RWETQVLAPC PVTCGGGRVP LSVRCVQLDR GHPISVPHSK CSPVPKPGSF EDCSPEPCPA
RWKVLSLGPC SASCGLGTAT QMVACMQLDQ GHDNEVNETF CKALVRPQAS VPCLIADCAF
RWHISAWTEC SVSCGDGIQR RHDTCLGPQA QVPVPANFCQ HLPKPMTVRG CWAGPCAGQE
TSSSLPHKEA TLPSQTQAAA TVASLQWSQP RARTPTLFSA SQSLGLQENL EEHGACGRQY
LEPTGTIHMR DQGRLDCVVA IGRPLGEVVT LQILESSLKC SAGEQLLLWG RFTWRKTCRK
MPGMTFSTKT NTVVVKQHRV LPGGGVLLRY WSQPAPGTFY KECDRQLFGP RGEIVSPSLS
PDGRKAGTCR VFISVAPQAR IAIRALASDM GTASEGTNAN YVSIRDIHSL RTTTFWGQQV
LYWESEGSEA ELEFSPGFLE AHASLQGEYW TISPRTSEQD DSLALS
