ATS1_RAT
ID ATS1_RAT Reviewed; 967 AA.
AC Q9WUQ1; Q9ERI1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1;
DE Short=ADAM-TS 1;
DE Short=ADAM-TS1;
DE Short=ADAMTS-1;
DE EC=3.4.24.-;
DE Flags: Precursor;
GN Name=Adamts1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Liu X., Tu Y., Yin T., Johnstone E.M., Stephenson D.T., Clemens J.A.,
RA Little S.P.;
RT "Induction of a disintegrin and metalloprotease with the thrombospondin
RT type I motif (ADAMTS).";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-967.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=10847486; DOI=10.1034/j.1600-0676.2000.020002165.x;
RA Diamantis I., Luethi M., Hoesli M., Reichen J.;
RT "Cloning of the rat ADAMTS-1 gene and its down regulation in endothelial
RT cells in cirrhotic rats.";
RL Liver 20:165-172(2000).
CC -!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1683-
CC Glu-|-Leu-1684' site (within the chondroitin sulfate attachment
CC domain), and may be involved in its turnover. Has angiogenic inhibitor
CC activity (By similarity). Active metalloprotease, which may be
CC associated with various inflammatory processes as well as development
CC of cancer cachexia. May play a critical role in follicular rupture (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9UHI8};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}.
CC -!- INDUCTION: Down-regulated in endothelial cells derived from cirrhotic
CC liver.
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix.
CC -!- DOMAIN: The conserved cysteine present in the cysteine-switch motif
CC binds the catalytic zinc ion, thus inhibiting the enzyme. The
CC dissociation of the cysteine from the zinc ion upon the activation-
CC peptide release activates the enzyme.
CC -!- PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
CC -!- PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a
CC threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-
CC G of the TSP type-1 repeat domains where C1 and C2 are the first and
CC second cysteine residue of the repeat, respectively. Fucosylated
CC repeats can then be further glycosylated by the addition of a beta-1,3-
CC glucose residue by the glucosyltransferase, B3GALTL. Fucosylation
CC mediates the efficient secretion of ADAMTS family members. Can also be
CC C-glycosylated with one or two mannose molecules on tryptophan residues
CC within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated.
CC These other glycosylations can also facilitate secretion (By
CC similarity). {ECO:0000250}.
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DR EMBL; AF149118; AAD34012.1; -; mRNA.
DR EMBL; AF304446; AAG29823.1; -; mRNA.
DR AlphaFoldDB; Q9WUQ1; -.
DR SMR; Q9WUQ1; -.
DR STRING; 10116.ENSRNOP00000002187; -.
DR MEROPS; M12.222; -.
DR GlyGen; Q9WUQ1; 5 sites.
DR PaxDb; Q9WUQ1; -.
DR PRIDE; Q9WUQ1; -.
DR UCSC; RGD:621241; rat.
DR RGD; 621241; Adamts1.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; Q9WUQ1; -.
DR PhylomeDB; Q9WUQ1; -.
DR BRENDA; 3.4.24.B11; 5301.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:Q9WUQ1; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005604; C:basement membrane; ISO:RGD.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:RGD.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
DR GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060347; P:heart trabecula formation; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0030728; P:ovulation; IEP:RGD.
DR GO; GO:0001542; P:ovulation from ovarian follicle; ISO:RGD.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:RGD.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0044691; P:tooth eruption; IEP:RGD.
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; IPR013274; Pept_M12B_ADAM-TS1.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
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; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01858; ADAMTS1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF82895; SSF82895; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Heparin-binding; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
KW Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..54
FT /evidence="ECO:0000255"
FT PROPEP 55..252
FT /evidence="ECO:0000250"
FT /id="PRO_0000029154"
FT CHAIN 253..967
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 1"
FT /id="PRO_0000029155"
FT DOMAIN 258..467
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 476..558
FT /note="Disintegrin"
FT DOMAIN 559..614
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 854..910
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 911..967
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 198..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 725..857
FT /note="Spacer"
FT MOTIF 203..210
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 211..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000250"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 261
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 405
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 411
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 462
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 465
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT CARBOHYD 547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 720
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 764
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 945
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 333..385
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 362..367
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 379..462
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 417..446
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 488..511
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 499..521
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 506..540
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 534..545
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 571..608
FT /evidence="ECO:0000250"
FT DISULFID 575..613
FT /evidence="ECO:0000250"
FT DISULFID 586..598
FT /evidence="ECO:0000250"
FT CONFLICT 21
FT /note="I -> V (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..31
FT /note="KFRSSQ -> RSRGSL (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="V -> A (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="R -> P (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="L -> TR (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="R -> G (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 262..265
FT /note="TMLV -> NLLK (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="S -> F (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="L -> V (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
FT CONFLICT 962
FT /note="I -> T (in Ref. 2; AAG29823)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 967 AA; 105706 MW; F93C864F6DCDB4CF CRC64;
MQPEVPLGSG KLKPCSDMGD IQRAAKFRSS QSAHMLLLLL ASITMLLCVR GAHGRPTEED
EELVLPSLER ARGHDSTTLL RLDAFGQQLH LKLQPDSGFL APGFTLQTVG RSPGSEAQHL
DPTGDLAHCF YSGTVNGDPS SAAALSLCEG VRGAFYLQGE EFFIQPAPAV ATERLVPAEP
KEESIAPPRF HILRRRRRGS GGAKCGVMDE ETLPTSNSGR ESQNTPDQWP LRNPTPQGAG
KPTGPGSIRK KRFVSSPRYV ETMLVADQSM ADFHGSGLKH YLLTLFSVAA RFYKHPSIRN
SISLVVVKIL VIYEEQKGPE VTSNAALTLR NFCSWQKQHN SPSDRDPEHY DTAILFTRQD
LCGSHTCDTL GMADVGTVCD PSRSCSVIED DGLQAAFTTA HELGHVFNMP HDDAKHCASF
NGVSGDSHLM ASMLSSLDHS QPWSPCSAYM VTSFLDNGHG ECLMDKPQNP IKLPSDLPGT
LYDANRQCQF TFGEESTHCP DAASTCSTLW CTGTSGGLLV CQTKHFPWAD GTSCGEGKWC
VSGKCVNKTD MKHFATPVHG SWGPWGPWGD CSRTCGGGVQ YTMRECDNPV PKNGGKYCEG
KRVRYRSCNI EDCPDNNGKT FREEQCEAHN EFSKASFGNE PTVEWTPKYA GVSPKDRCKL
TCEAKGIGYF FVLQPKVVDG TPCSPDSTSV CVQGQCVKAG CDRIIDSKKK FDKCGVCGGN
GSTCKKISGT VTSTRPGYHD IVTIPAGATN IEVKHRNPRG SRNNGSFLAI RAADGTYILN
GNFTLSTLEQ DLTYKGTVLR YSGSSAALER IRSFSPLKEP LTIQVLMVGH ALRPKIKYTY
FMKKKTEPFN AIPTFSEWVI EEWGECSKTC GSGWQRRVVE CRDINGHPAS ECAKEVKPAS
TRPCADLPCP RWQVGDWSPC SKTCGKGYKK RTLKCLSHDG GVLSNESCDP LKKPKHYIDF
CILTQCS
