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A disintegrin and metalloproteinase with thrombospondin motifs 1 (ADAM-TS 1) (ADAM-TS1) (ADAMTS-1) (EC 3.4.24.-)

 ATS1_RAT                Reviewed;         967 AA.
Q9WUQ1; Q9ERI1;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
23-MAY-2018, entry version 137.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 1;
Short=ADAM-TS 1;
Short=ADAM-TS1;
Short=ADAMTS-1;
EC=3.4.24.-;
Flags: Precursor;
Name=Adamts1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Brain;
Liu X., Tu Y., Yin T., Johnstone E.M., Stephenson D.T., Clemens J.A.,
Little S.P.;
"Induction of a disintegrin and metalloprotease with the
thrombospondin type I motif (ADAMTS).";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-967.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=10847486; DOI=10.1034/j.1600-0676.2000.020002165.x;
Diamantis I., Luethi M., Hoesli M., Reichen J.;
"Cloning of the rat ADAMTS-1 gene and its down regulation in
endothelial cells in cirrhotic rats.";
Liver 20:165-172(2000).
-!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the
'1683-Glu-|-Leu-1684' site (within the chondroitin sulfate
attachment domain), and may be involved in its turnover. Has
angiogenic inhibitor activity (By similarity). Active
metalloprotease, which may be associated with various inflammatory
processes as well as development of cancer cachexia. May play a
critical role in follicular rupture (By similarity).
{ECO:0000250}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9UHI8};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UHI8};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- INDUCTION: Down-regulated in endothelial cells derived from
cirrhotic liver.
-!- DOMAIN: The spacer domain and the TSP type-1 domains are important
for a tight interaction with the extracellular matrix.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Glycosylated. Can be 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 ADAMTS
family members. Also can be C-glycosylated with one or two mannose
molecules on tryptophan residues within the consensus sequence W-
X-X-W of the TPRs, and N-glycosylated. These other glycosylations
can also facilitate secretion (By similarity). {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; AF149118; AAD34012.1; -; mRNA.
EMBL; AF304446; AAG29823.1; -; mRNA.
UniGene; Rn.7897; -.
ProteinModelPortal; Q9WUQ1; -.
SMR; Q9WUQ1; -.
STRING; 10116.ENSRNOP00000002187; -.
MEROPS; M12.222; -.
PaxDb; Q9WUQ1; -.
PRIDE; Q9WUQ1; -.
UCSC; RGD:621241; rat.
RGD; 621241; Adamts1.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
HOGENOM; HOG000004799; -.
HOVERGEN; HBG004313; -.
InParanoid; Q9WUQ1; -.
PhylomeDB; Q9WUQ1; -.
BRENDA; 3.4.24.B11; 5301.
PRO; PR:Q9WUQ1; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031012; C:extracellular matrix; IDA:RGD.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEP:RGD.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IEP:RGD.
GO; GO:0071305; P:cellular response to vitamin D; IEP:RGD.
GO; GO:0030728; P:ovulation; IEP:RGD.
GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
GO; GO:0044691; P:tooth eruption; IEP:RGD.
Gene3D; 2.20.100.10; -; 3.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR010294; ADAM_spacer1.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR013274; Pept_M12B_ADAM-TS1.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
Pfam; PF05986; ADAM_spacer1; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 3.
PRINTS; PR01858; ADAMTS1.
SMART; SM00608; ACR; 1.
SMART; SM00209; TSP1; 3.
SUPFAM; SSF82895; SSF82895; 3.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50092; TSP1; 3.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Complete proteome;
Disulfide bond; Extracellular matrix; Glycoprotein; Heparin-binding;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 54 {ECO:0000255}.
PROPEP 55 252 {ECO:0000250}.
/FTId=PRO_0000029154.
CHAIN 253 967 A disintegrin and metalloproteinase with
thrombospondin motifs 1.
/FTId=PRO_0000029155.
DOMAIN 258 467 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 476 558 Disintegrin.
DOMAIN 559 614 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 854 910 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 911 967 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
REGION 725 857 Spacer.
MOTIF 203 210 Cysteine switch. {ECO:0000250}.
COMPBIAS 194 198 Poly-Arg.
COMPBIAS 616 724 Cys-rich.
ACT_SITE 402 402 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 205 205 Zinc; in inhibited form. {ECO:0000250}.
METAL 261 261 Calcium 1.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 261 261 Calcium 2.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 344 344 Calcium 1.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 344 344 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 351 351 Calcium 1.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 401 401 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 405 405 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 411 411 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 462 462 Calcium 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 465 465 Calcium 1.
{ECO:0000250|UniProtKB:Q9UHI8}.
METAL 465 465 Calcium 2.
{ECO:0000250|UniProtKB:Q9UHI8}.
CARBOHYD 547 547 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 764 764 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 945 945 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 333 385 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 362 367 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 379 462 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 417 446 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 488 511 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 499 521 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 506 540 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 534 545 {ECO:0000250|UniProtKB:Q9UHI8}.
DISULFID 571 608 {ECO:0000250}.
DISULFID 575 613 {ECO:0000250}.
DISULFID 586 598 {ECO:0000250}.
CONFLICT 21 21 I -> V (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 26 31 KFRSSQ -> RSRGSL (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 49 49 V -> A (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 72 72 R -> P (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 79 79 L -> TR (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 249 249 R -> G (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 262 265 TMLV -> NLLK (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 607 607 S -> F (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 936 936 L -> V (in Ref. 2; AAG29823).
{ECO:0000305}.
CONFLICT 962 962 I -> T (in Ref. 2; AAG29823).
{ECO:0000305}.
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


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