ATS1_MOUSE
ID ATS1_MOUSE Reviewed; 968 AA.
AC P97857; E9QMN9; O54768;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 186.
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 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 [GENOMIC DNA].
RC STRAIN=129/SvJ;
RX PubMed=9441751; DOI=10.1006/geno.1997.5064;
RA Kuno K., Lizasa H., Ohno S., Matsushima K.;
RT "The exon/intron organization and chromosomal mapping of the mouse ADAMTS-1
RT gene encoding an ADAM family protein with TSP motifs.";
RL Genomics 46:466-471(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8995297; DOI=10.1074/jbc.272.1.556;
RA Kuno K., Kanada N., Nakashima E., Fujiki F., Ichimura F., Matsushima K.;
RT "Molecular cloning of a gene encoding a new type of metalloproteinase-
RT disintegrin family protein with thrombospondin motifs as an inflammation
RT associated gene.";
RL J. Biol. Chem. 272:556-562(1997).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Limb, and Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP CHARACTERIZATION, AND MUTAGENESIS OF GLU-403.
RX PubMed=10373500; DOI=10.1074/jbc.274.26.18821;
RA Kuno K., Terashima Y., Matsushima K.;
RT "ADAMTS-1 is an active metalloproteinase associated with the extracellular
RT matrix.";
RL J. Biol. Chem. 274:18821-18826(1999).
RN [6]
RP FUNCTION.
RX PubMed=10930576; DOI=10.1016/s0014-5793(00)01854-8;
RA Kuno K., Okada Y., Kawashima H., Nakamura H., Miyasaka M., Ohno H.,
RA Matsushima K.;
RT "ADAMTS-1 cleaves a cartilage proteoglycan, aggrecan.";
RL FEBS Lett. 478:241-245(2000).
RN [7]
RP FUNCTION, AND INDUCTION.
RX PubMed=10781075; DOI=10.1073/pnas.080073497;
RA Robker R.L., Russell D.L., Espey L.L., Lydon J.P., O'Malley B.W.,
RA Richards J.S.;
RT "Progesterone-regulated genes in the ovulation process: ADAMTS-1 and
RT cathepsin L proteases.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:4689-4694(2000).
RN [8]
RP DEVELOPMENTAL STAGE.
RX PubMed=23233679; DOI=10.1074/jbc.m112.429647;
RA Stupka N., Kintakas C., White J.D., Fraser F.W., Hanciu M.,
RA Aramaki-Hattori N., Martin S., Coles C., Collier F., Ward A.C., Apte S.S.,
RA McCulloch D.R.;
RT "Versican processing by a disintegrin-like and metalloproteinase domain
RT with thrombospondin-1 repeats proteinases-5 and -15 facilitates myoblast
RT fusion.";
RL J. Biol. Chem. 288:1907-1917(2013).
CC -!- FUNCTION: Cleaves aggrecan, a cartilage proteoglycan, at the '1691-
CC Glu-|-Leu-1692' 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, ECO:0000269|PubMed:10781075,
CC ECO:0000269|PubMed:10930576}.
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.
CC -!- DEVELOPMENTAL STAGE: In embryonic skeletal muscle, significantly
CC increased levels between 13.5 dpc and 15.5 dpc with maximal expression
CC observed at 15.5 dpc (PubMed:23233679). Decreased levels in postnatal
CC skeletal muscle (PubMed:23233679). In myoblasts, up-regulated soon
CC after induction of myoblast differentiation (PubMed:23233679).
CC {ECO:0000269|PubMed:23233679}.
CC -!- INDUCTION: Induced in vitro in colon adenocarcinoma cells by
CC interleukin-1, or in vivo in kidney and heart by lipopolysaccharide.
CC Also induced by LH stimulation in granulosa cells of preovulatory
CC follicles. {ECO:0000269|PubMed:10781075}.
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.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA11088.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA24501.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB001735; BAA24501.1; ALT_INIT; Genomic_DNA.
DR EMBL; D67076; BAA11088.1; ALT_FRAME; mRNA.
DR EMBL; AC126936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040382; AAH40382.1; -; mRNA.
DR EMBL; BC050834; AAH50834.1; -; mRNA.
DR CCDS; CCDS28287.1; -.
DR PIR; T00017; T00017.
DR RefSeq; NP_033751.3; NM_009621.5.
DR AlphaFoldDB; P97857; -.
DR SMR; P97857; -.
DR BioGRID; 197974; 4.
DR STRING; 10090.ENSMUSP00000023610; -.
DR MEROPS; M12.222; -.
DR GlyGen; P97857; 5 sites.
DR iPTMnet; P97857; -.
DR PhosphoSitePlus; P97857; -.
DR CPTAC; non-CPTAC-3962; -.
DR MaxQB; P97857; -.
DR PaxDb; P97857; -.
DR PeptideAtlas; P97857; -.
DR PRIDE; P97857; -.
DR ProteomicsDB; 277135; -.
DR Antibodypedia; 4291; 419 antibodies from 33 providers.
DR DNASU; 11504; -.
DR Ensembl; ENSMUST00000023610; ENSMUSP00000023610; ENSMUSG00000022893.
DR GeneID; 11504; -.
DR KEGG; mmu:11504; -.
DR UCSC; uc012aho.1; mouse.
DR CTD; 9510; -.
DR MGI; MGI:109249; Adamts1.
DR VEuPathDB; HostDB:ENSMUSG00000022893; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156815; -.
DR HOGENOM; CLU_000660_3_0_1; -.
DR InParanoid; P97857; -.
DR OMA; KKHFDTP; -.
DR OrthoDB; 125522at2759; -.
DR PhylomeDB; P97857; -.
DR TreeFam; TF331949; -.
DR BRENDA; 3.4.24.B11; 3474.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 11504; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Adamts1; mouse.
DR PRO; PR:P97857; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P97857; protein.
DR Bgee; ENSMUSG00000022893; Expressed in iris and 263 other tissues.
DR ExpressionAtlas; P97857; baseline and differential.
DR Genevisible; P97857; MM.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060347; P:heart trabecula formation; IMP:MGI.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI.
DR GO; GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; ISO:MGI.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 1: Evidence at protein 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..48
FT /evidence="ECO:0000255"
FT PROPEP 49..253
FT /id="PRO_0000029152"
FT CHAIN 254..968
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 1"
FT /id="PRO_0000029153"
FT DOMAIN 259..468
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 477..559
FT /note="Disintegrin"
FT DOMAIN 560..615
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 855..911
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 912..968
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..850
FT /note="Spacer"
FT MOTIF 204..211
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 218..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 403
FT /evidence="ECO:0000269|PubMed:10373500"
FT BINDING 206
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 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 262
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 352
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 406
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 463
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT BINDING 466
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 765
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 946
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..386
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 363..368
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 380..463
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 418..447
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 489..512
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 500..522
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 507..541
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 535..546
FT /evidence="ECO:0000250|UniProtKB:Q9UHI8"
FT DISULFID 572..609
FT /evidence="ECO:0000250"
FT DISULFID 576..614
FT /evidence="ECO:0000250"
FT DISULFID 587..599
FT /evidence="ECO:0000250"
FT MUTAGEN 403
FT /note="E->Q: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10373500"
FT CONFLICT 335
FT /note="S -> N (in Ref. 1; BAA24501 and 4; AAH40382/
FT AAH50834)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="S -> T (in Ref. 1; BAA24501 and 4; AAH40382/
FT AAH50834)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 968 AA; 105801 MW; 90A44F7D5262B6C5 CRC64;
MQPKVPLGSR KQKPCSDMGD VQRAARSRGS LSAHMLLLLL ASITMLLCAR GAHGRPTEED
EELVLPSLER APGHDSTTTR LRLDAFGQQL HLKLQPDSGF LAPGFTLQTV GRSPGSEAQH
LDPTGDLAHC FYSGTVNGDP GSAAALSLCE GVRGAFYLQG EEFFIQPAPG VATERLAPAV
PEEESSARPQ FHILRRRRRG SGGAKCGVMD DETLPTSDSR PESQNTRNQW PVRDPTPQDA
GKPSGPGSIR KKRFVSSPRY VETMLVADQS MADFHGSGLK HYLLTLFSVA ARFYKHPSIR
NSISLVVVKI LVIYEEQKGP EVTSNAALTL RNFCSWQKQH NSPSDRDPEH YDTAILFTRQ
DLCGSHTCDT LGMADVGTVC DPSRSCSVIE DDGLQAAFTT AHELGHVFNM PHDDAKHCAS
LNGVSGDSHL MASMLSSLDH SQPWSPCSAY MVTSFLDNGH GECLMDKPQN PIKLPSDLPG
TLYDANRQCQ FTFGEESKHC PDAASTCTTL WCTGTSGGLL VCQTKHFPWA DGTSCGEGKW
CVSGKCVNKT DMKHFATPVH GSWGPWGPWG DCSRTCGGGV QYTMRECDNP VPKNGGKYCE
GKRVRYRSCN IEDCPDNNGK TFREEQCEAH NEFSKASFGN EPTVEWTPKY AGVSPKDRCK
LTCEAKGIGY FFVLQPKVVD GTPCSPDSTS VCVQGQCVKA GCDRIIDSKK KFDKCGVCGG
NGSTCKKMSG IVTSTRPGYH DIVTIPAGAT NIEVKHRNQR GSRNNGSFLA IRAADGTYIL
NGNFTLSTLE QDLTYKGTVL RYSGSSAALE RIRSFSPLKE PLTIQVLMVG HALRPKIKFT
YFMKKKTESF NAIPTFSEWV IEEWGECSKT CGSGWQRRVV QCRDINGHPA SECAKEVKPA
STRPCADLPC PHWQVGDWSP CSKTCGKGYK KRTLKCVSHD GGVLSNESCD PLKKPKHYID
FCTLTQCS
