ID ATS7_MOUSE Reviewed; 1657 AA.
AC Q68SA9; B2RUI8; E9QMY0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 24-JAN-2024, entry version 139.
DE RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 7;
DE Short=ADAM-TS 7;
DE Short=ADAM-TS7;
DE Short=ADAMTS-7;
DE EC=3.4.24.-;
DE AltName: Full=COMPase;
DE Flags: Precursor;
GN Name=Adamts7;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 61-66 AND
RP 221-226, FUNCTION, GLYCOSYLATION, PROTEOLYTIC PROCESSING, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo;
RX PubMed=15192113; DOI=10.1074/jbc.m402380200;
RA Somerville R.P.T., Longpre J.-M., Apel E.D., Lewis R.M., Wang L.W.,
RA Sanes J.R., Leduc R., Apte S.S.;
RT "ADAMTS7B, the full-length product of the ADAMTS7 gene, is a chondroitin
RT sulfate proteoglycan containing a mucin domain.";
RL J. Biol. Chem. 279:35159-35175(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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Metalloprotease that may play a role in the degradation of
CC COMP. {ECO:0000269|PubMed:15192113}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with COMP. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:15192113}. Note=Also found associated with
CC the external cell surface.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q68SA9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q68SA9-2; Sequence=VSP_035113;
CC -!- DOMAIN: The spacer domain and the TSP type-1 domains are important for
CC a tight interaction with the extracellular matrix. {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC -!- PTM: May be cleaved by a furin endopeptidase (By similarity). The
CC precursor is sequentially processed. {ECO:0000250,
CC ECO:0000269|PubMed:15192113}.
CC -!- PTM: N-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. N- and C-
CC glycosylations can also facilitate secretion (By similarity). O-
CC glycosylated proteoglycan. Contains chondroitin sulfate. {ECO:0000250,
CC ECO:0000269|PubMed:15192113}.
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DR EMBL; AY551090; AAT36307.1; -; mRNA.
DR EMBL; AC140392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC151735; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC141173; AAI41174.1; -; mRNA.
DR CCDS; CCDS40724.1; -. [Q68SA9-2]
DR CCDS; CCDS85708.1; -. [Q68SA9-1]
DR RefSeq; NP_001313280.1; NM_001326351.1. [Q68SA9-1]
DR AlphaFoldDB; Q68SA9; -.
DR SMR; Q68SA9; -.
DR BioGRID; 223868; 2.
DR IntAct; Q68SA9; 1.
DR STRING; 10090.ENSMUSP00000108682; -.
DR MEROPS; M12.231; -.
DR GlyCosmos; Q68SA9; 2 sites, No reported glycans.
DR GlyGen; Q68SA9; 2 sites.
DR iPTMnet; Q68SA9; -.
DR PhosphoSitePlus; Q68SA9; -.
DR PaxDb; 10090-ENSMUSP00000108682; -.
DR Antibodypedia; 27710; 199 antibodies from 21 providers.
DR DNASU; 108153; -.
DR Ensembl; ENSMUST00000113059.8; ENSMUSP00000108682.2; ENSMUSG00000032363.16. [Q68SA9-1]
DR Ensembl; ENSMUST00000113060.3; ENSMUSP00000108683.2; ENSMUSG00000032363.16. [Q68SA9-2]
DR GeneID; 108153; -.
DR KEGG; mmu:108153; -.
DR UCSC; uc009raa.1; mouse. [Q68SA9-1]
DR UCSC; uc009rab.1; mouse. [Q68SA9-2]
DR AGR; MGI:1347346; -.
DR CTD; 11173; -.
DR MGI; MGI:1347346; Adamts7.
DR VEuPathDB; HostDB:ENSMUSG00000032363; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159819; -.
DR InParanoid; Q68SA9; -.
DR OMA; YCSERQA; -.
DR OrthoDB; 2910701at2759; -.
DR PhylomeDB; Q68SA9; -.
DR TreeFam; TF313537; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 108153; 0 hits in 63 CRISPR screens.
DR ChiTaRS; Adamts7; mouse.
DR PRO; PR:Q68SA9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q68SA9; Protein.
DR Bgee; ENSMUSG00000032363; Expressed in ectoplacental cone and 115 other cell types or tissues.
DR ExpressionAtlas; Q68SA9; baseline and differential.
DR Genevisible; Q68SA9; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; ISO:MGI.
DR GO; GO:0008237; F:metallopeptidase activity; IDA:MGI.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:MGI.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IGI:MGI.
DR GO; GO:0030199; P:collagen fibril organization; IGI:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:MGI.
DR GO; GO:0001503; P:ossification; IGI:MGI.
DR GO; GO:0043931; P:ossification involved in bone maturation; IGI:MGI.
DR GO; GO:0006029; P:proteoglycan metabolic process; IGI:MGI.
DR GO; GO:0006508; P:proteolysis; IDA:MGI.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:MGI.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 8.
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; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF142; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 7; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 7.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 8.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 6.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Proteoglycan; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..220
FT /evidence="ECO:0000269|PubMed:15192113"
FT /id="PRO_0000348234"
FT CHAIN 221..1657
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 7"
FT /id="PRO_0000348235"
FT DOMAIN 226..437
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 447..522
FT /note="Disintegrin"
FT DOMAIN 523..578
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 804..863
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 864..923
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 925..978
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1366..1414
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1417..1477
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1479..1522
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1524..1584
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1587..1627
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 165..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..794
FT /note="Spacer"
FT REGION 1009..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1283..1304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 192..199
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 178..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1109..1127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1323..1363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 373
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 194
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 372
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CARBOHYD 84
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 622
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 302..356
FT /evidence="ECO:0000250"
FT DISULFID 331..338
FT /evidence="ECO:0000250"
FT DISULFID 350..432
FT /evidence="ECO:0000250"
FT DISULFID 389..416
FT /evidence="ECO:0000250"
FT DISULFID 459..482
FT /evidence="ECO:0000250"
FT DISULFID 470..488
FT /evidence="ECO:0000250"
FT DISULFID 477..507
FT /evidence="ECO:0000250"
FT DISULFID 501..512
FT /evidence="ECO:0000250"
FT DISULFID 535..572
FT /evidence="ECO:0000250"
FT DISULFID 539..577
FT /evidence="ECO:0000250"
FT DISULFID 550..562
FT /evidence="ECO:0000250"
FT VAR_SEQ 936..977
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035113"
FT CONFLICT 600
FT /note="K -> N (in Ref. 1; AAT36307)"
FT /evidence="ECO:0000305"
FT CONFLICT 1124
FT /note="G -> V (in Ref. 1; AAT36307 and 3; AAI41174)"
FT /evidence="ECO:0000305"
FT CONFLICT 1244
FT /note="A -> V (in Ref. 1; AAT36307 and 3; AAI41174)"
FT /evidence="ECO:0000305"
FT CONFLICT 1312..1333
FT /note="GTLLLTVPTDLRSPGPSGQPQT -> VAGPMV (in Ref. 1;
FT AAT36307)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1657 AA; 182313 MW; 2B05A3B6567617FD CRC64;
MHRGPSLLLI LCALASRVLG PASGLVTEGR AGLDIVHPVR VDAGGSFLSY ELWPRVLRKR
DVSTTQASSA FYQLQYQGRE LLFNLTTNPY LMAPGFVSEI RRHSTLGHAH IQTSVPTCHL
LGDVQDPELE GGFAAISACD GLRGVFQLSN EDYFIEPLDG VSAQPGHAQP HVVYKHQGSR
KQAQQGDSRP SGTCGMQVPP DLEQQREHWE QQQQKRRQQR SVSKEKWVET LVVADSKMVE
YHGQPQVESY VLTIMNMVAG LFHDPSIGNP IHISIVRLII LEDEEKDLKI THHAEETLKN
FCRWQKNINI KGDDHPQHHD TAILLTRKDL CASMNQPCET LGLSHVSGLC HPQLSCSVSE
DTGMPLAFTV AHELGHSFGI QHDGTGNDCE SIGKRPFIMS PQLLYDRGIP LTWSRCSREY
ITRFLDRGWG LCLDDRPSKD VIALPSVLPG VLYDVNHQCR LQYGSHSAYC EDMDDVCHTL
WCSVGTTCHS KLDAAVDGTS CGKNKWCLKG ECVPEGFQPE AVDGGWSGWS AWSDCSRSCG
VGVRSSERQC TQPVPKNRGK YCVGERKRSQ LCNLPACPPD RPSFRHTQCS QFDGMLYKGK
LHKWVPVPND DNPCELHCRP SNSSNTEKLR DAVVDGTPCY QSRISRDICL NGICKNVGCD
FVIDSGAEED RCGVCRGDGS TCQTVSRTFK ETEGQGYVDI GLIPAGAREI LIEEVAEAAN
FLALRSEDPD KYFLNGGWTI QWNGDYRVAG TTFTYARKGN WENLTSPGPT SEPVWIQLLF
QEKNPGVHYQ YTIQRDSHDQ VRPPEFSWHY GPWSKCTVTC GTGVQRQSLY CMERQAGVVA
EEYCNTLNRP DERQRKCSEE PCPPRWWAGE WQPCSRSCGP EGLSRRAVFC IRSMGLDEQR
ALELSACEHL PRPLAETPCN RHVICPSTWG VGNWSQCSVT CGAGIRQRSV LCINNTDVPC
DEAERPITET FCFLQPCQYP MYIVDTGASG SGSSSPELFN EVDFIPNQLA PRPSPASSPK
PVSISNAIDE EELDPPGPVF VDDFYYDYNF INFHEDLSYG SFEEPHPDLV DNGGWTAPPH
IRPTESPSDT PVPTAGALGA EAEDIQGSWS PSPLLSEASY SPPGLEQTSI NPLANFLTEE
DTPMGAPELG FPSLPWPPAS VDDMMTPVGP GNPDELLVKE DEQSPPSTPW SDRNKLSTDG
NPLGHTSPAL PQSPIPTQPS PPSISPTQAS PSPDVVEVST GWNAAWDPVL EADLKPGHGE
LPSTVEVASP PLLPMATVPG IWGRDSPLEP GTPTFSSPEL SSQHLKTLTM PGTLLLTVPT
DLRSPGPSGQ PQTPNLEGTQ SPGLLPTPAR ETQTNSSKDP EVQPLQPSLE EDGDPADPLP
ARNASWQVGN WSQCSTTCGL GAIWRLVSCS SGNDEDCTLA SRPQPARHCH LRPCAAWRTG
NWSKCSRNCG GGSSTRDVQC VDTRDLRPLR PFHCQPGPTK PPNRQLCGTQ PCLPWYTSSW
RECSEACGGG EQQRLVTCPE PGLCEESLRP NNSRPCNTHP CTQWVVGPWG QCSAPCGGGV
QRRLVRCVNT QTGLAEEDSD LCSHEAWPES SRPCATEDCE LVEPPRCERD RLSFNFCETL
RLLGRCQLPT IRAQCCRSCP PLSRGVPSRG HQRVARR
//
