ATS7_RAT
ID ATS7_RAT Reviewed; 1595 AA.
AC Q1EHB3; Q1XD63;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 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] (ISOFORMS 1 AND 2), INTERACTION WITH COMP, AND
RP TISSUE SPECIFICITY.
RC STRAIN=Brown Norway; TISSUE=Brain;
RX PubMed=16585064; DOI=10.1096/fj.05-3877fje;
RA Liu C.-J., Kong W., Ilalov K., Yu S., Xu K., Prazak L., Fajardo M.,
RA Sehgal B., Di Cesare P.E.;
RT "ADAMTS-7: a metalloproteinase that directly binds to and degrades
RT cartilage oligomeric matrix protein.";
RL FASEB J. 20:988-990(2006).
CC -!- FUNCTION: Metalloprotease that may play a role in the degradation of
CC COMP. {ECO:0000250}.
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:0000269|PubMed:16585064}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Note=Also found associated with the external cell
CC surface. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q1EHB3-1; Sequence=Displayed;
CC Name=2; Synonyms=ADAMTS7B;
CC IsoId=Q1EHB3-2; Sequence=VSP_035114;
CC -!- TISSUE SPECIFICITY: Detected in liver, ovary, kidney, testicle, lung
CC and embryo. {ECO:0000269|PubMed:16585064}.
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: Glycosylated (By similarity). Can be 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 ADAMTS family members.
CC Can also be C-glycosylated with one or two mannose molecules on
CC tryptophan residues within the consensus sequence W-X-X-W of the TPRs.
CC N- and C-glycosylations can also facilitate secretion. O-glycosylated
CC proteoglycan. Contains chondroitin sulfate (By similarity).
CC {ECO:0000250}.
CC -!- PTM: May be cleaved by a furin endopeptidase. The precursor is
CC sequentially processed (By similarity). {ECO:0000250}.
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DR EMBL; AY327121; AAQ94615.1; -; mRNA.
DR EMBL; AY257482; AAP79641.1; -; mRNA.
DR RefSeq; NP_001040566.1; NM_001047101.1. [Q1EHB3-2]
DR RefSeq; XP_006243587.1; XM_006243525.1. [Q1EHB3-1]
DR AlphaFoldDB; Q1EHB3; -.
DR SMR; Q1EHB3; -.
DR STRING; 10116.ENSRNOP00000060069; -.
DR MEROPS; M12.231; -.
DR GlyGen; Q1EHB3; 3 sites.
DR iPTMnet; Q1EHB3; -.
DR PhosphoSitePlus; Q1EHB3; -.
DR PaxDb; Q1EHB3; -.
DR PRIDE; Q1EHB3; -.
DR Ensembl; ENSRNOT00000068394; ENSRNOP00000060069; ENSRNOG00000028036. [Q1EHB3-2]
DR GeneID; 315879; -.
DR KEGG; rno:315879; -.
DR UCSC; RGD:1306713; rat. [Q1EHB3-1]
DR CTD; 11173; -.
DR RGD; 1306713; Adamts7.
DR VEuPathDB; HostDB:ENSRNOG00000028036; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159819; -.
DR HOGENOM; CLU_000660_2_1_1; -.
DR InParanoid; Q1EHB3; -.
DR OMA; VDEGHCD; -.
DR OrthoDB; 125522at2759; -.
DR TreeFam; TF313537; -.
DR Reactome; R-RNO-5173214; O-glycosylation of TSR domain-containing proteins.
DR PRO; PR:Q1EHB3; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000028036; Expressed in heart and 16 other tissues.
DR ExpressionAtlas; Q1EHB3; baseline and differential.
DR Genevisible; Q1EHB3; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
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:RGD.
DR GO; GO:0008237; F:metallopeptidase activity; ISO:RGD.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISO:RGD.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISO:RGD.
DR GO; GO:0030199; P:collagen fibril organization; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0043931; P:ossification involved in bone maturation; ISO:RGD.
DR GO; GO:0006029; P:proteoglycan metabolic process; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; ISO:RGD.
DR Gene3D; 2.20.100.10; -; 7.
DR Gene3D; 3.40.390.10; -; 1.
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 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; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 8.
DR SUPFAM; SSF82895; SSF82895; 8.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cleavage on pair of basic residues; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Proteoglycan; Reference proteome; Repeat;
KW Secreted; Signal; Zinc.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..217
FT /evidence="ECO:0000250"
FT /id="PRO_0000348236"
FT CHAIN 218..1595
FT /note="A disintegrin and metalloproteinase with
FT thrombospondin motifs 7"
FT /id="PRO_0000348237"
FT DOMAIN 223..434
FT /note="Peptidase M12B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276"
FT DOMAIN 444..519
FT /note="Disintegrin"
FT DOMAIN 520..575
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 801..860
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 861..917
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 922..975
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1320..1368
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1371..1431
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1433..1476
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1478..1538
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1541..1581
FT /note="PLAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00233"
FT REGION 165..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..791
FT /note="Spacer"
FT REGION 989..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1077..1121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 189..196
FT /note="Cysteine switch"
FT /evidence="ECO:0000250"
FT COMPBIAS 198..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1219..1234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1267..1301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 370
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00276,
FT ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 191
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 369
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 379
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 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 619
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 299..353
FT /evidence="ECO:0000250"
FT DISULFID 328..335
FT /evidence="ECO:0000250"
FT DISULFID 347..429
FT /evidence="ECO:0000250"
FT DISULFID 386..413
FT /evidence="ECO:0000250"
FT DISULFID 456..479
FT /evidence="ECO:0000250"
FT DISULFID 467..485
FT /evidence="ECO:0000250"
FT DISULFID 474..504
FT /evidence="ECO:0000250"
FT DISULFID 498..509
FT /evidence="ECO:0000250"
FT DISULFID 532..569
FT /evidence="ECO:0000250"
FT DISULFID 536..574
FT /evidence="ECO:0000250"
FT DISULFID 547..559
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="MHRGLNLLLILCALAPHVLGPASG -> MAEEDIGTESFGEEGERGPQSPDE
FT IIFQQCKMFALHIQRKRKQLGASFWHLCTGRCSGRWGSLSCSCHCQRCQRWREREDGTR
FT RSQGQREKKDDKGLEKPKRKVQKGKQMQKASGDKESENSISRKKPLPSLEGPRPLSWVD
FT FGHKSRSPPRRSCLLSVPSRSLAGFQVSFSEGQAFFAWDPETSETQIGDKKLQNSRSFG
FT GTSEGTDGLGLLHRQGTSVALQAVQSLSCRVGTVLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16585064"
FT /id="VSP_035114"
SQ SEQUENCE 1595 AA; 175814 MW; 4025D80EBFCF0C4C CRC64;
MHRGLNLLLI LCALAPHVLG PASGLPTEGR AGLDIVHPVR VDAGGSFLSY ELWPRVLRKR
DVSAAQASSA FYQLQYQGRE LLFNLTTNPY LLAPGFVSEI RRRSNLSNVH IQTSVPTCHL
LGDVQDPELE GGFAAISACD GLRGVFQLSN EDYFIEPLDE VPAQPGHAQP HMVYKHKRSG
QQDDSRTSGT CGVQGSPELK HQREHWEQRQ QKRRQQRSIS KEKWVETLVV ADSKMVEYHG
QPQVESYVLT IMNMVAGLYH DPSIGNPIHI TVVRLIILED EEKDLKITHH ADDTLKNFCR
WQKNVNMKGD DHPQHHDTAI LLTRKDLCAT MNHPCETLGL SHVAGLCHPQ LSCSVSEDTG
LPLAFTVAHE LGHSFGIQHD GTGNDCESIG KRPFIMSPQL LYDRGIPLTW SRCSREYITR
FLDRGWGLCL DDRPSKGVIN FPSVLPGVLY DVNHQCRLQY GPSSAYCEDV DNVCYTLWCS
VGTTCHSKMD AAVDGTSCGK NKWCLNGECV PEGFQPETVD GGWSGWSAWS VCSRSCGVGV
RSSERQCTQP VPKNKGKYCV GERKRYRLCN LQACPPDRPS FRHTQCSQFD SMLYKGKLHK
WVPVLNDENP CELHCRPFNY SNREKLRDAV MDGTPCYQGR ISRDICIDGI CKKVGCDFEL
DSGAEEDRCG VCRGDGSTCH TVSRTFKEAE GMGYVDVGLI PAGAREILIE EVAEAANFLA
LRSEDPDKYF LNGGWTIQWN GDYQVAGTTF TYTRKGNWET LTSPGPTTEP VWIQLLFQER
NPGVHYKYTI QRASHSEAQP PEFSWHYGPW SKCPVTCGTG VQRQSLYCME KQAGIVDEGH
CDHLSRPRDR KRKCNEEPCP ARWWVGDWQP CSRSCGPGGF FRRAVFCTRS VGLDEQRALE
PSACGHLPRP LAEIPCYHYV ACPSSWGVGN WSQCSVTCGA GIRQRSVLCI NNTGVPCDGA
ERPITETFCF LQPCQYSTYI VDTGASGSGS SSPELFNEVD FDPHQPVPRP SPASSPKPVS
ISNAIDEEDP ELDPPGPVFV DDFYYDYNFI NFHEDLSYGS FEESHSDLVD IGGQTVPPHI
RPTEPPSDSP VPTAGAPGAE EEGIQGSWSP SPLLSEASHS PPVLLENTPV NPLANFLTEE
ESPIGAPELG LPSVSWPPAS VDGMVTSVAP GNPDELLVRE DTQSQPSTPW SDRNKLSKDG
NPLGPTSPAL PKSPFPTQPS SPSNSTTQAS LSPDAVEVST GWNVALDPVL EADLKPVHAP
TDPGLLDQIQ TPHTEGTQSP GLLPRPAQET QTNSSKDPAV QPLQPSLVED GAPTDLLPAK
NASWQVGNWS QCSTTCGLGA IWRLVRCSSG NDEDCTLSSR PQPARHCHLR PCAAWRAGNW
SKCSRNCGGG SATRDVQCVD TRDLRPLRPF HCQPGPTKPP TRQLCGTQPC LPWYTSSWRE
CSEACGGGEQ QRLVTCPEPG LCEESLRPNN TRPCNTHPCT QWVVGPWGQC SAPCGGGVQR
RLVKCVNTQT GLAEEDSDLC SHEAWPESSR PCATEDCELV EPSRCERDRL PFNFCETLRL
LGRCQLPTIR AQCCRSCPPL SRGVPSRGHQ RVARR
