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ATS7_MOUSE
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   03-AUG-2022, entry version 131.
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   GlyGen; Q68SA9; 2 sites.
DR   iPTMnet; Q68SA9; -.
DR   PhosphoSitePlus; Q68SA9; -.
DR   PaxDb; Q68SA9; -.
DR   PRIDE; Q68SA9; -.
DR   Antibodypedia; 27710; 187 antibodies from 21 providers.
DR   DNASU; 108153; -.
DR   Ensembl; ENSMUST00000113059; ENSMUSP00000108682; ENSMUSG00000032363. [Q68SA9-1]
DR   Ensembl; ENSMUST00000113060; ENSMUSP00000108683; ENSMUSG00000032363. [Q68SA9-2]
DR   GeneID; 108153; -.
DR   KEGG; mmu:108153; -.
DR   UCSC; uc009raa.1; mouse. [Q68SA9-1]
DR   UCSC; uc009rab.1; mouse. [Q68SA9-2]
DR   CTD; 11173; -.
DR   MGI; MGI:1347346; Adamts7.
DR   VEuPathDB; HostDB:ENSMUSG00000032363; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   GeneTree; ENSGT00940000159819; -.
DR   InParanoid; Q68SA9; -.
DR   OMA; VDEGHCD; -.
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 60 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 113 other 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   Gene3D; 2.20.100.10; -; 8.
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; 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; SM00608; ACR; 1.
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; 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
 
 
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