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Database: UniProt
Entry: D3Z1A5_MOUSE
LinkDB: D3Z1A5_MOUSE
Original site: D3Z1A5_MOUSE 
ID   D3Z1A5_MOUSE            Unreviewed;      1117 AA.
AC   D3Z1A5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   SubName: Full=A disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 6 {ECO:0000313|Ensembl:ENSMUSP00000064570.7};
GN   Name=Adamts6 {ECO:0000313|Ensembl:ENSMUSP00000064570.7,
GN   ECO:0000313|MGI:MGI:1347348};
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 {ECO:0000313|Ensembl:ENSMUSP00000064570.7, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000064570.7, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000064570.7,
RC   ECO:0000313|Proteomes:UP000000589};
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   [2] {ECO:0000313|Ensembl:ENSMUSP00000064570.7}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000064570.7};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000256|ARBA:ARBA00004498}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR   RefSeq; NP_001074489.1; NM_001081020.2.
DR   RefSeq; XP_011242913.1; XM_011244611.2.
DR   SMR; D3Z1A5; -.
DR   STRING; 10090.ENSMUSP00000153359; -.
DR   MEROPS; M12.248; -.
DR   PhosphoSitePlus; D3Z1A5; -.
DR   PaxDb; 10090-ENSMUSP00000064570; -.
DR   Antibodypedia; 11532; 79 antibodies from 17 providers.
DR   DNASU; 108154; -.
DR   Ensembl; ENSMUST00000065766.7; ENSMUSP00000064570.7; ENSMUSG00000046169.11.
DR   Ensembl; ENSMUST00000224208.2; ENSMUSP00000153359.2; ENSMUSG00000046169.11.
DR   GeneID; 108154; -.
DR   KEGG; mmu:108154; -.
DR   UCSC; uc007rti.1; mouse.
DR   AGR; MGI:1347348; -.
DR   CTD; 11174; -.
DR   MGI; MGI:1347348; Adamts6.
DR   VEuPathDB; HostDB:ENSMUSG00000046169; -.
DR   eggNOG; KOG3538; Eukaryota.
DR   eggNOG; KOG4597; Eukaryota.
DR   GeneTree; ENSGT00940000156571; -.
DR   HOGENOM; CLU_000660_1_1_1; -.
DR   OMA; GPEWRHD; -.
DR   OrthoDB; 2910701at2759; -.
DR   TreeFam; TF313537; -.
DR   Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR   BioGRID-ORCS; 108154; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Adamts6; mouse.
DR   Proteomes; UP000000589; Chromosome 13.
DR   Bgee; ENSMUSG00000046169; Expressed in manus and 104 other cell types or tissues.
DR   ExpressionAtlas; D3Z1A5; baseline and differential.
DR   Genevisible; D3Z1A5; MM.
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; IBA:GO_Central.
DR   GO; GO:0035904; P:aorta development; IMP:MGI.
DR   GO; GO:0003279; P:cardiac septum development; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0001822; P:kidney development; IMP:MGI.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 5.
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:SF27; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 6; 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; PF08686; PLAC; 1.
DR   Pfam; PF01421; Reprolysin; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   4: Predicted;
KW   Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3};
KW   Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR613273-2};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1117
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015088517"
FT   DOMAIN          250..468
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          1079..1117
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   ACT_SITE        404
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /note="in inhibited form"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         253
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         351
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   BINDING         403
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         407
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         413
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT                   ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         463
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT   DISULFID        326..387
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        362..369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        381..463
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        420..447
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        490..512
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        501..519
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        507..542
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        532..547
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        570..607
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        574..612
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        585..597
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   1117 AA;  125059 MW;  00B3271CD1D84EB5 CRC64;
     MEISWKTLTW ILSLIMASSE FYSDHRLSYS SQEEFLTYLE HYQLTIPIRV DQNGAFLSFT
     VKNDKHSRRR RSMDLLDPQQ AVSKLFFKLS AYGKHFHLNL TLNTNFVSKH FTVEYWGKDG
     PQWKHDFLDN CHYTGYLQDQ HSTTKVALSN CVGLHGIIAT EDEEYFIEPL KNTTEDSKHF
     SYENGHPHVI YKKSTLQQQH IYDHSHCGVS DLTGSGKPWW LNKTSSFPSL PPINDTHIHH
     RKRRSVSTER FVETLVVADK MMVGYHGRKD IEHYILSVMN IVAKLYRDSS LGNVVNIIVA
     RLIVLTEDQP NLEINHHADK SLDSFCKWQK SILSHQSDGN TIPENGIAHH DNAVLITRYD
     ICTYKNKPCG TLGLASVAGM CEPERSCSIN EDIGLGSAFT IAHEIGHNFG MNHDGIGNSC
     GTKGHEAAKL MAAHITANTN PFSWSACSRD YITSFLDSGR GTCLDNEPPK RDFLYPAVAP
     GQVYDADEQC RFQYGATSRQ CKYGEVCREL WCLSKSNRCV TNSIPAAEGT LCQTGNIEKG
     WCYQGDCVPF GTWPQSIDGG WGSWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE
     RKRYRSCNTD PCPLGSRDFR EKQCADFDSM PFRGKHYNWK PYTGGGVKPC ALNCLAEGYN
     FYTERAPAVI DGTQCNADSL DICINGECKH VGCDNILGSD AREDRCRVCG GDGSTCDAIE
     GFFNDSLPRG GYMEVVQIPR GSVHIEVREV SMSKNYIALK SEGDDYYING AWTIDWPRKF
     DVSGTAFHYK RPTDEPESLE ALGPTSENLI VMVLLQEQNL GIRYKFNVPI VRTGSGDNEV
     GFMWTYQPWA ECSATCAGGV QRQEVVCKRL DDNSIVQNNF CDPDSKPPEN QRACNTEPCP
     PEWFIGDWLE CSKTCDGGMR TRAVLCIRKV GPSEEETLDY GDCLTHRPVE KESCNNQSCP
     PQWVALDWSE CTPKCGSGFK HRIVLCKSSD LSKTFPAAQC PEESKPPARI RCSLGRCPPP
     RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG QASVDCPETV RPPSMQQCDS KCDSTPLSST
     EECKDVNKVA YCPLVLKFKF CSRAYFRQMC CKTCQGH
//
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