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
//