ID E1BK03_BOVIN Unreviewed; 1117 AA.
AC E1BK03;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 6 {ECO:0000313|Ensembl:ENSBTAP00000053837.2};
GN Name=ADAMTS6 {ECO:0000313|Ensembl:ENSBTAP00000053837.2,
GN ECO:0000313|VGNC:VGNC:25628};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000053837.2, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000053837.2, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053837.2,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000053837.2}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000053837.2};
RG Ensembl;
RL Submitted (NOV-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_001179945.1; NM_001193016.1.
DR RefSeq; XP_010815027.1; XM_010816725.2.
DR AlphaFoldDB; E1BK03; -.
DR SMR; E1BK03; -.
DR STRING; 9913.ENSBTAP00000053837; -.
DR MEROPS; M12.248; -.
DR PaxDb; 9913-ENSBTAP00000053837; -.
DR Ensembl; ENSBTAT00000061189.3; ENSBTAP00000053837.2; ENSBTAG00000016963.7.
DR GeneID; 540722; -.
DR KEGG; bta:540722; -.
DR CTD; 11174; -.
DR VEuPathDB; HostDB:ENSBTAG00000016963; -.
DR VGNC; VGNC:25628; ADAMTS6.
DR eggNOG; KOG3538; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156571; -.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; E1BK03; -.
DR OMA; GPEWRHD; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF313537; -.
DR Reactome; R-BTA-5173214; O-glycosylation of TSR domain-containing proteins.
DR Proteomes; UP000009136; Chromosome 20.
DR Bgee; ENSBTAG00000016963; Expressed in oviduct epithelium and 89 other cell types or tissues.
DR ExpressionAtlas; E1BK03; baseline and differential.
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; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
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:UP000009136};
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_5003144078"
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; 125208 MW; 7CC576918B190548 CRC64;
MEILWKTFTW ILSLIMASSE FHSDYRLSYS SQEEFLTYLE HYQLTIPIRV DQNGAFLSFT
VKNDKHSRRR RSMDPIDPQQ AVSKLFFKLS AYGKHFHLNL TLNTDFVSKH FTVEYWGKDG
PQWKHDFLDN CHYTGYLQDQ RSTTKVALSN CVGLHGVIAT EDEEYFIEPL KNTTEDSKHF
SYENGHPHVI YKKSTLQQRH LYDHSHCGVS DLLRSGKPWW LNDTSAFPSS LPINGTHIHQ
RQKRSVSIER 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 WGPWSLWGEC SRTCGGGVSS SLRHCDSPAP SGGGKYCLGE
RKRYRSCNTD PCPLGARDFR EKQCADFDNM PFRGKYYNWK PYTGGGVKPC ALNCLAEGYN
FYTERSPAVI DGTQCNADSL DICINGECKH VGCDNILGSD AREDRCRVCG GDGSTCDAIE
GFFNDSLPRG GYMEVVQIPR GSVHIEVKEV AMSKNYIALK SEGDDYYING AWTIDWPRKF
DVAGTAFHYK RPTDEPESLE ALGPTSENLI VMVLLQEQNL GIRYKFNVPI TRTGSGDNEV
GFTWNHQPWS ECSATCAGGV QRQEVVCKRL DDNSIVQNNY CDPDSKPPEN QRTCNTEPCP
PEWFIGDWLE CSKTCDGGMR TRAVLCIRKI GPSEEETLDY SGCLTHRPIE KEPCNNQSCP
PQWVALDWSE CTPKCGPGFK HRIVLCKSSD LSKTFPATQC SEESKPPVRI RCSLGRCPPP
RWVTGDWGQC SAQCGLGQQM RTVQCLSYTG QASSDCPETS RPPSMQQCES KCDSTPISST
EECKDVNKVA YCPLVLKFKF CSRAYFRQMC CKTCQGH
//
