ID I3KE45_ORENI Unreviewed; 1123 AA.
AC I3KE45;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 6 {ECO:0000313|Ensembl:ENSONIP00000019390.2};
GN Name=ADAMTS6 {ECO:0000313|Ensembl:ENSONIP00000019390.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000019390.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000019390.2}
RP IDENTIFICATION.
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; XP_003455202.1; XM_003455154.4.
DR RefSeq; XP_019216229.1; XM_019360684.1.
DR RefSeq; XP_019216230.1; XM_019360685.1.
DR RefSeq; XP_019216231.1; XM_019360686.1.
DR AlphaFoldDB; I3KE45; -.
DR STRING; 8128.ENSONIP00000019390; -.
DR Ensembl; ENSONIT00000019407.2; ENSONIP00000019390.2; ENSONIG00000015412.2.
DR GeneID; 100701133; -.
DR KEGG; onl:100701133; -.
DR CTD; 11174; -.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156571; -.
DR HOGENOM; CLU_000660_1_1_1; -.
DR InParanoid; I3KE45; -.
DR OMA; GPEWRHD; -.
DR OrthoDB; 2910701at2759; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000005207; Linkage group LG7.
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; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
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; 4.
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; 4.
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:UP000005207};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1123
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025599937"
FT DOMAIN 256..474
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1085..1123
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 410
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 409
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 419
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 469
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 332..393
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 368..375
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 387..469
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 426..453
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 496..518
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 507..525
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 513..548
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..553
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..613
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 580..618
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 591..603
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1123 AA; 125467 MW; 5B41C0D4EF3C7053 CRC64;
MEILWKTLTW TLSLVVMTAS EFQSFNKLSH NSQEEFLSYL QHYQLTVPVQ VDENGEFLSY
TVKHHRPGRR RRGAVDPMMG AQPALDPLEP RLFYRLSAYG KHFHLNLTLN PHLVSKHFTV
EYWGKEGLEW RHNMVDNCHY IGFLQNQHST TRVALSNCKG LHGVITTEEE QYLIEPLKNI
SSTTSGEWNL EEAQQHVIYK MSAIPSPQEH SQEFSCGISD LIKTSAPCQL STPSPQNYSK
LSNSTHRQKR SISTERFVET LVVADKMMVG YHGRKDIEHY ILSVMNIVAK LYRDASLGNV
VNIIVTRLIV LTEDQPNLEI NHHADKSLDS FCKWQKSILS HHSNGNSIPE NGMAHHDNAV
LITRYDICTY KNKPCGTLGL ASVAGMCEPE RSCSINEDIG LGSAFTIAHE IGHNFGMNHD
GIGNSCGTKG HETAKLMAAH ITANTNPFSW SACSKDYITS FLDSGRGTCL DNEPLKRDFL
YPTVAPGQVY DADEQCRFQY GTSSRQCKYG EVCRELWCLS KSNRCVTNSI PAAEGTLCQT
GNIEKGWCYQ GECVAFGTWP QSVDGGWGPW SIWGECSRTC GGGVSSSMRH CDSPAPSGGG
KYCLGERKRY RSCNTNACPV GSRDFREKQC ADFDNSPFRG KYYNWKPYTG GGVKPCALNC
LAEGYNFYTE RSPAVIDGTQ CQADSLDICI NGECKHVGCD NILGSDAKED RCRVCGGDGS
TCEATEGLFN KSLPRGGYME VVQIPKGSVH IEIKEVTMSK NYIALKSEGD DYYINGAWTI
DWPRKFDIAG TAFHYKRPSD EPESLEALGA TTENLVVMVL LQEQNLGIHY KFNVPIQRTG
SGDNEVGFSW HHLPWSECSA TCAGGSQKQE LVCKRLDDNS VVQNNYCDPD SKPPENQRDC
NTEPCPPEWF IGDWSECPKT CDGGIRTRTV LCIRKIGPAE EETLEDTHCL THRPIERESC
NNQSCPPKWV TLDWSECTPK CGPGFKHRIA LCKSSDLTKT FPPARCSIHN KPQVRMRCTL
GRCPPPRWIP GEWGQCSAQC GLGQQMRTVQ CLSYTGQPSN DCAESLRPAT MQQCESKCDA
TPISSGDECK DVNKVAYCPL VLKFKFCSRA YFRQMCCKTC QGH
//
