ID I3KBT9_ORENI Unreviewed; 946 AA.
AC I3KBT9;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif, 15b {ECO:0000313|Ensembl:ENSONIP00000018584.2};
GN Name=ADAMTS8 {ECO:0000313|Ensembl:ENSONIP00000018584.2};
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:ENSONIP00000018584.2, 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:ENSONIP00000018584.2}
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 AlphaFoldDB; I3KBT9; -.
DR Ensembl; ENSONIT00000018601.2; ENSONIP00000018584.2; ENSONIG00000014762.2.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000159642; -.
DR HOGENOM; CLU_000660_3_0_1; -.
DR TreeFam; TF331949; -.
DR Proteomes; UP000005207; Linkage group LG14.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; IEA:InterPro.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; -; 2.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
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; IPR013277; Pept_M12B_ADAM-TS8.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF41; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 8; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 2.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01861; ADAMTS8.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00608; ACR; 1.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Cleavage on pair of basic residues {ECO:0000256|ARBA:ARBA00022685};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..37
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 38..946
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5025605205"
FT DOMAIN 221..430
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 365
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 224
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 314
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 364
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 368
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 374
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 425
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 296..348
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 325..330
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 342..425
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 380..409
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 451..476
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 462..484
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 471..505
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 499..510
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 536..573
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 540..578
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 551..563
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 946 AA; 103996 MW; BB767641BD4F7F18 CRC64;
CALAPSAGKC PRFCLQTMCA TACLLFSLLC VVNAALASSF ESEDVVPVRI NARTSGRFWK
RSEDQPRFVL SAFGKDFTLN LIPDTSFIAP SFTIQRVKAR DVGALRSAPG ARGHLRSCFY
SGNVDQDQNS LVAVSLCSGI FGSFVTEGKE YLIEPKLHGG PGPATAEEPH VIRRRTFNES
HGVPLPFDQA AVEQHNGESF THGDGDARRE PRRRRFVSAP RFIETLLVAD STMTHFYGDE
IKHYILTLMS MAAQLYKHPS IKNSVNMVVV KMLVVEDEEI GPEVSSNGGV ALRNFCSWQQ
LFNPPSQRHP EHYDTAMLFT REDICGQKSC DTLGVADVGT MCDPKRSCSV IEDNGLQAAF
TAAHELGHVL SMPHDDSKTC ERLFGDLGGH HLMAPLFVSL NKTMPWSPCS ALYVTEFFDN
GHGDCLLDVP ESAMPLPQEL PGSKYSVDQQ CQQIFGEEFV HCPNTSDSDI CSQLWCQEEG
TLQCSTKNGS LPWADGTPCS ANGTCLHGVC VPVHEAMKPL MVVDGGWSSW GPWQQCSRTC
GGGVEFSYRE CTNPVPQNGG KYCEGQRVQY QSCNIQPCDN NEGKSFREEQ CEKYNSPNYL
DHNGNAKQWI PKYAGVSPRD RCKLFCRARG SSEFKVFEPK VIDGTPCGPD TTSVCVQGQC
VKAGCDQVIG SNKRVDKCGV CGGSGLTCRK ITDSYNKATY GYSDIVTIPT GATNIDIKQR
SHRGIKHDGY YLAVKRESGG YILNGNFSVS TVEQDIPVLG AVLKYSGSST TLERIQSFRQ
LKEAITIQLL TTAGDGGPPK VKYTFFIPKD VTLNKSKEKK GLSLSLHMIH PFGVPEWVLG
EWSPCSKTCG SGWSRRNVEC MDDEGFLSSQ CGKDLKPIDI RPCADLPCPI WQMGPWSACS
RTCGQGERRR SVFCIDYTGK TVEAEQCDPK KIPEPVSGEC FNQDCL
//
