ID A0A3B4C272_PYGNA Unreviewed; 927 AA.
AC A0A3B4C272;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 8 {ECO:0000313|Ensembl:ENSPNAP00000005997.1};
GN Name=ADAMTS8 {ECO:0000313|Ensembl:ENSPNAP00000005997.1};
OS Pygocentrus nattereri (Red-bellied piranha).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Pygocentrus.
OX NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000005997.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000005997.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_017557271.1; XM_017701782.1.
DR AlphaFoldDB; A0A3B4C272; -.
DR STRING; 42514.ENSPNAP00000005997; -.
DR Ensembl; ENSPNAT00000004318.1; ENSPNAP00000005997.1; ENSPNAG00000012072.1.
DR GeneID; 108429771; -.
DR CTD; 569618; -.
DR GeneTree; ENSGT00940000159642; -.
DR OMA; QSCNIQT; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000261440; Unplaced.
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; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
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 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 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 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}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..927
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017429463"
FT DOMAIN 204..413
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 348
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 297
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 347
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 351
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 357
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 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 279..331
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 308..313
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 325..408
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 363..392
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 434..459
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 445..467
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 454..488
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 482..493
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 520..557
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 524..562
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 535..547
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 927 AA; 102259 MW; EDC9DB65F33FB521 CRC64;
MGCHIHLILA AVLLAEAVRC EFVESQETVA VKLTPRHGGS WRSEFTDRHL FKLAAFGQVF
ALDLKPDSSF VAPTLHIQRI KAKHLPAAVN GSEQTDNGVS ESGEELRGCF YSGTVNGDLD
SMVAVSLCRG IRGTFVTRGD EYFIQPTASG GTFSQPHVVK RRVVASSRET WKRDLDQAQD
DDRFLTGERD DGKRREKRFV SSARYIETLV VADYSMTRFY GDEIKHYLLT LMGMAAQLYA
HPSLKNAVSL VVVKILVIED EELGPELSSN GGMALRNFCA WQQLFNPSSQ RHPEHYDTAI
LFTREDICGH EHCDTLGVAD VGTMCDPKRS CSVIEDNGLQ AAFTVSHELG HVLSMPHDDS
RNCEKLFGHI DRHHMMAPLF VHLNKTFPWS PCSALYITEF FDNGHGDCLL DAPEQTIPLQ
AEPPGHAYGL DRQCQQSFGE EYTRCPNAPE DQACVQLWCR EEGKLQCTTR NGSLPWADGT
PCREDKSCRG GMCVLNTLLE SGQELPVDGG WGAWGPWGPC SRTCGGGVEF SRRECTDPVP
QNGGSYCVGQ RVKYQSCNIQ TCPGDHGKSF REEQCEKYNS DRYLDMDGNI KQWIPKYAGV
SPRDRCKLFC RAKHNNEFKV FESKVVDGTT CGPDTTSICV QGQCIKAGCD QVIGSNIRLD
KCGVCGGDGT SCRKISGSLN KATFGYNDIV TIPAGATNID VKQRSHRGIK HDGNYLAVKA
EDGTYILNGN FSVSTAEQDI PVSGAVLRYS GSSTTLERLL SFQELRQTIT IQLLSTAGDT
SPPRVKYSFF LPRDVPFSKP GTDSGLSPHV ILPFGGADWV LGEWSECSKS CGAGWSRRSV
ECQDKAGTPS YFCDADLRPT DIRPCGDLPC PVWQMGPWSA CSRTCGPGER RRSVLCIDYT
GKAVEPEKCN PDKRPEAVSG ECFYQDC
//
