ID A0A2U9B3F1_SCOMX Unreviewed; 948 AA.
AC A0A2U9B3F1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Putative disintegrin and metalloproteinase with thrombospondin motifs 8 {ECO:0000313|EMBL:AWO98483.1};
GN ORFNames=F2P81_017031 {ECO:0000313|EMBL:KAF0030300.1}, SMAX5B_008396
GN {ECO:0000313|EMBL:AWO98483.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWO98483.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWO98483.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAF0030300.1, ECO:0000313|Proteomes:UP000438429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ysfricsl-2016a {ECO:0000313|EMBL:KAF0030300.1};
RC TISSUE=Blood {ECO:0000313|EMBL:KAF0030300.1};
RA Xu H., Xu X.-W., Shao C., Chen S.;
RT "Draft genomes of female and male turbot (Scophthalmus maximus).";
RL Submitted (JUN-2019) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026245; AWO98483.1; -; Genomic_DNA.
DR EMBL; VEVO01000015; KAF0030300.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9B3F1; -.
DR STRING; 52904.ENSSMAP00000026502; -.
DR OMA; EDTKPCG; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000246464; Chromosome 3.
DR Proteomes; UP000438429; Unassembled WGS sequence.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
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:SF40; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 1; 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; 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 Integrin {ECO:0000313|EMBL:AWO98483.1};
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:UP000246464};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..948
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033328825"
FT DOMAIN 223..432
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT ACT_SITE 367
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 226
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 316
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 366
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 370
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 376
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 427
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 298..350
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 327..332
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 344..427
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 382..411
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 453..478
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 464..486
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 473..507
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 501..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 538..575
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 542..580
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 553..565
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 948 AA; 104738 MW; CD55AEEAFD251B15 CRC64;
MCYTVRLVFV SMCVMNAAHC AQFESEDVLP VRIKARTSGR FWKRSEEQPR FVLRAFDKDL
TLNLTPDTSF IAPSFTVQRI KARDAGALRS ASGGQPVPDP DLMSQTEDSE AHLRSCFYSG
NVDHDHNSLV AVSLCSGILG SFITEGNEYL IEPKLRGARG PDSAEQPHVI TRRTLVQSRG
APLLFDHAAE VRRAEVHSGE SFTRGDGDAR REPRRRRFVS APRFIETLLV ADSTMTHFYG
DEIKHYILTL MSMAAQLYKH PSIKNSVNMV VVKMLIVEDE EVGPELSSNG GVALRNFCSW
QQHFNPPSQR HPEHYDTAML FTREDICGHK SCDTLGVADV GTMCDPKRSC SVIEDNGLQA
AFTAAHELGH VLSMPHDDSK TCERLFGDLG GHFLMAPLFV SLNETAPWSP CSALYVTEFF
DNGHGDCLLD VPESTVPLPS ELPGTKYSLD KQCQQIFGEE FIHCPNTSDS DVCSQLWCQE
DGTMQCTTKN GSLAWADGTP CGLNGTCLRG ACMPTHEVMK PLVVVDGGWS LWGPWQQCSR
TCGGGVEFSY RECTDPVPRN GGKYCEGQRV RYQSCNTQSC DNNEGKSFRE EQCGKYNSLH
YLDYNGNMKQ WIPKYAGVSP RDRCKLFCRA RGSSEFKVFE SKVIDGTTCG PDTTSVCVQG
QCVKAGCDQV IGSNRRVDKC GVCGGSGLTC RKITGSYSKA TYGYSDIVTI PIGATNIDIK
QRSQRGIKHD GNYLAVKRES GGYILNGNFS VSTVEQDIPV LGAVLKYSGS STTLERIQSF
RQLNEAITVQ ILATAGDANP PKVKYTFFIP RDVTLNKSKE KKGSSPSLHM IHPFGMPDWV
LGEWSECSKS CGSGWSRRNV ECRDNAGFLS SQCDNDLKPA DIKPCGDLPC PMWQLGPWST
CSRNCGQGER RRSVFCIDYT GKIAEQEKCD PNKIPEPVSG ECLNQECL
//
