ID A0A3B3D420_ORYME Unreviewed; 1109 AA.
AC A0A3B3D420;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 10-like {ECO:0000313|Ensembl:ENSOMEP00000024611.1};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000024611.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000024611.1}
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 AlphaFoldDB; A0A3B3D420; -.
DR STRING; 30732.ENSOMEP00000024611; -.
DR PaxDb; 30732-ENSOMEP00000024611; -.
DR Ensembl; ENSOMET00000009217.1; ENSOMEP00000024611.1; ENSOMEG00000005389.1.
DR GeneTree; ENSGT00940000158404; -.
DR OMA; TQQCETK; -.
DR Proteomes; UP000261560; Unplaced.
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; 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:SF26; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 10; 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 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..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1109
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017294595"
FT DOMAIN 243..461
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1071..1109
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT ACT_SITE 397
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 203
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 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 344
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 396
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 400
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 406
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 456
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 319..380
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 355..362
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 374..456
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 413..440
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 483..505
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 494..512
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 500..535
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 525..540
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..600
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 567..605
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..590
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1109 AA; 124537 MW; 0303C57918204D1F CRC64;
METLWRTGLV CTVIVIMGAS EVAGGRRDDL AQSQAAFLST LGQYEIAIPV RVGPNGEKLD
GDNSHHQRKR RSPEDRLHDT LFYQLSTSQN NFLLNLTLQG GLLSRRFRVE YWKRGQLAWS
HPYSPHCHYT GHLQDQPHSS KVALSNCNGL QGVIVAGGEE YLIEPLVSSD NQTKTESSER
TEERPHVVYK RSSLRHQYKG RSCGVIDEKP MKSLSWWQRT LKMPPHHVGR GQLPLKRSVS
QERYVETLVV ADKMMVGYHG RRDIEQYILA VMNIVAKLFQ DSSLGNAVNI VVTRLILLME
DQPTLEINHH AGKSLDSFCK WQKSIQHRNS YGNAIPDNGI AHHDTAVLIT RYDICIQKNK
PCETLGLAPV GGMCEPERSC SINEDIGLGT AFTIAHEIGH TFGMNHDGMG NTCGPRSQET
AKLMADHITM KTNPFIWSAC SRDYITSFLD SGMGSCLNNV PLKQEFVYPT TAPGQAYDAD
EQCRFQYGIR SRQCKYSEVC SELWCMSKSN RCITSSIPAA EGTICQTNTI EKGWCYKRMC
VAYGTRPEGV DGGWSLWSPW GECSRTCGGG VSFSARHCDS PRPTIGGKYC LGERKRFRSC
NIDECPAGSR DFREIQCSDF DNIPFRGKFY TWKPYRGGGV KPCSLNCLAE GYNFYTERAS
AVVDGTLCRD ESLDMCVSGE CKHVGCDRVL GSDVREDRCR ICGGDGSSCD SVEGVFNDSL
PEGGYEEVVR IPKGSVFIHL QELNMSLNYL VLKSKSDQYF INGKLTIDTP RRFNVAGTMF
HYRRPTDGPE TLEALGPTNI TLIVMVLVRE ENPGIHYRFN PPLNRDPLSG FSWFYTSWSR
CSVLCAGGVQ IQQVVCKRLM DHTVVYNHFC DKKSKPKEKR RSCNTEPCSP TWWTGGWSEC
SRSCNGGLRT REVLCKRRIS VTEEKILDDS ACSSHRPSLT EPCNNHSCPP EWLALDWSEC
TPSCGPGYRH RVVLCKSGES GDILPESRCP KHGRPTSRVR CNLKRCPPPQ WIVGPWGECS
AKCGLGQEMR LVQCLTHTGQ PSSECLDHQR PAAMQQCRSK CDLNLPISTE NTEECKDVNT
VAYCPLVLRF KFCSRPYFRQ MCCKTCQGH
//
