ID A0A3B3DAV4_ORYME Unreviewed; 970 AA.
AC A0A3B3DAV4;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
GN ORFNames=FQA47_020862 {ECO:0000313|EMBL:KAF6729274.1};
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:ENSOMEP00000027021.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000027021.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
RN [2] {ECO:0000313|EMBL:KAF6729274.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Bigg-433 {ECO:0000313|EMBL:KAF6729274.1};
RX PubMed=32938378;
RA Liang P., Saqib H.S.A., Ni X., Shen Y.;
RT "Long-read sequencing and de novo genome assembly of marine medaka (Oryzias
RT melastigma).";
RL BMC Genomics 21:0-0(0).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01211,
CC ECO:0000256|RuleBase:RU361183};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PROSITE-
CC ProRule:PRU01211, ECO:0000256|RuleBase:RU361183};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; WKFB01000259; KAF6729274.1; -; Genomic_DNA.
DR STRING; 30732.ENSOMEP00000027021; -.
DR PaxDb; 30732-ENSOMEP00000027021; -.
DR Ensembl; ENSOMET00000003035.1; ENSOMEP00000027021.1; ENSOMEG00000009251.1.
DR GeneTree; ENSGT00940000157176; -.
DR OMA; RTVQTIN; -.
DR Proteomes; UP000261560; Unplaced.
DR Proteomes; UP000646548; Unassembled WGS sequence.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00041; CUB; 5.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd04281; ZnMc_BMP1_TLD; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 5.
DR InterPro; IPR015446; BMP_1/tolloid-like.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR034036; ZnMP_TLD/BMP1.
DR PANTHER; PTHR24251:SF42; BONE MORPHOGENETIC PROTEIN 1; 1.
DR PANTHER; PTHR24251; OVOCHYMASE-RELATED; 1.
DR Pfam; PF01400; Astacin; 1.
DR Pfam; PF00431; CUB; 5.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR PIRSF; PIRSF001199; BMP_1/tolloid-like; 2.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00042; CUB; 5.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00235; ZnMc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 5.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01180; CUB; 5.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
PE 4: Predicted;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001199-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|PROSITE-
KW ProRule:PRU01211};
KW Protease {ECO:0000256|PROSITE-ProRule:PRU01211,
KW ECO:0000256|RuleBase:RU361183};
KW Reference proteome {ECO:0000313|Proteomes:UP000646548};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|RuleBase:RU361183};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001199-2}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT CHAIN 20..970
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5041003286"
FT DOMAIN 105..304
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 306..418
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 419..531
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 531..572
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 575..687
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 731..843
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 844..960
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 81..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 198
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-2,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 167..189
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 169..170
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 970 AA; 109095 MW; AB7BD51E6C5DB785 CRC64;
MDLSVRCLFL FSCLGVILAI DLDAADPGYY VEPTATSEAI DYKDPCKAVA FLGDIALDEE
DLRHFKVDRI IDLAQRTVQN VNHTDEGSDN SGNANSQGSQ RRKRAATSRP ERVWPEGVIP
YVISGNFSGS QRAVFRQAMR HWEKHTCVTF IERTQEESYI VFTYRPCGCC SYVGRRGGGP
QAISIGKNCD KFGIVVHELG HVIGFWHEHT RPDRDEHVSI IKDNIQPGQE YNFLKMEPGE
VDSLGEVYDF DSIMHYARNT FSRGIFLDTI LPRYDVNGVR PPIGQRTRLS KGDIAQARKL
YKCSKCGESL QDSSGNFSSP GFPNGYSAYM HCIWRISVTP GEKIILNFTS MDLYRSHLCW
YDHVEIRDGY WRKAPLKGRF CGDKLPEPII STDSRLWIEF RSSSNWVGKG FSAVYEAICG
GDVKRDNGQI QSPNYPDDYR PNKVCIWKIS VSEGYHVGLT FQSFEIERHD SCAYDYLEVR
DGLSENSPLL GRFCGYDKPD DIKTSSNHLW MKFVSDGSVN KAGFAANFFK EMDECSKPDN
GRCEQRCVNT LGSYKCACDP GYELAADKRS CEAACGGFIT KLNGSITSPG WPREYPPNKN
CIWQLVAPTQ YRITLLFDVF ETEGNDVCKY DFVEVRSGLS ADSKLHGKFC GAEKPEAITS
QYNNMRIEFK SDNTVSKKGF KAQFFSDKDE CSKENGGCQH DCVNTFGSYR CQCRSGFVLH
ENKHDCKEAG CDHTVNSVSG TITSPNWPDK YPSKKACTWA LSTTPGHRIK IAFNEIDMEA
HLDCAYDHIQ IYDGRDAKAP SLGRFCGSKK PQPILSSGNK LFIRFFSDNS VQKKGFDASH
SAECGGILKA EVKTKDLFSH AQFGDNNYPG ASDCEWVISA EKGYGVELIF QTFEIEEEAD
CGYDYMELFD GADTKSPRLG RYCGSGPPEE IYSAGDSIVI KFHSDDTINK KGFHVRYTST
KFQDTLHSRK
//
