ID I3J6C1_ORENI Unreviewed; 988 AA.
AC I3J6C1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=Metalloendopeptidase {ECO:0000256|RuleBase:RU361183};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU361183};
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:ENSONIP00000004411.2, 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:ENSONIP00000004411.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|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 AlphaFoldDB; I3J6C1; -.
DR STRING; 8128.ENSONIP00000004411; -.
DR MEROPS; M12.005; -.
DR Ensembl; ENSONIT00000004413.2; ENSONIP00000004411.2; ENSONIG00000003503.2.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000157176; -.
DR HOGENOM; CLU_005140_0_0_1; -.
DR InParanoid; I3J6C1; -.
DR OMA; HCEQRCL; -.
DR TreeFam; TF314351; -.
DR Proteomes; UP000005207; Linkage group LG7.
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; 2.
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; 1.
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; 2.
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:UP000005207};
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..988
FT /note="Metalloendopeptidase"
FT /evidence="ECO:0000256|RuleBase:RU361183"
FT /id="PRO_5025707578"
FT DOMAIN 108..307
FT /note="Peptidase M12A"
FT /evidence="ECO:0000259|PROSITE:PS51864"
FT DOMAIN 309..421
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 422..548
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 548..589
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 593..705
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 705..745
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 749..861
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 862..978
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 69..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 201
FT /evidence="ECO:0000256|PIRSR:PIRSR001199-1,
FT ECO:0000256|PROSITE-ProRule:PRU01211"
FT BINDING 200
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 204
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 210
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 170..192
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
FT DISULFID 172..173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 988 AA; 110634 MW; CF9D34034B15ACAB CRC64;
MEVAPRFLFL LCGLCVSLAA DWETVETTFT DLGDEIDYKD PCKAAAFLGD IALDEDDLRL
FKGARGGDDA QHAVQSNHTN SANSSTSSEN RRSERAADRQ SLRRQRRAAT ARPERVWPDG
IIPYVISGNF SGSQRAIFRQ AMRHWEKHTC VTFTERTTEE SYIVFTYRPC GCCSYVGRRG
GGPQAISIGK NCDKFGIVVH ELGHVIGFWH EHTRPDRDEH VSIIRDNIQQ GQEYNFLKME
PGEVDSLGEV YDFGSIMHYA RNTFSRGIFL DTILPRYDVN GVRPSIGQRT KLSKGDIAQA
CKLYKCAKCG ESLQDSSGNF SSPGFPNGYS AYTHCVWRIS VTPGEKIVLN FTSMDLFRSH
LCWYDHVEVR DGFWRKAPLK GRFCGDTLPA QIISTDSRLW IEFRSSSSWV GKGFSAIYEA
ICGGEVKRES GQIQSPNYPD EYQSNKECVW KITVAEGFDV GLSFQSFEVK LPLLLLFLHS
GNIEKHDSCA YDYVEVRDGA SESSPLLGRF CGYDKPDDIK STSNQLWLKF ASDGSVNKAG
FAANFFKEMD ECSRPDNGNC EQRCLNTLGS YRCACDPGYE LAADKHTCET AACGGFITKL
NGSITTPGWP KEYPPNKNCV WQLVAPIQYR ITLVFDVFET EGNDVCKYDF VEVRSGLSSD
SKLHGKFCGA EKPEVITSQQ NNMRIEFKSD NTVSKRGFKA HFFSDIDECS KGNGGCQHEC
VNTFGSYSCQ CRRGFMLHDN RHDCKEAGCD HVINSVSGTI ASPNWPDKYP SKKACTWSLS
TTPGHRIKLI FNEVDMEAHL ECAYDHLEIY DGRDNRAASL GRFCGTKKPS PVISSANKMF
LRFFSDNSVQ KRGFEASYRA ECGGSFKAEV KTKDLYSHAQ FGDNNYPGGS DCLWVVTAEK
GYGVEIIFQV FEIEEEADCG YDYVELYDGA DTKSPRLGRY CGSGAPEDVY SAGDSIVLKF
HSDDSINKKG FHVRYTSTKF QDTLHASK
//
