LCE_ORYLA
ID LCE_ORYLA Reviewed; 271 AA.
AC P31579; O13115;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Low choriolytic enzyme;
DE EC=3.4.24.66;
DE AltName: Full=Choriolysin L;
DE AltName: Full=Hatching enzyme zinc-protease subunit LCE;
DE Flags: Precursor;
GN Name=lce;
OS Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=8090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-96, FUNCTION,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND MISCELLANEOUS.
RC TISSUE=Embryo;
RX PubMed=1397682; DOI=10.1016/0012-1606(92)90110-3;
RA Yasumasu S., Yamada K., Akasaka K., Mitsunaga K., Iuchi I., Shimada H.,
RA Yamagami K.;
RT "Isolation of cDNAs for LCE and HCE, two constituent proteases of the
RT hatching enzyme of Oryzias latipes, and concurrent expression of their
RT mRNAs during development.";
RL Dev. Biol. 153:250-258(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DRR;
RX PubMed=8647122; DOI=10.1111/j.1432-1033.1996.0752p.x;
RA Yasumasu S., Shimada H., Inohaya K., Yamazaki K., Iuchi I., Yasumasu I.,
RA Yamagami K.;
RT "Different exon-intron organizations of the genes for two astacin-like
RT proteases, high choriolytic enzyme (choriolysin H) and low choriolytic
RT enzyme (choriolysin L), the constituents of the fish hatching enzyme.";
RL Eur. J. Biochem. 237:752-758(1996).
CC -!- FUNCTION: Participates in the breakdown of the egg envelope, which is
CC derived from the egg extracellular matrix, at the time of hatching.
CC Thus allowing the newly hatched fish to swim free. LCE solubilizes the
CC egg envelope only after it has been swollen by the action of HCE.
CC {ECO:0000303|PubMed:1397682}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of the inner layer of fish egg envelope. Also
CC hydrolysis of casein and small molecule substrates such as succinyl-
CC Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide.; EC=3.4.24.66;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01211};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01211};
CC -!- SUBCELLULAR LOCATION: Zymogen granule {ECO:0000269|PubMed:1397682}.
CC Note=Stored as proenzymes in the zymogen granules.
CC {ECO:0000269|PubMed:1397682}.
CC -!- DEVELOPMENTAL STAGE: Production of the protein starts in day 2 to day 3
CC embryos and increases thereafter until hatching.
CC {ECO:0000269|PubMed:1397682}.
CC -!- MISCELLANEOUS: In medaka the hatching enzyme system is composed of two
CC distinct proteases, the high choriolytic enzyme (HCE), of which there
CC are two isoforms, and the low choriolytic enzyme (LCE).
CC {ECO:0000303|PubMed:1397682}.
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DR EMBL; M96169; AAA49440.1; -; mRNA.
DR EMBL; D83949; BAA20403.1; -; Genomic_DNA.
DR PIR; A48826; A48826.
DR RefSeq; NP_001098292.1; NM_001104822.1.
DR AlphaFoldDB; P31579; -.
DR SMR; P31579; -.
DR STRING; 8090.ENSORLP00000018819; -.
DR MEROPS; M12.006; -.
DR Ensembl; ENSORLT00000018820; ENSORLP00000018819; ENSORLG00000015017.
DR GeneID; 100049451; -.
DR KEGG; ola:100049451; -.
DR CTD; 100303754; -.
DR eggNOG; KOG3714; Eukaryota.
DR GeneTree; ENSGT00940000154856; -.
DR InParanoid; P31579; -.
DR OMA; SLQRYGC; -.
DR OrthoDB; 681837at2759; -.
DR TreeFam; TF315280; -.
DR Proteomes; UP000001038; Chromosome 24.
DR Proteomes; UP000265180; Unplaced.
DR Proteomes; UP000265200; Unplaced.
DR Bgee; ENSORLG00000015017; Expressed in embryo and 2 other tissues.
DR GO; GO:0042588; C:zymogen granule; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04283; ZnMc_hatching_enzyme; 1.
DR Gene3D; 3.40.390.10; -; 1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001506; Peptidase_M12A.
DR InterPro; IPR006026; Peptidase_Metallo.
DR InterPro; IPR034039; ZnMP_hatching_enz.
DR Pfam; PF01400; Astacin; 1.
DR PRINTS; PR00480; ASTACIN.
DR SMART; SM00235; ZnMc; 1.
DR PROSITE; PS51864; ASTACIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease;
KW Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT PROPEP 21..71
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1397682"
FT /id="PRO_0000028944"
FT CHAIN 72..271
FT /note="Low choriolytic enzyme"
FT /id="PRO_0000028945"
FT DOMAIN 72..271
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 173
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 76..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 123..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 144..164
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CONFLICT 38
FT /note="D -> V (in Ref. 2; BAA20403)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="G -> V (in Ref. 2; BAA20403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 30985 MW; 98B1342E2F7AA581 CRC64;
MDLLAKASVL LLLLLSLSNA QTDNMEEAEN GSSKEEIDES ELEDVSSIIF RMNNNSMEEL
LEGDLVLPKT RNAMKCFGAP DSCRWPKSSN GIVKVPYVVS DNYESDEKET IRNAMKEFAE
KTCIHFVPRN NERAYLSLEP RFGCKSMMGY VGDKQVVVLQ RFGCIKHAVI QHELLHALGF
YHEHTRSDRD QHVKINWENI IKDFTHNFDK NDTDNLGTPY DYGSIMHYGR TAFGKDRKET
ITPIPNPKAA IGQTERMSDI DILRVNKLYK C
