HCE2_ORYLA
ID HCE2_ORYLA Reviewed; 279 AA.
AC P31581;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=High choriolytic enzyme 2;
DE EC=3.4.24.67;
DE AltName: Full=Choriolysin H 2;
DE AltName: Full=HCE21;
DE AltName: Full=Hatching enzyme zinc-protease subunit HCE 2;
DE Flags: Precursor;
GN Name=hceb;
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], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP 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).
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. HCE binds tightly to
CC the egg envelope while it exerts the choriolytic swelling action.
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=3.4.24.67;
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:0000305|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; M96171; AAA49439.1; -; mRNA.
DR PIR; C48826; C48826.
DR RefSeq; NP_001098293.1; NM_001104823.1.
DR AlphaFoldDB; P31581; -.
DR SMR; P31581; -.
DR STRING; 8090.ENSORLP00000018636; -.
DR MEROPS; M12.007; -.
DR GeneID; 100049452; -.
DR KEGG; ola:100049452; -.
DR CTD; 100049452; -.
DR eggNOG; KOG3714; Eukaryota.
DR InParanoid; P31581; -.
DR OrthoDB; 455209at2759; -.
DR BRENDA; 3.4.24.67; 3199.
DR Proteomes; UP000001038; Unplaced.
DR Proteomes; UP000265180; Chromosome 9.
DR Proteomes; UP000265200; Chromosome 9.
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 2: Evidence at transcript level;
KW Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..20
FT PROPEP 21..79
FT /note="Activation peptide"
FT /id="PRO_0000028948"
FT CHAIN 80..279
FT /note="High choriolytic enzyme 2"
FT /id="PRO_0000028949"
FT DOMAIN 80..279
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT REGION 26..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 178
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 BINDING 188
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..89
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 129..278
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 150..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
SQ SEQUENCE 279 AA; 31490 MW; 00244107A8B01B8C CRC64;
MNLASSACLL LLFLLGIAQA LPVQNEEGHE EGNKEGHGEE GVEEGDEDDF VDFTTRILTS
NNNTDQLLLE GDLVAPTNRN AMKCWYNSCF WKKASNGFVV IPYVISSQYS RGEVATIEGA
MRAFNGRTCI RFVRRTNEYD FISVVSKNGC YSELGRKGGQ QELSLNRGGC MYSGIIQHEL
NHALGFQHEQ TRSDRDSYVR INWQNIIPAS AYNFNKHDTN NLNTPYDYSS IMHYGRDAFS
IAYGRDSITP IPNPNVPIGQ RNGMSRWDIT RSNVLYNCR
