HCE1_ORYLA
ID HCE1_ORYLA Reviewed; 270 AA.
AC P31580;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=High choriolytic enzyme 1;
DE EC=3.4.24.67;
DE AltName: Full=Choriolysin H 1;
DE AltName: Full=HCE23;
DE AltName: Full=Hatching enzyme zinc-protease subunit HCE 1;
DE Flags: Precursor;
GN Name=hcea;
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 71-119 AND 208-223,
RP FUNCTION, 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).
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; M96170; AAA49438.1; -; mRNA.
DR PIR; B48826; B48826.
DR RefSeq; NP_001188427.1; NM_001201498.1.
DR PDB; 3VTG; X-ray; 1.34 A; A=71-270.
DR PDBsum; 3VTG; -.
DR AlphaFoldDB; P31580; -.
DR SMR; P31580; -.
DR STRING; 8090.ENSORLP00000018613; -.
DR MEROPS; M12.007; -.
DR GeneID; 100529164; -.
DR KEGG; ola:100529164; -.
DR CTD; 100529164; -.
DR eggNOG; KOG3714; Eukaryota.
DR InParanoid; P31580; -.
DR OrthoDB; 681837at2759; -.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasmic vesicle; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Signal; Zinc; Zymogen.
FT SIGNAL 1..20
FT PROPEP 21..70
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:1397682"
FT /id="PRO_0000028946"
FT CHAIN 71..270
FT /note="High choriolytic enzyme 1"
FT /id="PRO_0000028947"
FT DOMAIN 71..270
FT /note="Peptidase M12A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT ACT_SITE 170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 75..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 120..269
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT DISULFID 141..161
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01211"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 90..96
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:3VTG"
FT TURN 114..118
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 130..136
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3VTG"
FT TURN 158..160
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 199..205
FT /evidence="ECO:0007829|PDB:3VTG"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3VTG"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:3VTG"
FT HELIX 257..266
FT /evidence="ECO:0007829|PDB:3VTG"
SQ SEQUENCE 270 AA; 30392 MW; D85C972906E3735A CRC64;
MNLAPSTCLL LLFLLDIAQA LPVWDEEGHE EGHEEGDGDD FVDITTRILT SNNNTDQLLL
EGDLVAPTNR NAMKCWSSSC FWKKASNGLV VIPYVISSEY SGGEVATIEG AMRAFNGKTC
IRFVRRTNEY DFISVVSKTG CYSELGRKGG QQELSINRGG CMYSGIIQHE LNHALGFQHE
QTRSDRDSYV RINWENIIPA SAYNFNKHDT NNLNTPYDYS SIMHYGRDAF SIAYGRDSIT
PIPNPNVPIG QRNGMSRWDI TRINVLYNCR
