Reviewed, UniProtKB/Swiss-Prot P31579 (LCE_ORYLA)

Names and origin

Protein names

Recommended name:
    Low choriolytic enzyme
    EC=3.4.24.66
Alternative name(s):
    Hatching enzyme zinc-protease subunit LCE
    Choriolysin L

Gene names

Name:

lce

Organism

Oryzias latipes (Medaka fish) (Japanese ricefish)

Taxonomic identifier

8090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Atherinomorpha › Beloniformes › Adrianichthyidae › Oryziinae › Oryzias

Protein attributes

Sequence length	271 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Participates in the breakdown of the egg envelope, which is derived from the egg extracellular matrix, at the time of hatching. Thus allowing the newly hatched fish to swim free. LCE solubilizes the egg envelope only after it has been swollen by the action of HCE.
Catalytic activity	Hydrolysis of the inner layer of fish egg envelope. Also hydrolysis of casein and small molecule substrates such as succinyl-Leu-Leu-Val-Tyr-|-7-(4-methyl)coumarylamide.
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Note: Stored as proenzymes in the zymogen granules.
Developmental stage	Production of the protein starts in day 2 to day 3 embryos and increases thereafter until hatching.
Post-translational modification	O-glycosylated Probable.
Miscellaneous	In medaka the hatching enzyme system is composed of two distinct proteases, the high choriolytic enzyme (HCE), of which there are two isoforms, and the low choriolytic enzyme (LCE).
Sequence similarities	Belongs to the peptidase M12A family.

Ontologies

Keywords
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Glycoprotein Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20
	Propeptide	21 – 71	51	Activation peptide Ref.1		PRO_0000028944
	Chain	72 – 271	200	Low choriolytic enzyme		PRO_0000028945
Sites
	Active site	173	1	By similarity
	Metal binding	172	1	Zinc; catalytic By similarity
	Metal binding	176	1	Zinc; catalytic By similarity
	Metal binding	182	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
	Glycosylation	54	1	N-linked (GlcNAc...) Potential
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
Experimental info
	Sequence conflict	38	1	D → V in BAA20403. Ref.2
	Sequence conflict	152	1	G → V in BAA20403. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P31579-1 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: 98B1342E2F7AA581	FASTA	271	30,985
	10 20 30 40 50 60 MDLLAKASVL LLLLLSLSNA QTDNMEEAEN GSSKEEIDES ELEDVSSIIF RMNNNSMEEL 70 80 90 100 110 120 LEGDLVLPKT RNAMKCFGAP DSCRWPKSSN GIVKVPYVVS DNYESDEKET IRNAMKEFAE 130 140 150 160 170 180 KTCIHFVPRN NERAYLSLEP RFGCKSMMGY VGDKQVVVLQ RFGCIKHAVI QHELLHALGF 190 200 210 220 230 240 YHEHTRSDRD QHVKINWENI IKDFTHNFDK NDTDNLGTPY DYGSIMHYGR TAFGKDRKET 250 260 270 ITPIPNPKAA IGQTERMSDI DILRVNKLYK C

References

[1]

"Isolation of cDNAs for LCE and HCE, two constituent proteases of the hatching enzyme of Oryzias latipes, and concurrent expression of their mRNAs during development." Yasumasu S., Yamada K., Akasaka K., Mitsunaga K., Iuchi I., Shimada H., Yamagami K. Dev. Biol. 153:250-258(1992) [PubMed: 1397682] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-96. Tissue: Embryo.

[2]

"Different exon-intron organizations of the genes for two astacin-like proteases, high choriolytic enzyme (choriolysin H) and low choriolytic enzyme (choriolysin L), the constituents of the fish hatching enzyme." Yasumasu S., Shimada H., Inohaya K., Yamazaki K., Iuchi I., Yasumasu I., Yamagami K. Eur. J. Biochem. 237:752-758(1996) [PubMed: 8647122] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DRR.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M96169 mRNA. Translation: AAA49440.1. D83949 Genomic DNA. Translation: BAA20403.1.
PIR	A48826.
RefSeq	NP_001098292.1.
UniGene	Ola.92
3D structure databases
HSSP	HSSP built from PDB template 1IAE based on UniProtKB P07584.
ModBase	Search...
Protein family/group databases
MEROPS	M12.006.
Genome annotation databases
Ensembl	ENSORLG00000015017. Oryzias latipes. [Contig view]
GeneID	100049451.
Phylogenomic databases
HOVERGEN	P31579.
OMA	P31579. HINSYID.
Enzyme and pathway databases
BRENDA	3.4.24.66. 19130.
Family and domain databases
InterPro	IPR006025. Pept_M_Zn_BS. IPR006026. Peptidase_M. IPR001506. Peptidase_M12A. [Graphical view]
Pfam	PF01400. Astacin. 1 hit. [Graphical view]
PRINTS	PR00480. ASTACIN.
SMART	SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LCE_ORYLA

Accession

Primary (citable) accession number: P31579
Secondary accession number(s): O13115

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)