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UniProtKB/Swiss-Prot entry P31579


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LCE_ORYLA
Primary accession number P31579
Secondary accession number O13115
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on July 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 65)
Name and origin of the protein
Protein name Low choriolytic enzyme [Precursor]
Synonyms EC 3.4.24.66
Hatching enzyme zinc-protease subunit LCE
Choriolysin L
Gene name
Name: lce
From
Oryzias latipes (Medaka fish) (Japanese ricefish) [TaxID: 8090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha; Beloniformes; Adrianichthyidae; Oryziinae; Oryzias.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-96.
TISSUE=Embryo;
DOI=10.1016/0012-1606(92)90110-3; PubMed=1397682 [NCBI, ExPASy, EBI, Israel, Japan]
Yasumasu S., Yamada K., Akasaka K., Mitsunaga K., Iuchi I., Shimada H., Yamagami K.;
"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.";
Dev. Biol. 153:250-258(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=DRR;
PubMed=8647122 [NCBI, ExPASy, EBI, Israel, Japan]
Yasumasu S., Shimada H., Inohaya K., Yamazaki K., Iuchi I., Yasumasu I., Yamagami K.;
"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.";
Eur. J. Biochem. 237:752-758(1996).
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.
  • PTM: 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).
  • SIMILARITY: Belongs to the peptidase M12A family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M96169; AAA49440.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D83949; BAA20403.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A48826; A48826.
RefSeq NP_001098292.1; -.
UniGene Ola.92
3D structure databases
HSSP P07584; 1IAE. [HSSP ENTRY / PDB]
ModBase P31579.
Protein family/group databases
MEROPS M12.006; -.
Ontologies
GO
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR001506; Peptidase_M12A.
Graphical view of domain structure.
Pfam PF01400; Astacin; 1.
Pfam graphical view of domain structure.
PRINTS PR00480; ASTACIN.
SMART SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS P31579.
ProtoNet P31579.
Genome annotation databases
Ensembl ENSORLG00000015017; Oryzias latipes. [Contig view]
GeneID 100049451; -.
Phylogenomic databases
HOVERGEN P31579; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
PROPEP   21    71  51     Activation peptide. PRO_0000028944
CHAIN   72   271  200     Low choriolytic enzyme. PRO_0000028945
ACT_SITE   173   173        By similarity. 
METAL   172   172        Zinc; catalytic (By similarity). 
METAL   176   176        Zinc; catalytic (By similarity). 
METAL   182   182        Zinc; catalytic (By similarity). 
CARBOHYD   30    30        N-linked (GlcNAc...) (Potential). 
CARBOHYD   54    54        N-linked (GlcNAc...) (Potential). 
CARBOHYD   211   211        N-linked (GlcNAc...) (Potential). 
CONFLICT   38    38        D -> V (in Ref. 2; BAA20403). 
CONFLICT   152   152        G -> V (in Ref. 2; BAA20403). 
Sequence information
Length: 271 AA [This is the length of the unprocessed precursor] Molecular weight: 30985 Da [This is the MW of the unprocessed precursor] CRC64: 98B1342E2F7AA581 [This is a checksum on the sequence]
        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 

P31579 in FASTA format

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