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UniProtKB/Swiss-Prot entry P31580


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

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Entry information
Entry name HCE1_ORYLA
Primary accession number P31580
Secondary accession numbers None
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 62)
Name and origin of the protein
Protein name High choriolytic enzyme 1 [Precursor]
Synonyms EC 3.4.24.67
Hatching enzyme zinc-protease subunit HCE 1
Choriolysin H 1
HCE23
Gene name
Name: hcea
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 71-119 AND 208-223.
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).
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. HCE binds tightly to the egg envelope while it exerts the choriolytic swelling action.
  • 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
M96170; AAA49438.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B48826; B48826.
3D structure databases
HSSP P07584; 1IAE. [HSSP ENTRY / PDB]
ModBase P31580.
Protein family/group databases
MEROPS M12.007; -.
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 P31580.
ProtoNet P31580.
Genome annotation databases
Ensembl ENSORLG00000014873; Oryzias latipes. [Contig view]
Phylogenomic databases
HOVERGEN P31580; -.
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    70  50     Activation peptide. PRO_0000028946
CHAIN   71   270  200     High choriolytic enzyme 1. PRO_0000028947
ACT_SITE   170   170        By similarity. 
METAL   169   169        Zinc; catalytic (By similarity). 
METAL   173   173        Zinc; catalytic (By similarity). 
METAL   179   179        Zinc; catalytic (By similarity). 
CARBOHYD   53    53        N-linked (GlcNAc...) (Potential). 
Sequence information
Length: 270 AA [This is the length of the unprocessed precursor] Molecular weight: 30392 Da [This is the MW of the unprocessed precursor] CRC64: D85C972906E3735A [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNLAPSTCLL LLFLLDIAQA LPVWDEEGHE EGHEEGDGDD FVDITTRILT SNNNTDQLLL 

        70         80         90        100        110        120 
EGDLVAPTNR NAMKCWSSSC FWKKASNGLV VIPYVISSEY SGGEVATIEG AMRAFNGKTC 

       130        140        150        160        170        180 
IRFVRRTNEY DFISVVSKTG CYSELGRKGG QQELSINRGG CMYSGIIQHE LNHALGFQHE 

       190        200        210        220        230        240 
QTRSDRDSYV RINWENIIPA SAYNFNKHDT NNLNTPYDYS SIMHYGRDAF SIAYGRDSIT 

       250        260        270 
PIPNPNVPIG QRNGMSRWDI TRINVLYNCR 

P31580 in FASTA format

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