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Reviewed, UniProtKB/Swiss-Prot P31580 (HCE1_ORYLA)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    High choriolytic enzyme 1
    EC=3.4.24.67
Alternative name(s):
    Hatching enzyme zinc-protease subunit HCE 1
    Choriolysin H 1
    HCE23
Gene names
Name: hcea
OrganismOryzias latipes (Medaka fish) (Japanese ricefish)
Taxonomic identifier8090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaAtherinomorphaBeloniformesAdrianichthyidaeOryziinaeOryzias

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. 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.

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
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Zymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Propeptide21 – 7050Activation peptide Ref.1
PRO_0000028946
Chain71 – 270200High choriolytic enzyme 1
PRO_0000028947

Sites

Active site1701 By similarity
Metal binding1691Zinc; catalytic By similarity
Metal binding1731Zinc; catalytic By similarity
Metal binding1791Zinc; catalytic By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P31580-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: D85C972906E3735A

FASTA27030,392
        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 

« Hide

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 71-119 AND 208-223.
Tissue: Embryo.

Cross-references

Sequence databases

M96170 mRNA. Translation: AAA49438.1.
PIRB48826.

3D structure databases

HSSPHSSP built from PDB template 1IAE based on UniProtKB P07584.
ModBaseSearch...

Protein family/group databases

MEROPSM12.007.

Genome annotation databases

EnsemblENSORLG00000014873. Oryzias latipes. [Contig view]

Phylogenomic databases

HOVERGENP31580.

Enzyme and pathway databases

BRENDA3.4.24.67. 19130.

Family and domain databases

InterProIPR006025. Pept_M_Zn_BS.
IPR006026. Peptidase_M.
IPR001506. Peptidase_M12A.
[Graphical view]
PfamPF01400. Astacin. 1 hit.
[Graphical view]
PRINTSPR00480. ASTACIN.
SMARTSM00235. ZnMc. 1 hit.
[Graphical view]
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHCE1_ORYLA
AccessionPrimary (citable) accession number: P31580
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents