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P31581 (HCE2_ORYLA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
High choriolytic enzyme 2

EC=3.4.24.67
Alternative name(s):
Choriolysin H 2
HCE21
Hatching enzyme zinc-protease subunit HCE 2
Gene names
Name:hceb
OrganismOryzias latipes (Medaka fish) (Japanese ricefish)
Taxonomic identifier8090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiEuteleosteiNeoteleosteiAcanthomorphaAcanthopterygiiPercomorphaAtherinomorphaBeloniformesAdrianichthyidaeOryziinaeOryzias

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Cytoplasmic vesiclesecretory vesicle. 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
   Cellular componentCytoplasmic vesicle
   DomainSignal
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Zymogen
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componenttransport vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Propeptide21 – 7959Activation peptide
PRO_0000028948
Chain80 – 279200High choriolytic enzyme 2
PRO_0000028949

Sites

Active site1791 By similarity
Metal binding1781Zinc; catalytic By similarity
Metal binding1821Zinc; catalytic By similarity
Metal binding1881Zinc; catalytic By similarity

Amino acid modifications

Glycosylation621N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
P31581 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: 00244107A8B01B8C

FASTA27931,490
        10         20         30         40         50         60 
MNLASSACLL LLFLLGIAQA LPVQNEEGHE EGNKEGHGEE GVEEGDEDDF VDFTTRILTS 

        70         80         90        100        110        120 
NNNTDQLLLE GDLVAPTNRN AMKCWYNSCF WKKASNGFVV IPYVISSQYS RGEVATIEGA 

       130        140        150        160        170        180 
MRAFNGRTCI RFVRRTNEYD FISVVSKNGC YSELGRKGGQ QELSLNRGGC MYSGIIQHEL 

       190        200        210        220        230        240 
NHALGFQHEQ TRSDRDSYVR INWQNIIPAS AYNFNKHDTN NLNTPYDYSS IMHYGRDAFS 

       250        260        270 
IAYGRDSITP IPNPNVPIGQ RNGMSRWDIT RSNVLYNCR 

« 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].
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M96171 mRNA. Translation: AAA49439.1.
PIRC48826.
RefSeqNP_001098293.1. NM_001104823.1.
UniGeneOla.4722.

3D structure databases

ProteinModelPortalP31581.
ModBaseSearch...

Protein family/group databases

MEROPSM12.007.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100049452.

Organism-specific databases

CTD100049452.

Phylogenomic databases

eggNOGfiNOG07293.
GeneTreeENSGT00550000074269.
HOVERGENHBG004293.
InParanoidP31581.
OrthoDBEOG4QZ7MW.

Family and domain databases

InterProIPR024079. MetalloPept_cat_dom.
IPR001506. Peptidase_M12A.
IPR006026. Peptidase_Metallo.
[Graphical view]
Gene3DG3DSA:3.40.390.10. G3DSA:3.40.390.10. 1 hit.
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 nameHCE2_ORYLA
AccessionPrimary (citable) accession number: P31581
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families