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P55956 (ASP3_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartic protease 3

EC=3.4.23.-
Gene names
Name:asp-3
ORF Names:H22K11.1
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Secreted.

Sequence similarities

Belongs to the peptidase A1 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAspartyl protease
Hydrolase
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processcell death

Inferred from mutant phenotype. Source: WormBase

determination of adult lifespan

Inferred from mutant phenotype. Source: WormBase

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaspartic-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Propeptide18 – 5538Removed in mature form
PRO_0000025937
Chain56 – 398343Aspartic protease 3
PRO_0000025938

Sites

Active site871 By similarity
Active site2791 By similarity

Amino acid modifications

Glycosylation3211N-linked (GlcNAc...) Ref.3
Disulfide bond100 ↔ 107 By similarity
Disulfide bond313 ↔ 351 By similarity

Sequences

Sequence LengthMass (Da)Tools
P55956 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 4A16251D2CB14121

FASTA39843,413
        10         20         30         40         50         60 
MSGRVFLLLA LVALASAIQR IKLEKRTYTR EQYKFGSIQE HLKAKYVPGY IPNKDAFNEG 

        70         80         90        100        110        120 
LSDYSNAQYY GPVTIGTPPQ NFQVLFDTGS SNLWVPCANC PFGDIACRMH NRFDCKKSSS 

       130        140        150        160        170        180 
CTATGASFEI QYGTGSMKGT VDNDVVCFGH DTTYCTDKNQ GLACATSEPG ITFVAAKFDG 

       190        200        210        220        230        240 
IFGMGWDTIS VNKISQPMDQ IFANSAICKN QLFAFWLSRD ANDITNGGEI TLCETDPNHY 

       250        260        270        280        290        300 
VGNIAWEPLV SEDYWRIKLA SVVIDGTTYT SGPIDSIVDT GTSLLTGPTD VIKKIQHKIG 

       310        320        330        340        350        360 
GIPLFNGEYE VECSKIPSLP NITFNLGGQN FDLQGKDYIL QMSNGNGGST CLSGFMGMDI 

       370        380        390 
PAPAGPLWIL GDVFIGRFYS VFDHGNKRVG FATSRTGK 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[2]"Two-dimensional gel electrophoresis of Caenorhabditis elegans homogenates and identification of protein spots by microsequencing."
Bini L., Heid H., Liberatori S., Geier G., Pallini V., Zwilling R.
Electrophoresis 18:557-562(1997) [PubMed: 9150941] [Abstract]
Cited for: PROTEIN SEQUENCE OF 56-65.
Strain: Bristol N2.
[3]"Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed: 17761667] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-321, MASS SPECTROMETRY.
Strain: Bristol N2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FO081559 Genomic DNA. Translation: CCD72415.1.
PIRT33383.
RefSeqNP_509142.1. NM_076741.4.
UniGeneCel.17775.

3D structure databases

ProteinModelPortalP55956.
SMRP55956. Positions 18-395.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-26574N.
IntActP55956. 1 interaction.
MINTMINT-1064632.
STRINGP55956.

Protein family/group databases

MEROPSA01.A69.

2D gel databases

Siena-2DPAGEP55956.

Proteomic databases

PRIDEP55956.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaH22K11.1; H22K11.1; H22K11.1.
GeneID180947.
KEGGcel:H22K11.1.
NMPDRfig|6239.3.peg.23623.
UCSCH22K11.1. c. elegans.

Organism-specific databases

CTD180947.
WormBaseH22K11.1; CE19495; WBGene00000216; asp-3.

Phylogenomic databases

eggNOGmeNOG05119.
GeneTreeEMGT00050000005383.
HOGENOMHBG590923.
InParanoidP55956.
OMAFYSVFDH.
PhylomeDBP55956.

Gene expression databases

ArrayExpressP55956.

Family and domain databases

InterProIPR001461. Peptidase_A1.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR009007. Peptidase_aspartic_catalytic.
[Graphical view]
Gene3DG3DSA:2.40.70.10. Pept_Aspartc_cat. 2 hits.
KOK01386.
PANTHERPTHR13683. Peptidase_A1. 1 hit.
PfamPF00026. Asp. 1 hit.
[Graphical view]
PRINTSPR00792. PEPSIN.
SUPFAMSSF50630. Pept_Aspartic. 1 hit.
PROSITEPS00141. ASP_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio911692.

Entry information

Entry nameASP3_CAEEL
AccessionPrimary (citable) accession number: P55956
Secondary accession number(s): Q9TXI5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 20, 2002
Last modified: December 14, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

SIMILARITY comments

Index of protein domains and families