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Reviewed, UniProtKB/Swiss-Prot P30918 (ASPG_PIG)

Last modified June 16, 2009. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
    N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase
    EC=3.5.1.26
Alternative name(s):
    Glycosylasparaginase
    Aspartylglucosaminidase
      Short name=AGA
    N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
    1- Recommended name:
            Glycosylasparaginase alpha chain
    2- Recommended name:
            Glycosylasparaginase beta chain
Gene names
Name: AGA
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length34 AA.
Sequence statusFragments.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

Catalytic activity

N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.

Subunit structure

Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers.

Subcellular location

Lysosome.

Sequence similarities

Belongs to the Ntn-hydrolase family.

Ontologies

Keywords
   Cellular componentLysosome
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentlysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionN4-(beta-N-acetylglucosaminyl)-L-asparaginase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›17›17Glycosylasparaginase alpha chain
PRO_0000002337
Chain18 – ›34›17Glycosylasparaginase beta chain
PRO_0000002338

Experimental info

Non-adjacent residues17 – 182
Non-terminal residue341

Sequences

Sequence LengthMass (Da)Tools
P30918-1 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: A527053E8DBA8B56

FASTA343,621
        10         20         30 
SXPLPLIVNT WPFKXATTIG MVVIHLKGYT AAGT 

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References

[1]"Comparison of liver glycosylasparaginases from six vertebrates."
Tollersrud O.-K., Aronson N.N. Jr.
Biochem. J. 282:891-897(1992) [PubMed: 1554372] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

3D structure databases

ModBaseSearch...

Phylogenomic databases

HOVERGENP30918.

Enzyme and pathway databases

BRENDA3.5.1.26. 249.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameASPG_PIG
AccessionPrimary (citable) accession number: P30918
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: June 16, 2009
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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