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Protein

N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase

Gene

Aga

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei205NucleophileBy similarity1

GO - Molecular functioni

  • N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Source: RGD
  • peptidase activity Source: UniProtKB-KW
  • protein self-association Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease

Enzyme and pathway databases

ReactomeiR-RNO-6798695. Neutrophil degranulation.

Protein family/group databases

MEROPSiT02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase (EC:3.5.1.26)
Alternative name(s):
Aspartylglucosaminidase
Short name:
AGA
Glycosylasparaginase
N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase
Cleaved into the following 2 chains:
Gene namesi
Name:Aga
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi1309646. Aga.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: Ensembl
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • lysosome Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Lysosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 231 PublicationAdd BLAST23
ChainiPRO_000004457124 – 204Glycosylasparaginase alpha chainAdd BLAST181
ChainiPRO_0000044572205 – 345Glycosylasparaginase beta chainAdd BLAST141

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi64 ↔ 69By similarity
Glycosylationi149N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi163 ↔ 179By similarity
Disulfide bondi285 ↔ 305By similarity
Glycosylationi307N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi316 ↔ 344By similarity

Post-translational modificationi

Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme. The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).By similarity

Keywords - PTMi

Autocatalytic cleavage, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP30919.
PRIDEiP30919.

Expressioni

Gene expression databases

BgeeiENSRNOG00000000108.
GenevisibleiP30919. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000120.

Structurei

3D structure databases

ProteinModelPortaliP30919.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni233 – 236Substrate bindingBy similarity4
Regioni256 – 259Substrate bindingBy similarity4

Sequence similaritiesi

Belongs to the Ntn-hydrolase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1593. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174614.
HOVERGENiHBG004289.
InParanoidiP30919.
KOiK01444.
OMAiKFFGAVI.
OrthoDBiEOG091G0L36.
PhylomeDBiP30919.
TreeFamiTF300756.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 2 hits.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P30919-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARKWNLPFL LLPLVLGIPL VRGSNPLPLV VNTWPFKNAT EAAWWTLVSG
60 70 80 90 100
GSALDAVEKG CAMCEKEQCG GTVGFGGSPD EVGETTLDAM IMDGTAMDVG
110 120 130 140 150
AVGGLRRIKN AIGVARKVLE HTTHTLLVGD SATKFAVSMG FTSEDLSTNT
160 170 180 190 200
SRALHSDWLS RNCQPNYWRN VIPDPSKYCG PYKPPDFLEQ NNRAHKEVDI
210 220 230 240 250
HSHDTIGMVV IHKTGHTAAG TSTNGLKFKI PGRVGDSPIP GAGAYADDMA
260 270 280 290 300
GAAAATGDGD TLLRFLPSYQ AVEYMRGGDD PARACQKVIS RIQKYYPKFF
310 320 330 340
GAVICANVTG SYGAACNRLP TFTQFSFMVY NSLHNQAIEE KVDCM
Length:345
Mass (Da):37,167
Last modified:December 6, 2005 - v2
Checksum:iBC809F2116B65871
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098718 mRNA. Translation: AAH98718.1.
PIRiS04228.
S04229.
S57865.
RefSeqiNP_001026811.1. NM_001031641.1.
UniGeneiRn.104649.

Genome annotation databases

EnsembliENSRNOT00000000120; ENSRNOP00000000120; ENSRNOG00000000108.
GeneIDi290923.
KEGGirno:290923.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC098718 mRNA. Translation: AAH98718.1.
PIRiS04228.
S04229.
S57865.
RefSeqiNP_001026811.1. NM_001031641.1.
UniGeneiRn.104649.

3D structure databases

ProteinModelPortaliP30919.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000120.

Protein family/group databases

MEROPSiT02.001.

Proteomic databases

PaxDbiP30919.
PRIDEiP30919.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000000120; ENSRNOP00000000120; ENSRNOG00000000108.
GeneIDi290923.
KEGGirno:290923.

Organism-specific databases

CTDi175.
RGDi1309646. Aga.

Phylogenomic databases

eggNOGiKOG1593. Eukaryota.
COG1446. LUCA.
GeneTreeiENSGT00530000063034.
HOGENOMiHOG000174614.
HOVERGENiHBG004289.
InParanoidiP30919.
KOiK01444.
OMAiKFFGAVI.
OrthoDBiEOG091G0L36.
PhylomeDBiP30919.
TreeFamiTF300756.

Enzyme and pathway databases

ReactomeiR-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP30919.

Gene expression databases

BgeeiENSRNOG00000000108.
GenevisibleiP30919. RN.

Family and domain databases

InterProiIPR029055. Ntn_hydrolases_N.
IPR000246. Peptidase_T2.
[Graphical view]
PANTHERiPTHR10188. PTHR10188. 2 hits.
PfamiPF01112. Asparaginase_2. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiASPG_RAT
AccessioniPrimary (citable) accession number: P30919
Secondary accession number(s): Q4G065
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 6, 2005
Last modified: November 30, 2016
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.