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Protein

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

Gene

Aga

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

Functioni

Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.2 Publications

Catalytic activityi

N4-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate.2 Publications

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

Keywordsi

Molecular functionHydrolase, 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:3.5.1.262 Publications)
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi1309646 Aga

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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...) asparagine1 Publication1
Disulfide bondi64 ↔ 69By similarity
Glycosylationi149N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi163 ↔ 179By similarity
Disulfide bondi285 ↔ 305By similarity
Glycosylationi307N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi316 ↔ 344By similarity

Post-translational modificationi

N-glycosylated.1 Publication
Cleaved into an alpha and beta chain by autocatalysis; this activates the enzyme (PubMed:2775174). The N-terminal residue of the beta subunit is responsible for the nucleophile hydrolase activity (By similarity).By similarity1 Publication

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.By similarity

GO - Molecular functioni

  • protein self-association Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000000120

Structurei

3D structure databases

ProteinModelPortaliP30919
SMRiP30919
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
OMAiNIENHDT
OrthoDBiEOG091G0L36
PhylomeDBiP30919
TreeFamiTF300756

Family and domain databases

InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000246 Peptidase_T2
PANTHERiPTHR10188 PTHR10188, 1 hit
PfamiView protein in Pfam
PF01112 Asparaginase_2, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiASPG_RAT
AccessioniPrimary (citable) accession number: P30919
Secondary accession number(s): Q4G065
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: December 6, 2005
Last modified: May 23, 2018
This is version 126 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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