ASPG_MOUSE
ID ASPG_MOUSE Reviewed; 346 AA.
AC Q64191;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26 {ECO:0000269|PubMed:8586423};
DE AltName: Full=Aspartylglucosaminidase {ECO:0000303|PubMed:8586423};
DE Short=AGA {ECO:0000303|PubMed:8586423};
DE AltName: Full=Glycosylasparaginase;
DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase;
DE Contains:
DE RecName: Full=Glycosylasparaginase alpha chain;
DE Contains:
DE RecName: Full=Glycosylasparaginase beta chain;
DE Flags: Precursor;
GN Name=Aga;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, GLYCOSYLATION,
RP AND PROTEOLYTIC CLEAVAGE.
RX PubMed=8586423; DOI=10.1006/geno.1995.9881;
RA Tenhunen K., Laan M., Manninen T., Palotie A., Peltonen L., Jalanko A.;
RT "Molecular cloning, chromosomal assignment, and expression of the mouse
RT aspartylglucosaminidase gene.";
RL Genomics 30:244-250(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins.
CC {ECO:0000269|PubMed:8586423}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine = H(+)
CC + L-aspartate + N-acetyl-beta-D-glucosaminylamine;
CC Xref=Rhea:RHEA:11544, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15947, ChEBI:CHEBI:29991, ChEBI:CHEBI:58080; EC=3.5.1.26;
CC Evidence={ECO:0000269|PubMed:8586423};
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000250|UniProtKB:P20933}.
CC -!- SUBCELLULAR LOCATION: Lysosome.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme (PubMed:8586423). The N-terminal residue of the
CC beta subunit is responsible for the nucleophile hydrolase activity.
CC {ECO:0000250|UniProtKB:P20933, ECO:0000269|PubMed:8586423}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20933}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; S81393; AAB36101.1; -; mRNA.
DR CCDS; CCDS22304.1; -.
DR RefSeq; NP_001005847.1; NM_001005847.2.
DR AlphaFoldDB; Q64191; -.
DR SMR; Q64191; -.
DR BioGRID; 198019; 11.
DR STRING; 10090.ENSMUSP00000033920; -.
DR MEROPS; T02.001; -.
DR GlyGen; Q64191; 2 sites.
DR PhosphoSitePlus; Q64191; -.
DR CPTAC; non-CPTAC-3449; -.
DR EPD; Q64191; -.
DR MaxQB; Q64191; -.
DR PaxDb; Q64191; -.
DR PeptideAtlas; Q64191; -.
DR PRIDE; Q64191; -.
DR ProteomicsDB; 283187; -.
DR Antibodypedia; 28679; 163 antibodies from 22 providers.
DR DNASU; 11593; -.
DR Ensembl; ENSMUST00000033920; ENSMUSP00000033920; ENSMUSG00000031521.
DR GeneID; 11593; -.
DR KEGG; mmu:11593; -.
DR UCSC; uc009lrz.2; mouse.
DR CTD; 175; -.
DR MGI; MGI:104873; Aga.
DR VEuPathDB; HostDB:ENSMUSG00000031521; -.
DR eggNOG; KOG1593; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_0_0_1; -.
DR InParanoid; Q64191; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; Q64191; -.
DR TreeFam; TF300756; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 11593; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Aga; mouse.
DR PRO; PR:Q64191; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q64191; protein.
DR Bgee; ENSMUSG00000031521; Expressed in vault of skull and 215 other tissues.
DR ExpressionAtlas; Q64191; baseline and differential.
DR Genevisible; Q64191; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IDA:MGI.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IDA:MGI.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; ISO:MGI.
DR GO; GO:0006517; P:protein deglycosylation; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Protease; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT CHAIN 24..205
FT /note="Glycosylasparaginase alpha chain"
FT /id="PRO_0000002335"
FT CHAIN 206..346
FT /note="Glycosylasparaginase beta chain"
FT /id="PRO_0000002336"
FT ACT_SITE 206
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 234..237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 257..260
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 64..69
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 163..179
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 286..306
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 317..345
FT /evidence="ECO:0000250|UniProtKB:P20933"
SQ SEQUENCE 346 AA; 37022 MW; 75464327B740D10D CRC64;
MERKSNLSLL LLLLVLGMPL VRGSSPLPLV VNTWPFKNAT EAAWWTLLSG GSALDAVENG
CAVCEKEQCD GTVGFGGSPD EGGETTLDAM IMDGTAMDVG AVGGLRRIKN AIGVARRVLE
HTTHTLLVGD SATKFAESMG FTNEDLSTKT SRDLHSDWLS RNCQPNYWRN VIPDPSKYCG
PYKPSGFLKQ SISPHKEEVD IHSHDTIGMV VIHKTGHTAA GTSTNGIKFK IPGRVGDSPI
PGAGAYADDT AGAAAATGDG DTLLRFLPSY QAVEYMRGGD DPAIACQKVI LRIQKYYPNF
FGAVICASVN GSYGAACNKL PTFTQFSFMV SNSLHNEPTE KKVDCI
