ID   ASPG_MACFA              Reviewed;         346 AA.
AC   Q4R6C4;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase;
DE            EC=3.5.1.26 {ECO:0000250|UniProtKB:P20933};
DE   AltName: Full=Aspartylglucosaminidase;
DE            Short=AGA;
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; ORFNames=QtsA-18326;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC       the peptide of asparagine-linked glycoproteins.
CC       {ECO:0000250|UniProtKB:P20933}.
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:0000250|UniProtKB:P20933};
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 {ECO:0000250}.
CC   -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC       activates the enzyme. The N-terminal residue of the beta subunit is
CC       responsible for the nucleophile hydrolase activity.
CC       {ECO:0000250|UniProtKB:P20933}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P20933}.
CC   -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR   EMBL; AB169261; BAE01351.1; -; mRNA.
DR   RefSeq; NP_001271601.1; NM_001284672.1.
DR   AlphaFoldDB; Q4R6C4; -.
DR   SMR; Q4R6C4; -.
DR   STRING; 9541.XP_005556411.1; -.
DR   MEROPS; T02.001; -.
DR   PRIDE; Q4R6C4; -.
DR   GeneID; 101866403; -.
DR   CTD; 175; -.
DR   eggNOG; KOG1593; Eukaryota.
DR   OrthoDB; 1487354at2759; -.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043405"
FT   CHAIN           206..346
FT                   /note="Glycosylasparaginase beta chain"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000043406"
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        308
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;  37065 MW;  98174510534A2FB5 CRC64;
     MARKSKLPLL LVPLLLCQAL VRCSSPLPLV LNTWPFKNAT EAAWRALASG GSALDAVESG
     CAMCETEQCG GSVGFGGSPD ELGETTLDAM IMEGTTMDVG AVGDLRRIKN AIGVARKVLE
     HTTHTLLVGE SATKFAESMG FVNEDLSTSA SQALHSDWLA RNCQPNYWRN VVPDPSKYCG
     PYKPLGILKQ DIPIHKETED NRGHDTIGMV VIHKTGRIAA GTSTNGIKFK IHGRVGDSPV
     PGAGAYADDT AGAAAATGEG DILMRFLPSY QAVEYMRGGE DPTIACQKVI SRIQKYFPEF
     FGAVICANVT GSYGAACNKL STFTQFSFMV YNSEKNQPTE EKVDCI