ASPG_CAEEL
ID ASPG_CAEEL Reviewed; 363 AA.
AC Q21697;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26;
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 ORFNames=R04B3.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins. {ECO:0000250}.
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 -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; FO081538; CCD72284.1; -; Genomic_DNA.
DR PIR; T30965; T30965.
DR RefSeq; NP_508448.1; NM_076047.4.
DR AlphaFoldDB; Q21697; -.
DR SMR; Q21697; -.
DR BioGRID; 45494; 2.
DR IntAct; Q21697; 1.
DR STRING; 6239.R04B3.2; -.
DR MEROPS; T02.001; -.
DR EPD; Q21697; -.
DR PaxDb; Q21697; -.
DR PeptideAtlas; Q21697; -.
DR EnsemblMetazoa; R04B3.2.1; R04B3.2.1; WBGene00019867.
DR GeneID; 180550; -.
DR KEGG; cel:CELE_R04B3.2; -.
DR UCSC; R04B3.2; c. elegans.
DR CTD; 180550; -.
DR WormBase; R04B3.2; CE28745; WBGene00019867; -.
DR eggNOG; KOG1593; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_0_0_1; -.
DR InParanoid; Q21697; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; Q21697; -.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR PRO; PR:Q21697; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00019867; Expressed in embryo and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IBA:GO_Central.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006517; P:protein deglycosylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Autocatalytic cleavage; Disulfide bond; Glycoprotein; Hydrolase; Lysosome;
KW Protease; Reference proteome; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..211
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002343"
FT CHAIN 212..363
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002344"
FT ACT_SITE 212
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 240..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 262..265
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 161..177
FT /evidence="ECO:0000250"
FT DISULFID 322..346
FT /evidence="ECO:0000250"
SQ SEQUENCE 363 AA; 39359 MW; 4A34D1450AAB1BC7 CRC64;
MRRFYIFLLL IPYINGTIND DSLPMVITTW GSDGFKKATK NAVDATLLGG RMFGLVEGLS
TCEALQCDTT VGYGGSPDEN GETCLDSLVI DADGMRVGAV ANLHRIRDAA RVAWGVMNFT
KHTLLVGESA TQFAKTLGFK EEDLSTEETK SWISKWKTEK CQPNFWKNVS PDPSSSCGPY
KTNPLTKSMR YYSLVNQSDE AGYLVEKTNH DTIGMVVRDT ENIFSAGTSS NGARFKIPGR
VGDSPIPGAG AYANKFGGAA ATGDGDVMMR FLPSFFAVTQ MELGTKPSKA AYKAITRILK
VFPKFSGAVV AMNVKGRIGA SCANINKFGY NVAFQNGTVV TYSISCLKEV NSLKYLKEGI
EFA
