ASPG_RAT
ID ASPG_RAT Reviewed; 345 AA.
AC P30919; Q4G065;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=N(4)-(Beta-N-acetylglucosaminyl)-L-asparaginase;
DE EC=3.5.1.26 {ECO:0000269|PubMed:1554372, ECO:0000269|PubMed:2775174};
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;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PROTEIN SEQUENCE OF 24-41 AND 205-226, FUNCTION, CATALYTIC ACTIVITY,
RP PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION.
RC TISSUE=Liver;
RX PubMed=2775174; DOI=10.1042/bj2600101;
RA Tollersrud O.-K., Aronson N.N. Jr.;
RT "Purification and characterization of rat liver glycosylasparaginase.";
RL Biochem. J. 260:101-108(1989).
RN [3]
RP SEQUENCE REVISION, FUNCTION, AND CATALYTIC ACTIVITY.
RC TISSUE=Liver;
RX PubMed=1554372; DOI=10.1042/bj2820891;
RA Tollersrud O.-K., Aronson N.N. Jr.;
RT "Comparison of liver glycosylasparaginases from six vertebrates.";
RL Biochem. J. 282:891-897(1992).
CC -!- FUNCTION: Cleaves the GlcNAc-Asn bond which joins oligosaccharides to
CC the peptide of asparagine-linked glycoproteins.
CC {ECO:0000269|PubMed:1554372, ECO:0000269|PubMed:2775174}.
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:1554372, ECO:0000269|PubMed:2775174};
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: N-glycosylated. {ECO:0000269|PubMed:2775174}.
CC -!- PTM: Cleaved into an alpha and beta chain by autocatalysis; this
CC activates the enzyme (PubMed:2775174). The N-terminal residue of the
CC beta subunit is responsible for the nucleophile hydrolase activity (By
CC similarity). {ECO:0000250|UniProtKB:P20933,
CC ECO:0000269|PubMed:2775174}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; BC098718; AAH98718.1; -; mRNA.
DR PIR; S04228; S04228.
DR PIR; S04229; S04229.
DR PIR; S57865; S57865.
DR RefSeq; NP_001026811.1; NM_001031641.1.
DR AlphaFoldDB; P30919; -.
DR SMR; P30919; -.
DR STRING; 10116.ENSRNOP00000000120; -.
DR MEROPS; T02.001; -.
DR GlyGen; P30919; 3 sites.
DR iPTMnet; P30919; -.
DR jPOST; P30919; -.
DR PaxDb; P30919; -.
DR PRIDE; P30919; -.
DR Ensembl; ENSRNOT00000000120; ENSRNOP00000000120; ENSRNOG00000000108.
DR GeneID; 290923; -.
DR KEGG; rno:290923; -.
DR CTD; 175; -.
DR RGD; 1309646; Aga.
DR eggNOG; KOG1593; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_0_0_1; -.
DR InParanoid; P30919; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; P30919; -.
DR TreeFam; TF300756; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P30919; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000000108; Expressed in pancreas and 19 other tissues.
DR Genevisible; P30919; RN.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005764; C:lysosome; IDA:RGD.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; IDA:RGD.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0043621; F:protein self-association; IDA:RGD.
DR GO; GO:0006517; P:protein deglycosylation; ISO:RGD.
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; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Lysosome; Protease; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:2775174"
FT CHAIN 24..204
FT /note="Glycosylasparaginase alpha chain"
FT /id="PRO_0000044571"
FT CHAIN 205..345
FT /note="Glycosylasparaginase beta chain"
FT /id="PRO_0000044572"
FT ACT_SITE 205
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 233..236
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 256..259
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT CARBOHYD 38
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2775174"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
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 285..305
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 316..344
FT /evidence="ECO:0000250|UniProtKB:P20933"
SQ SEQUENCE 345 AA; 37167 MW; BC809F2116B65871 CRC64;
MARKWNLPFL LLPLVLGIPL VRGSNPLPLV VNTWPFKNAT EAAWWTLVSG GSALDAVEKG
CAMCEKEQCG GTVGFGGSPD EVGETTLDAM IMDGTAMDVG AVGGLRRIKN AIGVARKVLE
HTTHTLLVGD SATKFAVSMG FTSEDLSTNT SRALHSDWLS RNCQPNYWRN VIPDPSKYCG
PYKPPDFLEQ NNRAHKEVDI HSHDTIGMVV IHKTGHTAAG TSTNGLKFKI PGRVGDSPIP
GAGAYADDMA GAAAATGDGD TLLRFLPSYQ AVEYMRGGDD PARACQKVIS RIQKYYPKFF
GAVICANVTG SYGAACNRLP TFTQFSFMVY NSLHNQAIEE KVDCM
