ASPG1_DROME
ID ASPG1_DROME Reviewed; 393 AA.
AC Q8MR45; A1Z7W5; A1Z7W6; Q6NN89;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Putative N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase CG1827;
DE EC=3.5.1.26;
DE AltName: Full=Aspartylglucosaminidase {ECO:0000250|UniProtKB:P20933};
DE Short=AGA {ECO:0000250|UniProtKB:P20933};
DE AltName: Full=Glycosylasparaginase {ECO:0000250|UniProtKB:P20933};
DE AltName: Full=N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase {ECO:0000250|UniProtKB:P20933};
DE Contains:
DE RecName: Full=Glycosylasparaginase alpha chain {ECO:0000250|UniProtKB:P20933};
DE Contains:
DE RecName: Full=Glycosylasparaginase beta chain {ECO:0000250|UniProtKB:P20933};
DE Flags: Precursor;
GN ORFNames=CG1827;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:AAF58918.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF58918.5}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAM52645.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM52645.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAR96196.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) 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 -!- 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:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR96196.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58918.5; -; Genomic_DNA.
DR EMBL; AY122133; AAM52645.1; -; mRNA.
DR EMBL; BT011404; AAR96196.1; ALT_SEQ; mRNA.
DR RefSeq; NP_610504.4; NM_136660.3.
DR AlphaFoldDB; Q8MR45; -.
DR SMR; Q8MR45; -.
DR STRING; 7227.FBpp0271751; -.
DR MEROPS; T02.001; -.
DR GlyGen; Q8MR45; 2 sites.
DR PaxDb; Q8MR45; -.
DR PRIDE; Q8MR45; -.
DR DNASU; 35989; -.
DR EnsemblMetazoa; FBtr0339392; FBpp0308484; FBgn0033431.
DR GeneID; 35989; -.
DR KEGG; dme:Dmel_CG1827; -.
DR UCSC; CG1827-RB; d. melanogaster.
DR UCSC; CG1827-RC; d. melanogaster.
DR FlyBase; FBgn0033431; CG1827.
DR VEuPathDB; VectorBase:FBgn0033431; -.
DR eggNOG; KOG1593; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_0_0_1; -.
DR InParanoid; Q8MR45; -.
DR OMA; PDENCET; -.
DR OrthoDB; 1487354at2759; -.
DR PhylomeDB; Q8MR45; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 35989; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 35989; -.
DR PRO; PR:Q8MR45; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033431; Expressed in seminal fluid secreting gland and 24 other tissues.
DR Genevisible; Q8MR45; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0003948; F:N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
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; Protease;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..242
FT /note="Glycosylasparaginase alpha chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384129"
FT CHAIN 243..393
FT /note="Glycosylasparaginase beta chain"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT /id="PRO_0000384130"
FT ACT_SITE 243
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT BINDING 271..274
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 294..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 97..102
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 196..212
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT DISULFID 354..381
FT /evidence="ECO:0000250|UniProtKB:P20933"
FT CONFLICT 370
FT /note="A -> G (in Ref. 4; AAR96196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 393 AA; 42240 MW; 993979A39BF9129C CRC64;
MRRHLRASLW ILCLATMAFS ILAAVNTSPK PTLTSAFSGK AGTTAVKANK TTGELLPMVI
NTWNFTAANV LAWRILKQSK GGLRQTRNAV VEGCSKCEKL QCDRTVGYGG SPDELGETTL
DAMVMDGATM DVGAVAGLRR IKDAIKVARH VLEHTQHTML VGDAASAFAN AMGFESESLV
TPESKDMWLQ WTAENCQPNF WKNVHPDPKV SCGPYKPRPT PLTRWKEDRA RNEYEIGRKN
HDTIGMIAID VESNIHAGTS TNGARHKIPG RVGDSPIPGA GAYADNEVGA AVATGDGDVM
MRFLPSLLAV ETMRAGKPPA EAAQEGLRRI LKHHKDFMGA LIAVDRLGNY GAACYGLAEF
PFMVSSPAGA DGPTRLETVK CIGGQDKVNI VAL
