ASGL1_DROME
ID ASGL1_DROME Reviewed; 332 AA.
AC Q9VXT7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable isoaspartyl peptidase/L-asparaginase CG7860;
DE EC=3.4.19.5;
DE EC=3.5.1.1;
DE AltName: Full=Beta-aspartyl-peptidase CG7860;
DE AltName: Full=Isoaspartyl dipeptidase CG7860;
DE AltName: Full=L-asparagine amidohydrolase CG7860;
DE Contains:
DE RecName: Full=Probable isoaspartyl peptidase/L-asparaginase CG7860 alpha chain;
DE Contains:
DE RecName: Full=Probable isoaspartyl peptidase/L-asparaginase CG7860 beta chain;
DE Flags: Precursor;
GN ORFNames=CG7860;
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]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
CC -!- FUNCTION: Has both L-asparaginase and beta-aspartyl peptidase activity.
CC Does not have aspartylglucosaminidase activity and is inactive toward
CC GlcNAc-L-Asn. Likewise, has no activity toward glutamine.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5; Evidence={ECO:0000250|UniProtKB:Q7L266};
CC -!- SUBUNIT: Heterodimer of an alpha and beta chain produced by
CC autocleavage. {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. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AE014298; AAF48471.1; -; Genomic_DNA.
DR EMBL; AY061292; AAL28840.1; -; mRNA.
DR RefSeq; NP_001285275.1; NM_001298346.1.
DR RefSeq; NP_573039.1; NM_132811.3.
DR AlphaFoldDB; Q9VXT7; -.
DR SMR; Q9VXT7; -.
DR BioGRID; 58839; 3.
DR IntAct; Q9VXT7; 1.
DR STRING; 7227.FBpp0073861; -.
DR PaxDb; Q9VXT7; -.
DR DNASU; 32488; -.
DR EnsemblMetazoa; FBtr0074045; FBpp0073861; FBgn0030653.
DR EnsemblMetazoa; FBtr0339691; FBpp0308748; FBgn0030653.
DR GeneID; 32488; -.
DR KEGG; dme:Dmel_CG7860; -.
DR UCSC; CG7860-RA; d. melanogaster.
DR FlyBase; FBgn0030653; CG7860.
DR VEuPathDB; VectorBase:FBgn0030653; -.
DR eggNOG; KOG1592; Eukaryota.
DR GeneTree; ENSGT00950000183045; -.
DR HOGENOM; CLU_021603_1_2_1; -.
DR InParanoid; Q9VXT7; -.
DR OMA; RRMAWGY; -.
DR OrthoDB; 797598at2759; -.
DR PhylomeDB; Q9VXT7; -.
DR Reactome; R-DME-8964208; Phenylalanine metabolism.
DR BioGRID-ORCS; 32488; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 32488; -.
DR PRO; PR:Q9VXT7; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0030653; Expressed in embryonic/larval hemocyte (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q9VXT7; baseline and differential.
DR Genevisible; Q9VXT7; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0033345; P:asparagine catabolic process via L-aspartate; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04702; ASRGL1_like; 1.
DR InterPro; IPR033844; ASRGL1_meta.
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; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..187
FT /note="Probable isoaspartyl peptidase/L-asparaginase CG7860
FT alpha chain"
FT /id="PRO_0000420567"
FT CHAIN 188..332
FT /note="Probable isoaspartyl peptidase/L-asparaginase CG7860
FT beta chain"
FT /id="PRO_0000420568"
FT ACT_SITE 188
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 216..219
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 239..242
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 332 AA; 34861 MW; B4BA4AC9A3521CBB CRC64;
MPRPVLLIHG GAGDISDSRI AGKFAGIKQA LRSAWGLLSP DNGSGGGSAL DAVEAAVRSM
ELDENFNAGY GSCLNTSGQV ELEASLMEGR DLRAGCITLL RDVMHPITVA RRLMEKQRHT
FLGGAAAQEL ALATGSERLQ PGALVTEGAR LTLKEFEDQV AQGKDPFFAR TELTDDKPVP
KTDPSGETVG AVAMDASGQI VVGTSTGGIT GKWPGRIGDT PILGSGTYAD NCRGGVSTTG
HGETLMRYNL AQRILSAMEY QGLSAQAAAD KECREMTKRL GGTGGAIVVG HSGDLGISFT
SRRMAWGYVQ DGTIFYGIEG QVVHQEPFTL ST
