NTAQ1_DROME
ID NTAQ1_DROME Reviewed; 205 AA.
AC Q7K2Y9;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Protein N-terminal glutamine amidohydrolase;
DE EC=3.5.1.122 {ECO:0000250|UniProtKB:Q80WB5};
DE AltName: Full=Protein NH2-terminal glutamine deamidase;
DE Short=N-terminal Gln amidase;
DE Short=Nt(Q)-amidase;
DE AltName: Full=Protein tungus;
GN Name=tun; ORFNames=CG8253;
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).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=12593794; DOI=10.1016/s0960-9822(03)00064-2;
RA Dubnau J., Chiang A.-S., Grady L., Barditch J., Gossweiler S., McNeil J.,
RA Smith P., Buldoc F., Scott R., Certa U., Broger C., Tully T.;
RT "The staufen/pumilio pathway is involved in Drosophila long-term memory.";
RL Curr. Biol. 13:286-296(2003).
CC -!- FUNCTION: Mediates the side-chain deamidation of N-terminal glutamine
CC residues to glutamate, an important step in N-end rule pathway of
CC protein degradation. Conversion of the resulting N-terminal glutamine
CC to glutamate renders the protein susceptible to arginylation,
CC polyubiquitination and degradation as specified by the N-end rule. Does
CC not act on substrates with internal or C-terminal glutamine and does
CC not act on non-glutamine residues in any position.
CC {ECO:0000250|UniProtKB:Q80WB5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-terminal L-glutaminyl-[protein] = N-terminal L-
CC glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:50680, Rhea:RHEA-
CC COMP:12668, Rhea:RHEA-COMP:12777, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:64721, ChEBI:CHEBI:64722;
CC EC=3.5.1.122; Evidence={ECO:0000250|UniProtKB:Q80WB5};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q96HA8}.
CC -!- DISRUPTION PHENOTYPE: Defects in long term memory after olfactory
CC learning. {ECO:0000269|PubMed:12593794}.
CC -!- SIMILARITY: Belongs to the NTAQ1 family. {ECO:0000305}.
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DR EMBL; AE013599; AAF58102.2; -; Genomic_DNA.
DR EMBL; AY060439; AAL25478.1; -; mRNA.
DR RefSeq; NP_001246351.1; NM_001259422.2.
DR RefSeq; NP_001246352.1; NM_001259423.2.
DR RefSeq; NP_001286468.1; NM_001299539.1.
DR RefSeq; NP_611061.1; NM_137217.3.
DR AlphaFoldDB; Q7K2Y9; -.
DR SMR; Q7K2Y9; -.
DR BioGRID; 62471; 2.
DR IntAct; Q7K2Y9; 3.
DR STRING; 7227.FBpp0300971; -.
DR PaxDb; Q7K2Y9; -.
DR DNASU; 36743; -.
DR EnsemblMetazoa; FBtr0087287; FBpp0086423; FBgn0034046.
DR EnsemblMetazoa; FBtr0308814; FBpp0300971; FBgn0034046.
DR EnsemblMetazoa; FBtr0308815; FBpp0300972; FBgn0034046.
DR EnsemblMetazoa; FBtr0340013; FBpp0309027; FBgn0034046.
DR GeneID; 36743; -.
DR KEGG; dme:Dmel_CG8253; -.
DR UCSC; CG8253-RA; d. melanogaster.
DR CTD; 36743; -.
DR FlyBase; FBgn0034046; tun.
DR VEuPathDB; VectorBase:FBgn0034046; -.
DR eggNOG; KOG3261; Eukaryota.
DR GeneTree; ENSGT00390000014398; -.
DR HOGENOM; CLU_091083_1_0_1; -.
DR InParanoid; Q7K2Y9; -.
DR OMA; GWGTVYS; -.
DR OrthoDB; 1337506at2759; -.
DR PhylomeDB; Q7K2Y9; -.
DR BRENDA; 3.5.1.122; 1994.
DR BioGRID-ORCS; 36743; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Zasp52; fly.
DR GenomeRNAi; 36743; -.
DR PRO; PR:Q7K2Y9; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034046; Expressed in egg cell and 19 other tissues.
DR ExpressionAtlas; Q7K2Y9; baseline and differential.
DR Genevisible; Q7K2Y9; DM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008418; F:protein-N-terminal asparagine amidohydrolase activity; IEA:InterPro.
DR GO; GO:0070773; F:protein-N-terminal glutamine amidohydrolase activity; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; IBA:GO_Central.
DR Gene3D; 3.10.620.10; -; 1.
DR InterPro; IPR037132; N_Gln_amidohydro_ab_roll_sf.
DR InterPro; IPR039733; NTAQ1.
DR InterPro; IPR023128; Prot_N_Gln_amidohydro_ab_roll.
DR PANTHER; PTHR13035; PTHR13035; 1.
DR Pfam; PF09764; Nt_Gln_amidase; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Reference proteome.
FT CHAIN 1..205
FT /note="Protein N-terminal glutamine amidohydrolase"
FT /id="PRO_0000381826"
FT ACT_SITE 20
FT /evidence="ECO:0000250"
FT ACT_SITE 74
FT /evidence="ECO:0000250"
FT ACT_SITE 90
FT /evidence="ECO:0000250"
SQ SEQUENCE 205 AA; 24006 MW; 4CA5F5E7F23790F5 CRC64;
MTTDFLFPKI SDCSYVSCYC EENVWKLCEQ VKRTRPEELS KCYAVFVSNE GRTVPLWRQK
AGRGDDQVVI WDYHVFFIHN PLLNRCLVFD LDTTLPFPTY FHKYVTETFR SDLALRPEHH
RFFRVIPADT YLIEFSSDRR HMRRPDGSWI KPPPSYPPIL SNSNMHCLGD FICMSAGKGP
GSVYSLSEFV QNFYKSPHVM AQNNK
