GLNA2_DROME
ID GLNA2_DROME Reviewed; 369 AA.
AC P20478; Q8IR90; Q95SM4; Q9VYZ0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Glutamine synthetase 2 cytoplasmic;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase 2;
GN Name=Gs2; ORFNames=CG1743;
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 (ISOFORM C).
RX PubMed=1969491; DOI=10.1016/0022-2836(90)90301-2;
RA Caizzi R., Bozzetti M.P., Caggese C., Ritossa F.;
RT "Homologous nuclear genes encode cytoplasmic and mitochondrial glutamine
RT synthetase in Drosophila melanogaster.";
RL J. Mol. Biol. 212:17-26(1990).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 229-369.
RC STRAIN=Berkeley; TISSUE=Head;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC -!- SUBUNIT: Homooctamer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C;
CC IsoId=P20478-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P20478-2; Sequence=VSP_010623;
CC Name=B;
CC IsoId=P20478-3; Sequence=VSP_010624;
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28249.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X52759; CAA36970.1; -; mRNA.
DR EMBL; AE014298; AAF48043.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09632.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65314.1; -; Genomic_DNA.
DR EMBL; AY060701; AAL28249.1; ALT_INIT; mRNA.
DR PIR; S09108; AJFF2C.
DR RefSeq; NP_001285122.1; NM_001298193.1. [P20478-1]
DR RefSeq; NP_001285123.1; NM_001298194.1. [P20478-1]
DR RefSeq; NP_511123.2; NM_078568.3. [P20478-1]
DR RefSeq; NP_727525.1; NM_167284.2. [P20478-3]
DR RefSeq; NP_996408.1; NM_206685.2. [P20478-2]
DR PDB; 7CPR; X-ray; 2.12 A; A/B/C/D/E/F/G/H/I/J=3-369.
DR PDBsum; 7CPR; -.
DR AlphaFoldDB; P20478; -.
DR SMR; P20478; -.
DR BioGRID; 58498; 1.
DR IntAct; P20478; 27.
DR STRING; 7227.FBpp0073344; -.
DR PaxDb; P20478; -.
DR DNASU; 32087; -.
DR EnsemblMetazoa; FBtr0073494; FBpp0073344; FBgn0001145. [P20478-3]
DR EnsemblMetazoa; FBtr0073495; FBpp0073345; FBgn0001145. [P20478-1]
DR EnsemblMetazoa; FBtr0073496; FBpp0089332; FBgn0001145. [P20478-2]
DR EnsemblMetazoa; FBtr0343562; FBpp0310163; FBgn0001145. [P20478-1]
DR EnsemblMetazoa; FBtr0343563; FBpp0310164; FBgn0001145. [P20478-1]
DR GeneID; 32087; -.
DR KEGG; dme:Dmel_CG1743; -.
DR CTD; 32087; -.
DR FlyBase; FBgn0001145; Gs2.
DR VEuPathDB; VectorBase:FBgn0001145; -.
DR eggNOG; KOG0683; Eukaryota.
DR GeneTree; ENSGT00390000010047; -.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; P20478; -.
DR OMA; DRRPNAN; -.
DR PhylomeDB; P20478; -.
DR Reactome; R-DME-210455; Astrocytic Glutamate-Glutamine Uptake And Metabolism.
DR Reactome; R-DME-8964539; Glutamate and glutamine metabolism.
DR SignaLink; P20478; -.
DR BioGRID-ORCS; 32087; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Gs2; fly.
DR GenomeRNAi; 32087; -.
DR PRO; PR:P20478; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001145; Expressed in head capsule and 37 other tissues.
DR ExpressionAtlas; P20478; baseline and differential.
DR Genevisible; P20478; DM.
DR GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IDA:FlyBase.
DR GO; GO:0006538; P:glutamate catabolic process; IMP:FlyBase.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0045213; P:neurotransmitter receptor metabolic process; IMP:FlyBase.
DR GO; GO:0007416; P:synapse assembly; IMP:FlyBase.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..369
FT /note="Glutamine synthetase 2 cytoplasmic"
FT /id="PRO_0000153148"
FT DOMAIN 32..112
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 119..369
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_010623"
FT VAR_SEQ 2..4
FT /note="SAR -> HSA (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_010624"
FT CONFLICT 145..164
FT /note="FLDFDGHPLGWPKNGFPGPQ -> SDFDGHHWAGQEWFPDP (in Ref.
FT 1; CAA36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 176..182
FT /note="VYARDIV -> SSPRHL (in Ref. 1; CAA36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 187..188
FT /note="RA -> AP (in Ref. 1; CAA36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 194..198
FT /note="IKVSG -> TQGVP (in Ref. 1; CAA36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 222
FT /note="D -> H (in Ref. 1; CAA36970)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="R -> C (in Ref. 1; CAA36970)"
FT /evidence="ECO:0000305"
FT TURN 5..8
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 19..23
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:7CPR"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 120..129
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 136..146
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:7CPR"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 179..192
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 207..216
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 219..237
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 257..263
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:7CPR"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 306..312
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 327..331
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 333..338
FT /evidence="ECO:0007829|PDB:7CPR"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:7CPR"
FT HELIX 354..365
FT /evidence="ECO:0007829|PDB:7CPR"
SQ SEQUENCE 369 AA; 41304 MW; 8B4488F01746702A CRC64;
MSARILEDSP NARINKTILD RYLSLPLQEN IVQATYVWID GTGEDLRCKD RTLDFIPQSP
KELPVWNYDG SSCYQAEGSN SDTYLYPVAI YKDPFRRGNN ILVMCDTYKF DGTPTDTNKR
KTCLEVANKC AAEEPWFGIE QEYTFLDFDG HPLGWPKNGF PGPQGPYYCG VGANKVYARD
IVDAHYRACL YAGIKVSGTN AEVMPAQWEF QVGPCEGISI GDDLWMARFL LHRISEEFGI
VSTLDPKPMP GDWNGAGAHT NVSTKAMRED GGIRDIEKAV AKLSKCHERH IRAYDPKQGQ
DNARRLTGKH ETSSINDFSA GVANRGCSIR IPRGVNDDGK GYFEDRRPSS NCDPYSVVEA
ILRTICLDE
