CISY_DROME
ID CISY_DROME Reviewed; 464 AA.
AC Q9W401; Q8T477;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable citrate synthase, mitochondrial;
DE EC=2.3.3.16;
DE AltName: Full=Protein knockdown;
DE Flags: Precursor;
GN Name=kdn; Synonyms=l(1)G0030; ORFNames=CG3861;
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, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC STRAIN=Berkeley; TISSUE=Testis;
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 IDENTIFICATION.
RX PubMed=14680800; DOI=10.1016/j.bbrc.2003.10.156;
RA Guedes Sde M., Vitorino R., Tomer K., Domingues M.R., Correia A.J.,
RA Amado F., Domingues P.;
RT "Drosophila melanogaster larval hemolymph protein mapping.";
RL Biochem. Biophys. Res. Commun. 312:545-554(2003).
RN [5]
RP FUNCTION.
RX PubMed=16648587; DOI=10.1534/genetics.106.057463;
RA Fergestad T., Bostwick B., Ganetzky B.;
RT "Metabolic disruption in Drosophila bang-sensitive seizure mutants.";
RL Genetics 173:1357-1364(2006).
CC -!- FUNCTION: Plays a role in controlling neuronal activity and seizure
CC susceptibility. {ECO:0000269|PubMed:16648587}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+);
CC Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10117};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q9W401-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9W401-2; Sequence=VSP_027491;
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- MISCELLANEOUS: Mutation of kdn causes a behavioral mutation ('bang
CC sensitivity' = temporarily paralysis in response to a physical jolt).
CC Flies lacking kdn exhibit alterations in neuronal firing patterns in
CC the giant fiber (GF) pathway.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
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DR EMBL; AE014298; AAF46159.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09169.1; -; Genomic_DNA.
DR EMBL; AY089318; AAL90056.1; -; mRNA.
DR RefSeq; NP_572319.2; NM_132091.3. [Q9W401-1]
DR RefSeq; NP_727091.1; NM_167072.2. [Q9W401-2]
DR AlphaFoldDB; Q9W401; -.
DR SMR; Q9W401; -.
DR BioGRID; 58066; 48.
DR IntAct; Q9W401; 25.
DR STRING; 7227.FBpp0070871; -.
DR PaxDb; Q9W401; -.
DR PRIDE; Q9W401; -.
DR DNASU; 31579; -.
DR EnsemblMetazoa; FBtr0070906; FBpp0070871; FBgn0261955. [Q9W401-2]
DR EnsemblMetazoa; FBtr0070907; FBpp0070872; FBgn0261955. [Q9W401-1]
DR GeneID; 31579; -.
DR KEGG; dme:Dmel_CG3861; -.
DR CTD; 31579; -.
DR FlyBase; FBgn0261955; kdn.
DR VEuPathDB; VectorBase:FBgn0261955; -.
DR eggNOG; KOG2617; Eukaryota.
DR GeneTree; ENSGT00390000006813; -.
DR InParanoid; Q9W401; -.
DR OMA; TVGWCAQ; -.
DR PhylomeDB; Q9W401; -.
DR Reactome; R-DME-71403; Citric acid cycle (TCA cycle).
DR SignaLink; Q9W401; -.
DR UniPathway; UPA00223; UER00717.
DR BioGRID-ORCS; 31579; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 31579; -.
DR PRO; PR:Q9W401; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0261955; Expressed in mouthpart and 38 other tissues.
DR ExpressionAtlas; Q9W401; baseline and differential.
DR Genevisible; Q9W401; DM.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:FlyBase.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:FlyBase.
DR GO; GO:0007610; P:behavior; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006101; P:citrate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 1.10.230.10; -; 1.
DR Gene3D; 1.10.580.10; -; 1.
DR InterPro; IPR016142; Citrate_synth-like_lrg_a-sub.
DR InterPro; IPR016143; Citrate_synth-like_sm_a-sub.
DR InterPro; IPR002020; Citrate_synthase.
DR InterPro; IPR019810; Citrate_synthase_AS.
DR InterPro; IPR010109; Citrate_synthase_euk.
DR InterPro; IPR036969; Citrate_synthase_sf.
DR PANTHER; PTHR11739; PTHR11739; 1.
DR Pfam; PF00285; Citrate_synt; 1.
DR PRINTS; PR00143; CITRTSNTHASE.
DR SUPFAM; SSF48256; SSF48256; 1.
DR TIGRFAMs; TIGR01793; cit_synth_euk; 1.
DR PROSITE; PS00480; CITRATE_SYNTHASE; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Behavior; Mitochondrion; Reference proteome;
KW Transferase; Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..464
FT /note="Probable citrate synthase, mitochondrial"
FT /id="PRO_0000291603"
FT ACT_SITE 302
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 348
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 403
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT VAR_SEQ 2..13
FT /note="SLYRISARKLSE -> FVRRFGNGSLGHHFAFQRRYLAKNSMWDSKSIGTPS
FT SFRMRSKKDNVTGNLKEQQQSATPETLNMPDMQD (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_027491"
SQ SEQUENCE 464 AA; 51574 MW; 57D582652931B4F9 CRC64;
MSLYRISARK LSEAQKLPNV GAYVRMIAAD GKSLRDVLAA KVPQEQERVK NFRKQHGATK
MGETTIDMMY GGMRGIKALV TETSVLDADE GIRFRGLSIP ECQKVLPAAD GGTEPLPEGL
FWLLLTGEVP TKSQVQQLSR EWAERAALPQ HVVTMLNNMP TTLHPMSQFA AAVTALNHDS
KFAKAYSDGV HKSKYWEYVY EDSMDLIAKL PVVAATIYCN TYRGGKGSRS IDSSLDWSAN
FVKMLGYDNA PFTELMRLYL TIHSDHEGGN VSAHTVHLVG SALSDPYLSF AAGLNGLAGP
LHGLANQEVL VWLRKLQKEA GNNPSEEQLK EYIWKTLKSG QVVPGYGHAV LRKTDPRYTC
QREFALKHLP EDETFQLVSK IYKVVPPILT ETGKVKNPWP NVDAHSGVLL QYYGMKEMNY
YTVLFGVSRA LGVLASLVWD RALGLPIERP KSFSTDLLVK MVQK
