CISY_MOUSE
ID CISY_MOUSE Reviewed; 464 AA.
AC Q9CZU6; Q3UDP3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Citrate synthase, mitochondrial;
DE EC=2.3.3.1;
DE AltName: Full=Citrate (Si)-synthase;
DE Flags: Precursor;
GN Name=Cs;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Sone H., Shimano H., Yamada N.;
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Egg;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Kidney, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 35-43; 58-73; 77-92; 223-256; 328-351; 376-393 AND
RP 429-450, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-57; LYS-103; LYS-193; LYS-321;
RP LYS-327; LYS-375; LYS-393; LYS-450 AND LYS-459, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321; LYS-327; LYS-375; LYS-382;
RP LYS-393 AND LYS-459, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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=2.3.3.1; 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 -!- PTM: Methylated. Trimethylation at Lys-395 by CSKMT decreases citrate
CC synthase activity. {ECO:0000250|UniProtKB:O75390}.
CC -!- MISCELLANEOUS: Citrate synthase is found in nearly all cells capable of
CC oxidative metabolism.
CC -!- SIMILARITY: Belongs to the citrate synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB056479; BAB63945.1; -; mRNA.
DR EMBL; AK012151; BAB28063.1; -; mRNA.
DR EMBL; AK145643; BAE26560.1; -; mRNA.
DR EMBL; AK149990; BAE29218.1; -; mRNA.
DR EMBL; AK163273; BAE37268.1; -; mRNA.
DR EMBL; AK166814; BAE39041.1; -; mRNA.
DR EMBL; AK167125; BAE39273.1; -; mRNA.
DR EMBL; BC013554; AAH13554.1; -; mRNA.
DR EMBL; BC029754; AAH29754.1; -; mRNA.
DR CCDS; CCDS24273.1; -.
DR RefSeq; NP_080720.1; NM_026444.4.
DR PDB; 3NZI; X-ray; 2.75 A; B=371-377.
DR PDBsum; 3NZI; -.
DR AlphaFoldDB; Q9CZU6; -.
DR SMR; Q9CZU6; -.
DR BioGRID; 198926; 53.
DR IntAct; Q9CZU6; 9.
DR MINT; Q9CZU6; -.
DR STRING; 10090.ENSMUSP00000005826; -.
DR ChEMBL; CHEMBL2176798; -.
DR iPTMnet; Q9CZU6; -.
DR PhosphoSitePlus; Q9CZU6; -.
DR SwissPalm; Q9CZU6; -.
DR EPD; Q9CZU6; -.
DR jPOST; Q9CZU6; -.
DR MaxQB; Q9CZU6; -.
DR PaxDb; Q9CZU6; -.
DR PeptideAtlas; Q9CZU6; -.
DR PRIDE; Q9CZU6; -.
DR ProteomicsDB; 281628; -.
DR DNASU; 12974; -.
DR Ensembl; ENSMUST00000005826; ENSMUSP00000005826; ENSMUSG00000005683.
DR GeneID; 12974; -.
DR KEGG; mmu:12974; -.
DR UCSC; uc007hmj.1; mouse.
DR CTD; 1431; -.
DR MGI; MGI:88529; Cs.
DR VEuPathDB; HostDB:ENSMUSG00000005683; -.
DR eggNOG; KOG2617; Eukaryota.
DR GeneTree; ENSGT00390000006813; -.
DR HOGENOM; CLU_022049_2_1_1; -.
DR InParanoid; Q9CZU6; -.
DR OMA; TVGWCAQ; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; Q9CZU6; -.
DR TreeFam; TF300398; -.
DR BRENDA; 2.3.3.1; 3474.
DR Reactome; R-MMU-71403; Citric acid cycle (TCA cycle).
DR UniPathway; UPA00223; UER00717.
DR BioGRID-ORCS; 12974; 19 hits in 77 CRISPR screens.
DR ChiTaRS; Cs; mouse.
DR PRO; PR:Q9CZU6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9CZU6; protein.
DR Bgee; ENSMUSG00000005683; Expressed in paneth cell and 271 other tissues.
DR Genevisible; Q9CZU6; MM.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; IDA:MGI.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; ISS:UniProtKB.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; ISO:MGI.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006101; P:citrate metabolic process; ISO:MGI.
DR GO; GO:0006107; P:oxaloacetate metabolic process; ISO:MGI.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Methylation;
KW Mitochondrion; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide; Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..464
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000005472"
FT ACT_SITE 301
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 347
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT ACT_SITE 402
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10117"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q29RK1"
FT MOD_RES 103
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 375
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 382
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 395
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 450
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 459
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 459
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 464 AA; 51737 MW; 710639871C31EED5 CRC64;
MALLTAATRL LGAKNSSCLV LAARHASASS TNLKDVLSNL IPKEQARIKT FKQQHGKTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKMLPKAKG GEEPLPEGLF
WLLVTGQMPT EEQVSWLSRE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN
FARAYAEGMN RAKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSRLDWSHNF
TNMLGYTDPQ FTELMRLYLT IHSDHEGGNV SAHTSHLVGS ALSDPYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYSCQ
REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSK
