CISY_RAT
ID CISY_RAT Reviewed; 466 AA.
AC Q8VHF5;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 122.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Rossignol F., Jouaville L., Mounier R., Clottes E.;
RT "Rattus norvegicus citrate synthase cDNA.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 77-92; 184-191; 209-215; 223-233; 330-340; 383-393 AND
RP 429-440, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX PubMed=19423663; DOI=10.1530/rep-09-0052;
RA Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.;
RT "Identification of novel immunodominant epididymal sperm proteins using
RT combinatorial approach.";
RL Reproduction 138:81-93(2009).
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 -!- TISSUE SPECIFICITY: Expressed in the head region and flagellum of
CC epididymal sperm. {ECO:0000269|PubMed:19423663}.
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}.
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DR EMBL; AF461496; AAL66372.1; -; mRNA.
DR RefSeq; NP_570111.1; NM_130755.1.
DR AlphaFoldDB; Q8VHF5; -.
DR SMR; Q8VHF5; -.
DR BioGRID; 250939; 3.
DR IntAct; Q8VHF5; 4.
DR MINT; Q8VHF5; -.
DR STRING; 10116.ENSRNOP00000034921; -.
DR iPTMnet; Q8VHF5; -.
DR PhosphoSitePlus; Q8VHF5; -.
DR SwissPalm; Q8VHF5; -.
DR World-2DPAGE; 0004:Q8VHF5; -.
DR jPOST; Q8VHF5; -.
DR PaxDb; Q8VHF5; -.
DR PRIDE; Q8VHF5; -.
DR GeneID; 170587; -.
DR KEGG; rno:170587; -.
DR UCSC; RGD:620330; rat.
DR CTD; 1431; -.
DR RGD; 620330; Cs.
DR eggNOG; KOG2617; Eukaryota.
DR InParanoid; Q8VHF5; -.
DR OrthoDB; 1131452at2759; -.
DR PhylomeDB; Q8VHF5; -.
DR Reactome; R-RNO-71403; Citric acid cycle (TCA cycle).
DR SABIO-RK; Q8VHF5; -.
DR UniPathway; UPA00223; UER00717.
DR PRO; PR:Q8VHF5; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0046912; F:acyltransferase activity, acyl groups converted into alkyl on transfer; ISO:RGD.
DR GO; GO:0004108; F:citrate (Si)-synthase activity; IDA:MGI.
DR GO; GO:0006084; P:acetyl-CoA metabolic process; IDA:RGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; ISS:UniProtKB.
DR GO; GO:0006101; P:citrate metabolic process; IDA:RGD.
DR GO; GO:0006107; P:oxaloacetate metabolic process; IDA:RGD.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IDA:RGD.
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 Acetylation; Direct protein sequencing; Methylation; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transferase; Transit peptide;
KW Tricarboxylic acid cycle.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 28..466
FT /note="Citrate synthase, mitochondrial"
FT /id="PRO_0000253899"
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:0000250|UniProtKB:Q9CZU6"
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:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 193
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 321
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 327
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 327
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 375
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 375
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 382
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 393
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O75390"
FT MOD_RES 393
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
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:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
FT MOD_RES 459
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CZU6"
SQ SEQUENCE 466 AA; 51867 MW; AF8D38379CD38124 CRC64;
MALLTAAARL LGAKNSSCLV LAARHASASS TNLKDILSNL IPKEQARVKT FRQQHGKTVV
GQITVDMMYG GMRGMKGLVY ETSVLDPDEG IRFRGYSIPE CQKLLPKAKG GEEPLPEGLF
WLLVTGQMPT EEQVSWLSQE WAKRAALPSH VVTMLDNFPT NLHPMSQLSA AITALNSESN
FARAYAEGIN RTKYWELIYE DCMDLIAKLP CVAAKIYRNL YREGSSIGAI DSKLDWSHNF
TNMLCYTEPQ FTELMRLYLT IHSDHDGGNV SAHTSHLVGS ALSDTYLSFA AAMNGLAGPL
HGLANQEVLV WLTQLQKEVG KDVSDEKLRD YIWNTLNSGR VVPGYGHAVL RKTDPRYSCQ
REFALKHLPK DPMFKLVAQL YKIVPNILLE QGKAKNPWPN VDAHSGVLLQ YYGMTEMNYY
TVLFGVSRAL GVLAQLIWSR ALGFPLERPK SMSTDGLMKF VDSKSG
