LOCUS       NP_080720                464 aa            linear   ROD 28-APR-2025
DEFINITION  citrate synthase, mitochondrial precursor [Mus musculus].
ACCESSION   NP_080720
VERSION     NP_080720.1
DBSOURCE    REFSEQ: accession NM_026444.4
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 464)
  AUTHORS   Ayyangar,U., Karkhanis,A., Tay,H., Afandi,A.F.B., Bhattacharjee,O.,
            Ks,L., Lee,S.H., Chan,J. and Raghavan,S.
  TITLE     Metabolic rewiring of macrophages by epidermal-derived lactate
            promotes sterile inflammation in the murine skin
  JOURNAL   EMBO J 43 (7), 1113-1134 (2024)
   PUBMED   38418556
REFERENCE   2  (residues 1 to 464)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   3  (residues 1 to 464)
  AUTHORS   Beutner,G., Burris,J.R., Collins,M.P., Kulkarni,C.A.,
            Nadtochiy,S.M., de Mesy Bentley,K.L., Cohen,E.D., Brookes,P.S. and
            Porter,G.A. Jr.
  TITLE     Coordinated metabolic responses to cyclophilin D deletion in the
            developing heart
  JOURNAL   iScience 27 (3), 109157 (2024)
   PUBMED   38414851
  REMARK    Publication Status: Online-Only
REFERENCE   4  (residues 1 to 464)
  AUTHORS   Khadhraoui,N., Prola,A., Vandestienne,A., Blondelle,J.,
            Guillaud,L., Courtin,G., Bodak,M., Prost,B., Huet,H.,
            Wintrebert,M., Pechoux,C., Solgadi,A., Relaix,F., Tiret,L. and
            Pilot-Storck,F.
  TITLE     Hacd2 deficiency in mice leads to an early and lethal mitochondrial
            disease
  JOURNAL   Mol Metab 69, 101677 (2023)
   PUBMED   36693621
REFERENCE   5  (residues 1 to 464)
  AUTHORS   Li,Z., Liu,R., Liu,Y., Zhao,M., Luan,J., Wang,Y., Shang,W.,
            Song,X., Sun,Y. and Han,F.
  TITLE     H55 N variation in citrate synthase leads to decrement in the
            enzyme activity and transport rate to mitochondria in HEI-OC1 cells
  JOURNAL   Biochem Biophys Res Commun 612, 134-140 (2022)
   PUBMED   35525197
  REMARK    GeneRIF: H55 N variation in citrate synthase leads to decrement in
            the enzyme activity and transport rate to mitochondria in HEI-OC1
            cells.
REFERENCE   6  (residues 1 to 464)
  AUTHORS   Chow,K.M., Ma,Z., Cai,J., Pierce,W.M. and Hersh,L.B.
  TITLE     Nardilysin facilitates complex formation between mitochondrial
            malate dehydrogenase and citrate synthase
  JOURNAL   Biochim Biophys Acta 1723 (1-3), 292-301 (2005)
   PUBMED   15809022
REFERENCE   7  (residues 1 to 464)
  AUTHORS   Mootha,V.K., Bunkenborg,J., Olsen,J.V., Hjerrild,M.,
            Wisniewski,J.R., Stahl,E., Bolouri,M.S., Ray,H.N., Sihag,S.,
            Kamal,M., Patterson,N., Lander,E.S. and Mann,M.
  TITLE     Integrated analysis of protein composition, tissue diversity, and
            gene regulation in mouse mitochondria
  JOURNAL   Cell 115 (5), 629-640 (2003)
   PUBMED   14651853
REFERENCE   8  (residues 1 to 464)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
REFERENCE   9  (residues 1 to 464)
  AUTHORS   Jiang,C.H., Tsien,J.Z., Schultz,P.G. and Hu,Y.
  TITLE     The effects of aging on gene expression in the hypothalamus and
            cortex of mice
  JOURNAL   Proc Natl Acad Sci U S A 98 (4), 1930-1934 (2001)
   PUBMED   11172053
REFERENCE   10 (residues 1 to 464)
  AUTHORS   Lahbib-Mansais,Y., Yerle,M., Pinton,P. and Gellin,J.
  TITLE     Chromosomal localization of homeobox genes and associated markers
            on porcine chromosomes 3, 5, 12, 15, 16 and 18: comparative mapping
            study with human and mouse
  JOURNAL   Mamm Genome 7 (3), 174-179 (1996)
   PUBMED   8833235
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from CJ144772.1, AC090489.8 and
            BU700437.1.
            
            Summary: The protein encoded by this gene is a central metabolic
            pathway enzyme, catalyzing the first step of the tricarboxylic acid
            cycle in which acetyl coenzyme A and oxaloacetate are converted to
            citrate and coenzyme A. This enzyme is found in nearly all cells
            capable of oxidative metabolism. This protein is nuclear encoded
            and transported into the mitochondrial matrix, where the mature
            form is found. [provided by RefSeq, Jul 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC029754.1, AK149990.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            gene product(s) localized to mito. :: reported by MitoCarta
            RefSeq Select criteria             :: based on conservation,
                                                  expression, longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..464
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="10"
                     /map="10 76.53 cM"
     Protein         1..464
                     /product="citrate synthase, mitochondrial precursor"
                     /EC_number="2.3.3.1"
                     /note="citrate synthase, mitochondrial; citrate
                     (Si)-synthase"
                     /calculated_mol_wt=49015
     transit_peptide 1..27
                     /note="Mitochondrion. /evidence=ECO:0000250; propagated
                     from UniProtKB/Swiss-Prot (Q9CZU6.1)"
                     /calculated_mol_wt=2740
     Region          2..21
                     /region_name="SIFI-degron.
                     /evidence=ECO:0000250|UniProtKB:O75390"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZU6.1)"
     mat_peptide     28..464
                     /product="Citrate synthase, mitochondrial.
                     /id=PRO_0000005472"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9CZU6.1)"
                     /calculated_mol_wt=49015
     Region          33..459
                     /region_name="ScCit1-2_like"
                     /note="Saccharomyces cerevisiae (Sc) citrate synthases
                     Cit1-2_like. Citrate synthases (CS) catalyzes the
                     condensation of acetyl coenzyme A (AcCoA) with
                     oxaloacetate (OAA) to form citrate and coenzyme A (CoA),
                     the first step in the citric acid cycle (TCA or...;
                     cd06105"
                     /db_xref="CDD:99858"
     Site            order(71..72,75..81,166,170,173,265,270,273..274,277..278,
                     281..283,287,294..295,298..300,348,445..453)
                     /site_type="other"
                     /note="dimer interface [polypeptide binding]"
                     /db_xref="CDD:99858"
     Site            order(73,265,269,299..302,304,307,341..348,351,356,397,
                     400,402,424,428,445,448)
                     /site_type="active"
                     /db_xref="CDD:99858"
     Site            order(73,299..301,304,307,341..348,351,397,400,402,445)
                     /site_type="other"
                     /note="coenzyme A binding site [chemical binding]"
                     /db_xref="CDD:99858"
     Site            order(73,265,269,300..301,341..342,344..348,356,400,428)
                     /site_type="other"
                     /note="citrylCoA binding site [chemical binding]"
                     /db_xref="CDD:99858"
     Site            76
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0000250|UniProtKB:Q29RK1; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            226
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            order(265,269,301..302,347..348,356,402,424,428,448)
                     /site_type="other"
                     /note="oxalacetate/citrate binding site [chemical
                     binding]"
                     /db_xref="CDD:99858"
     Site            order(301,347,402)
                     /site_type="active"
                     /note="catalytic triad [active]"
                     /db_xref="CDD:99858"
     Site            321
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            327
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            375
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            382
                     /site_type="acetylation"
                     /note="N6-acetyllysine.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            393
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            395
                     /site_type="methylation"
                     /note="N6,N6,N6-trimethyllysine.
                     /evidence=ECO:0000250|UniProtKB:O75390; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     Site            459
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:23576753; propagated from
                     UniProtKB/Swiss-Prot (Q9CZU6.1)"
     CDS             1..464
                     /gene="Cs"
                     /gene_synonym="2610511A05Rik; 9030605P22Rik; Ahl4; Cis"
                     /coded_by="NM_026444.4:192..1586"
                     /db_xref="CCDS:CCDS24273.1"
                     /db_xref="GeneID:12974"
                     /db_xref="MGI:MGI:88529"
ORIGIN      
        1 malltaatrl lgaknssclv laarhasass tnlkdvlsnl ipkeqarikt fkqqhgktvv
       61 gqitvdmmyg gmrgmkglvy etsvldpdeg irfrgysipe cqkmlpkakg geeplpeglf
      121 wllvtgqmpt eeqvswlsre wakraalpsh vvtmldnfpt nlhpmsqlsa aitalnsesn
      181 farayaegmn rakyweliye dcmdliaklp cvaakiyrnl yregssigai dsrldwshnf
      241 tnmlgytdpq ftelmrlylt ihsdheggnv sahtshlvgs alsdpylsfa aamnglagpl
      301 hglanqevlv wltqlqkevg kdvsdeklrd yiwntlnsgr vvpgyghavl rktdpryscq
      361 refalkhlpk dpmfklvaql ykivpnille qgkaknpwpn vdahsgvllq yygmtemnyy
      421 tvlfgvsral gvlaqliwsr algfplerpk smstdglmkf vdsk
//
