ID A0A2R8MPG3_CALJA Unreviewed; 301 AA.
AC A0A2R8MPG3;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=cardiolipin synthase (CMP-forming) {ECO:0000256|ARBA:ARBA00039001};
DE EC=2.7.8.41 {ECO:0000256|ARBA:ARBA00039001};
GN Name=CRLS1 {ECO:0000313|EMBL:JAB04453.1,
GN ECO:0000313|Ensembl:ENSCJAP00000063117.1};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000063117.1, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000063117.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:JAB04453.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bladder {ECO:0000313|EMBL:JAB04453.1}, Cerebral cortex
RC {ECO:0000313|EMBL:JAB28294.1}, Hippocampus
RC {ECO:0000313|EMBL:JAB16774.1}, and Skeletal muscle
RC {ECO:0000313|EMBL:JAB40825.1};
RX PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT sequences.";
RL Gigascience 3:14-14(2014).
RN [3] {ECO:0000313|Ensembl:ENSCJAP00000063117.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the synthesis of cardiolipin (CL)
CC (diphosphatidylglycerol) by specifically transferring a phosphatidyl
CC group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key
CC phospholipid in mitochondrial membranes and plays important roles in
CC maintaining the functional integrity and dynamics of mitochondria under
CC both optimal and stress conditions. {ECO:0000256|ARBA:ARBA00037454}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a CDP-1,2-
CC diacyl-sn-glycerol = a cardiolipin + CMP + H(+);
CC Xref=Rhea:RHEA:32931, ChEBI:CHEBI:15378, ChEBI:CHEBI:58332,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; EC=2.7.8.41;
CC Evidence={ECO:0000256|ARBA:ARBA00036453};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; GAMT01007408; JAB04453.1; -; mRNA.
DR EMBL; GAMS01006362; JAB16774.1; -; mRNA.
DR EMBL; GAMR01005638; JAB28294.1; -; mRNA.
DR EMBL; GAMQ01001026; JAB40825.1; -; mRNA.
DR RefSeq; XP_002747387.1; XM_002747341.4.
DR STRING; 9483.ENSCJAP00000063117; -.
DR Ensembl; ENSCJAT00000071061.3; ENSCJAP00000063117.1; ENSCJAG00000021302.5.
DR GeneID; 100406450; -.
DR KEGG; cjc:100406450; -.
DR CTD; 54675; -.
DR GeneTree; ENSGT00390000001607; -.
DR OMA; KRFNMAS; -.
DR OrthoDB; 5490365at2759; -.
DR TreeFam; TF314169; -.
DR Proteomes; UP000008225; Chromosome 5.
DR Bgee; ENSCJAG00000021302; Expressed in liver and 6 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043337; F:cardiolipin synthase (CMP-forming); IEA:Ensembl.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR Gene3D; 1.20.120.1760; -; 1.
DR InterPro; IPR000462; CDP-OH_P_trans.
DR InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 1.
DR PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR Pfam; PF01066; CDP-OH_P_transf; 1.
PE 2: Evidence at transcript level;
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 69..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32304 MW; 5FE52F6A1809DA88 CRC64;
MLASRVARGS WGALRGAAWV QGTRPGKGRT CGALLPPVPC CLGCLAEGWW LRPAALGLRL
PGVGQRKHCS GAGKATPRPA VGAGAAAEDP GSQWGPASAP SLYENPWTIP NMLSMTRIGL
APVLGYLIIE EDFNIALGVF ALAGLTDLLD GFIARNWASQ KSALGSALDP LADKILISIL
YVSLTYADLI PVPLTYMIIS RDVMLIAAVF YVRYRTLPTP RTLAKYFNPC YATARLKPTF
ISKVNTAVQL ILVAASLAAP VFNYADSIYL QILWCCTAFT TAASAYSYYH YGQKTVQVIK
D
//