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Database: UniProt
Entry: A0A2R8MPG3_CALJA
LinkDB: A0A2R8MPG3_CALJA
Original site: A0A2R8MPG3_CALJA 
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
//
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