ID A0A2Y9RG12_TRIMA Unreviewed; 302 AA.
AC A0A2Y9RG12;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=cardiolipin synthase (CMP-forming) {ECO:0000256|ARBA:ARBA00039001};
DE EC=2.7.8.41 {ECO:0000256|ARBA:ARBA00039001};
GN Name=LOC101360345 {ECO:0000313|RefSeq:XP_023593322.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_023593322.1};
RN [1] {ECO:0000313|RefSeq:XP_023593322.1}
RP IDENTIFICATION.
RG RefSeq;
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}.
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 RefSeq; XP_023593322.1; XM_023737554.1.
DR STRING; 127582.A0A2Y9RG12; -.
DR KEGG; tmu:101360345; -.
DR InParanoid; A0A2Y9RG12; -.
DR OrthoDB; 5490365at2759; -.
DR Proteomes; UP000248480; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030572; F:phosphatidyltransferase activity; IEA:UniProt.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
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 4: Predicted;
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:UP000248480};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 198..214
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"
SQ SEQUENCE 302 AA; 32529 MW; D5AEA451F3DB9E50 CRC64;
MLASRVARGS WALRGAAWVP GARXXXXXXX XXXXXXXXXX XXXXXXXXXX XXXXXXGLRL
PGIRLRGHCS GAGKAAPGPA AGGSTAADAP AGQWGPASAA SLYENPWTIP NMLSMTRIGL
APVLGYLIIE EDFNIALGVF ALAGLTDLLD GFIARNWASQ KSALGSALDP LADKILISIL
YVSLTCADLI PVSLTYMIIS RDIMLIAAVF YVRYRTLPTP RTLAKYFNPC YATARLKPTF
ISKVNTAVQL ILVAASLAAP VFNYVDSIYL QILWCFTAFT TAASAYSYYH YGRKTVQVIK
GR
//
