ID A0A1S3PH74_SALSA Unreviewed; 358 AA.
AC A0A1S3PH74;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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|RefSeq:XP_014027020.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014027020.1};
RN [1] {ECO:0000313|RefSeq:XP_014027020.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014027020.1};
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}.
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DR RefSeq; XP_014027020.1; XM_014171545.1.
DR AlphaFoldDB; A0A1S3PH74; -.
DR GeneID; 100380602; -.
DR CTD; 54675; -.
DR OrthoDB; 5490365at2759; -.
DR Proteomes; UP000087266; Chromosome ssa01.
DR Bgee; ENSSSAG00000005519; Expressed in zone of skin and 15 other cell types or tissues.
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};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT REGION 66..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 358 AA; 39277 MW; 8AC5707FCFADEE7B CRC64;
MFFLSVSKNN LAVCARGHVA HCARSVCWAI PASWRQQTGV CVRVELKLLQ RLKNSVSSVA
QWSSYTQYHT PPPQDTHIPS PTTPEVSGHA LKGPNESVTR SCRRRGHERT QGWRGLCSGK
PRETPADCTP GVDLRETTQP ADGPSDLGQG LFKFKELYEN PWTIPNLLCV CRIALAPVLG
VLITEQHFHL SLGLFALAGF TDVLDGYIAR NWPSQKSALG SALDPLADKI LISVLYISLT
YAQLIPAPLT ALVIARDVGL IAAVFYVRYK TVPPPVTLSK FFNPCYTTAQ LKPTTLSKVN
TAIQLFLVAA SLASPVFHYT DSPLLQALWY ITAVTTTVSG YSYYHYGMKT VAVLNSTK
//
