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Database: UniProt
Entry: D3TM08_GLOMM
LinkDB: D3TM08_GLOMM
Original site: D3TM08_GLOMM 
ID   D3TM08_GLOMM            Unreviewed;       336 AA.
AC   D3TM08;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=cardiolipin synthase (CMP-forming) {ECO:0000256|ARBA:ARBA00039001};
DE            EC=2.7.8.41 {ECO:0000256|ARBA:ARBA00039001};
OS   Glossina morsitans morsitans (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD18736.1};
RN   [1] {ECO:0000313|EMBL:ADD18736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:ADD18736.1};
RX   PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA   Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA   Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT   "An insight into the sialome of Glossina morsitans morsitans.";
RL   BMC Genomics 11:213-213(2010).
RN   [2] {ECO:0000313|EMBL:ADD18736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Salivary gland {ECO:0000313|EMBL:ADD18736.1};
RG   International Glossina Genome Initiative;
RA   da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., Haines L.R.,
RA   Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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; EZ422460; ADD18736.1; -; mRNA.
DR   AlphaFoldDB; D3TM08; -.
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   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   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        223..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        302..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   336 AA;  37690 MW;  9C382B780DAB64B3 CRC64;
     MLPATVFRQI SRQHNGLCKG LTDLVASTGA SIPASNVINC LNRYAAATGF IRISFLDVNQ
     YRNWDVEKLR LYADRKKQSL HQRTLKGRDI LQEVIGKKRE SFIERKNVIV EDIREARHKV
     QERMREKMGE VIERENILTV PNMLTVSRML LSPYIGWVIV NGDYGMAISL LAVAGVTDVL
     DGQIARRWPS QASKAGSFLD PAADKILMGS LVLSMTYCDL LPLWLAGVIL FRDVFLLTAG
     FVIRYISLPP PRTFSRYFDA THVTAQLEPT LISKINTGVQ LAAVGISLGA PVWHYIDHVG
     LHGLWYLTGC TTVAAALSYI LNKNTFKIFK RPSRKT
//
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