ID   CRLS1_RAT               Reviewed;         302 AA.
AC   Q5U2V5;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cardiolipin synthase (CMP-forming);
DE            Short=CLS;
DE            EC=2.7.8.41 {ECO:0000250|UniProtKB:Q9UJA2};
GN   Name=Crls1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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:0000250|UniProtKB:Q9UJA2}.
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:0000250|UniProtKB:Q9UJA2};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:Q9UJA2};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250};
CC       Multi-pass membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000305}.
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DR   EMBL; BC085849; AAH85849.1; -; mRNA.
DR   RefSeq; NP_001014280.1; NM_001014258.1.
DR   AlphaFoldDB; Q5U2V5; -.
DR   SMR; Q5U2V5; -.
DR   STRING; 10116.ENSRNOP00000028900; -.
DR   PaxDb; Q5U2V5; -.
DR   Ensembl; ENSRNOT00000028900; ENSRNOP00000028900; ENSRNOG00000021273.
DR   GeneID; 366196; -.
DR   KEGG; rno:366196; -.
DR   UCSC; RGD:1311037; rat.
DR   CTD; 54675; -.
DR   RGD; 1311037; Crls1.
DR   eggNOG; KOG1617; Eukaryota.
DR   GeneTree; ENSGT00390000001607; -.
DR   HOGENOM; CLU_051314_0_1_1; -.
DR   InParanoid; Q5U2V5; -.
DR   OMA; KRFNMAS; -.
DR   OrthoDB; 1169813at2759; -.
DR   PhylomeDB; Q5U2V5; -.
DR   Reactome; R-RNO-1482925; Acyl chain remodelling of PG.
DR   Reactome; R-RNO-1483076; Synthesis of CL.
DR   SABIO-RK; Q5U2V5; -.
DR   PRO; PR:Q5U2V5; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000021273; Expressed in ovary and 20 other tissues.
DR   Genevisible; Q5U2V5; RN.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; IDA:RGD.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0008808; F:cardiolipin synthase activity; IDA:RGD.
DR   GO; GO:0043337; F:CDP-diacylglycerol-phosphatidylglycerol phosphatidyltransferase activity; IEA:RHEA.
DR   GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; IBA:GO_Central.
DR   GO; GO:1905711; P:response to phosphatidylethanolamine; IDA:RGD.
DR   GO; GO:0097068; P:response to thyroxine; IDA:RGD.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
PE   2: Evidence at transcript level;
KW   Lipid biosynthesis; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..302
FT                   /note="Cardiolipin synthase (CMP-forming)"
FT                   /id="PRO_0000233262"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        190..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        271..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          65..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   302 AA;  32628 MW;  B6AA1C5DEF2E09E8 CRC64;
     MLAWRVARGA WGSLRVAVRP PGARLGRGGS RRALLPPAAC CLGCLAERWR LRPAAFALRL
     PGTSPRTHCS GAGKAAPEPA AGGDAAAQAP SARWVRASAT SSYENPWTIP NLLSMTRIGL
     APVLGYLILE EDFNVALGVF ALAGLTDLLD GFIARNWANQ KSALGSALDP LADKVLISIL
     YISLTYADLI PVPLTYMIIS RDVMLIAAVF YVRYRTLPTP RTLAKYFNPC YATARLKPTF
     ISKVNTAVQL ILVAASLAAP VFNYADSIYL QILWCCTAFT TAASAYSYYH YGRKTVQVIK
     GK