TAM41_MOUSE
ID TAM41_MOUSE Reviewed; 337 AA.
AC Q3TUH1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Phosphatidate cytidylyltransferase, mitochondrial;
DE EC=2.7.7.41 {ECO:0000250|UniProtKB:D3ZKT0};
DE AltName: Full=CDP-diacylglycerol synthase;
DE Short=CDP-DAG synthase;
DE AltName: Full=Mitochondrial translocator assembly and maintenance protein 41 homolog;
DE Short=TAM41;
GN Name=Tamm41;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Head;
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).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the conversion of phosphatidic acid (PA) to CDP-
CC diacylglycerol (CDP-DAG), an essential intermediate in the synthesis of
CC phosphatidylglycerol, cardiolipin and phosphatidylinositol.
CC {ECO:0000250|UniProtKB:D3ZKT0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-
CC diacyl-sn-glycerol + diphosphate; Xref=Rhea:RHEA:16229,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:58608; EC=2.7.7.41;
CC Evidence={ECO:0000250|UniProtKB:D3ZKT0};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000250|UniProtKB:D3ZKT0};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
CC {ECO:0000250|UniProtKB:D3ZKT0}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:D3ZKT0}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:D3ZKT0}; Matrix side
CC {ECO:0000250|UniProtKB:P53230}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TUH1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TUH1-2; Sequence=VSP_020248, VSP_020249;
CC -!- SIMILARITY: Belongs to the TAM41 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK005100; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK005100; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK160774; BAE36000.1; -; mRNA.
DR CCDS; CCDS20437.1; -. [Q3TUH1-1]
DR AlphaFoldDB; Q3TUH1; -.
DR SMR; Q3TUH1; -.
DR STRING; 10090.ENSMUSP00000032461; -.
DR iPTMnet; Q3TUH1; -.
DR PhosphoSitePlus; Q3TUH1; -.
DR EPD; Q3TUH1; -.
DR MaxQB; Q3TUH1; -.
DR PaxDb; Q3TUH1; -.
DR PeptideAtlas; Q3TUH1; -.
DR PRIDE; Q3TUH1; -.
DR ProteomicsDB; 262929; -. [Q3TUH1-1]
DR ProteomicsDB; 262930; -. [Q3TUH1-2]
DR UCSC; uc009dik.1; mouse. [Q3TUH1-2]
DR MGI; MGI:1916221; Tamm41.
DR eggNOG; KOG2986; Eukaryota.
DR InParanoid; Q3TUH1; -.
DR PhylomeDB; Q3TUH1; -.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:Q3TUH1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3TUH1; protein.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IBA:GO_Central.
DR InterPro; IPR015222; Tam41.
DR PANTHER; PTHR13619; PTHR13619; 1.
DR Pfam; PF09139; Tam41_Mmp37; 1.
DR PIRSF; PIRSF028840; Mmp37; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Magnesium;
KW Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Nucleotidyltransferase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome; Transferase.
FT CHAIN 1..337
FT /note="Phosphatidate cytidylyltransferase, mitochondrial"
FT /id="PRO_0000248355"
FT VAR_SEQ 189..239
FT /note="DFRMVIGEEKSKVLNIVKPNVGHFRELYESILQKDPQVVYKMHQGQLEIDK
FT -> LYSAWWVLHPSLAGSSWHQPHAGQLFVRKLGAWPQLLGHLGCGPAQVFPTS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020248"
FT VAR_SEQ 240..337
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020249"
SQ SEQUENCE 337 AA; 37828 MW; CBC7BDB1DDFFC093 CRC64;
MALQALHSSG VGLRRILAHF PEDLSLAFAY GSAVYRQAGP SAHQENPMLD LVFTVDDPVA
WHAMNLKKNW SHYSFLKLLG PRIISSIQNN YGAGVYFNPL IRCDGKLIKY GVISTGTLIE
DLLNWNNLYI AGRLQKPVKI VSMNENMALR AALDKNLRSA VTTACLMLPE SFSEEDLFIE
IAGLSYSGDF RMVIGEEKSK VLNIVKPNVG HFRELYESIL QKDPQVVYKM HQGQLEIDKS
PEGQFTQLMT LPRTLQQQIN HIMDPPGRNR DVEETLLQVA QDPDCGDVVR LAISSIVRPS
SIRQSTKGLF TAGMKKSVIY SSRKLNKMWK GWMSKAS
