TAM41_RAT
ID TAM41_RAT Reviewed; 337 AA.
AC D3ZKT0;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Phosphatidate cytidylyltransferase, mitochondrial;
DE EC=2.7.7.41 {ECO:0000269|PubMed:29253589};
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 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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP PATHWAY.
RX PubMed=29253589; DOI=10.1016/j.bbalip.2017.12.005;
RA Blunsom N.J., Gomez-Espinosa E., Ashlin T.G., Cockcroft S.;
RT "Mitochondrial CDP-diacylglycerol synthase activity is due to the
RT peripheral protein, TAMM41 and not due to the integral membrane protein,
RT CDP-diacylglycerol synthase 1.";
RL Biochim. Biophys. Acta 1863:284-298(2018).
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:0000269|PubMed:29253589}.
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:0000269|PubMed:29253589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000305|PubMed:29253589};
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:0000305|PubMed:29253589}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:29253589}; Peripheral membrane protein
CC {ECO:0000269|PubMed:29253589}; Matrix side
CC {ECO:0000250|UniProtKB:P53230}.
CC -!- TISSUE SPECIFICITY: Brain and liver. {ECO:0000269|PubMed:29253589}.
CC -!- SIMILARITY: Belongs to the TAM41 family. {ECO:0000305}.
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DR EMBL; AABR07073059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473964; EDM02163.1; -; Genomic_DNA.
DR RefSeq; NP_001102112.1; NM_001108642.1.
DR AlphaFoldDB; D3ZKT0; -.
DR SMR; D3ZKT0; -.
DR STRING; 10116.ENSRNOP00000010397; -.
DR SwissLipids; SLP:000001894; -.
DR jPOST; D3ZKT0; -.
DR PaxDb; D3ZKT0; -.
DR PeptideAtlas; D3ZKT0; -.
DR Ensembl; ENSRNOT00000010397; ENSRNOP00000010397; ENSRNOG00000007874.
DR GeneID; 362419; -.
DR KEGG; rno:362419; -.
DR UCSC; RGD:1586150; rat.
DR CTD; 132001; -.
DR RGD; 1586150; Tamm41.
DR eggNOG; KOG2986; Eukaryota.
DR GeneTree; ENSGT00390000000616; -.
DR HOGENOM; CLU_030279_1_2_1; -.
DR InParanoid; D3ZKT0; -.
DR OMA; HYSFLKF; -.
DR OrthoDB; 1145430at2759; -.
DR PhylomeDB; D3ZKT0; -.
DR TreeFam; TF314503; -.
DR BRENDA; 2.7.7.41; 5301.
DR UniPathway; UPA00557; UER00614.
DR PRO; PR:D3ZKT0; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Proteomes; UP000234681; Chromosome 4.
DR Bgee; ENSRNOG00000007874; Expressed in duodenum and 19 other tissues.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004605; F:phosphatidate cytidylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
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 Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Nucleotidyltransferase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..337
FT /note="Phosphatidate cytidylyltransferase, mitochondrial"
FT /id="PRO_0000449324"
SQ SEQUENCE 337 AA; 37786 MW; 63E5C5EB4CACCC1F CRC64;
MALQALHSSG VGLRRILAHF PEDLSLAFAY GSAVYRQAGP SAHQENPMLD LVFTVDDPVA
WHAMNLKKNW SHYSLLKLLG PRIISSVQNN YGAGVYFNPL IMCDGKLIKY GVISTGTLIE
DLLNWNNLYI AGRLQKPVKI VSMNESTVLR AALDKNLKSA VTTACLMLPE SFSEEDLFIE
IAGLSYSGDF RMVIGEEKAK VLNIVKPNVV HFRELYESIL QKDPQMVYKM HQGQLEIDKS
PEGQFTQLMT LPRTLQQHIN HIMDPPGRNR DVEETLLQVA QDPDCGDVVR LAVSSIVRPS
SIRQSTKGLF TAGVKKSVIY SSRKLNKMWK GWVRKTS
