TAM41_DROME
ID TAM41_DROME Reviewed; 342 AA.
AC Q8INF2; Q6NN16;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 ORFNames=CG33331, CG3641;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of CDP-diacylglycerol (CDP-DAG) from
CC phosphatidic acid (PA) in the mitochondrial inner membrane. Required
CC for the biosynthesis of the dimeric phospholipid cardiolipin, which
CC stabilizes supercomplexes of the mitochondrial respiratory chain in the
CC mitochondrial inner membrane. {ECO:0000250|UniProtKB:P53230}.
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:P53230};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16230;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000250|UniProtKB:P53230};
CC Note=Magnesium. Also active with cobalt or copper.
CC {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:P53230}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P53230}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P53230}; Matrix side
CC {ECO:0000250|UniProtKB:P53230}.
CC -!- SIMILARITY: Belongs to the TAM41 family. {ECO:0000305}.
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DR EMBL; AE014297; AAN13621.1; -; Genomic_DNA.
DR EMBL; BT011333; AAR96125.1; -; mRNA.
DR EMBL; BT011484; AAR99142.1; -; mRNA.
DR RefSeq; NP_996213.1; NM_206491.3.
DR AlphaFoldDB; Q8INF2; -.
DR SMR; Q8INF2; -.
DR STRING; 7227.FBpp0082457; -.
DR PaxDb; Q8INF2; -.
DR PRIDE; Q8INF2; -.
DR DNASU; 2768668; -.
DR EnsemblMetazoa; FBtr0082998; FBpp0082457; FBgn0067628.
DR GeneID; 2768668; -.
DR KEGG; dme:Dmel_CG33331; -.
DR UCSC; CG33331-RA; d. melanogaster.
DR FlyBase; FBgn0067628; CG33331.
DR VEuPathDB; VectorBase:FBgn0067628; -.
DR eggNOG; KOG2986; Eukaryota.
DR GeneTree; ENSGT00390000000616; -.
DR HOGENOM; CLU_030279_1_1_1; -.
DR InParanoid; Q8INF2; -.
DR OMA; HYSFLKF; -.
DR OrthoDB; 1145430at2759; -.
DR PhylomeDB; Q8INF2; -.
DR UniPathway; UPA00557; UER00614.
DR BioGRID-ORCS; 2768668; 1 hit in 1 CRISPR screen.
DR ChiTaRS; CG33332; fly.
DR GenomeRNAi; 2768668; -.
DR PRO; PR:Q8INF2; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0067628; Expressed in secondary oocyte and 25 other tissues.
DR Genevisible; Q8INF2; DM.
DR GO; GO:0031314; C:extrinsic component of mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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 2: Evidence at transcript 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..342
FT /note="Phosphatidate cytidylyltransferase, mitochondrial"
FT /id="PRO_0000248360"
FT CONFLICT 182
FT /note="F -> L (in Ref. 3; AAR99142)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="A -> S (in Ref. 3; AAR99142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38219 MW; 4AF076B14B489DA6 CRC64;
MLDLYRRTVA RFPLGSVSYM FAYGSGVKQQ EGYGKVGNGN NLRPPPGTVV DLVFCVRDAR
GFHAENLHRH PDHYSALRHL GPNFVAKYQE RLGAGVYCNT LVPLPDVGIT IKYGVVSQEE
LLEDLLDWRH LYLAGRLHKP VTNLVNPSDN PPLKAALERN LVSALQVALL LLPEKFTAYG
LFHTIAGLSY KGDFRMIFGE NKQKVHNIVS PQINDFFALY QPSLGQLSDY VAVNMKGQEP
GSRKPAIIFE QDKSSSATCQ HLRQLPRELQ KRLQRNAACR GDYTQVVNHL SMASQLPEVL
QASVNDIVWR SSVTQSIKNI PSAGILKSLA YSYRKAQKTF AV
