TAZ_DROME
ID TAZ_DROME Reviewed; 378 AA.
AC Q9V6G5; Q8ML32; Q8SZ79; Q9U9U8; Q9V6G4;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Tafazzin {ECO:0000303|PubMed:17082194, ECO:0000303|PubMed:19114128, ECO:0000303|PubMed:19164547, ECO:0000303|PubMed:19416660, ECO:0000303|PubMed:19700766, ECO:0000303|PubMed:22941046};
DE Short=TAZ {ECO:0000303|PubMed:17082194, ECO:0000303|PubMed:19164547, ECO:0000303|PubMed:19416660, ECO:0000303|PubMed:22941046};
DE Short=dTAZ;
DE EC=2.3.1.- {ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:22941046};
GN Name=Taz {ECO:0000312|FlyBase:FBgn0026619};
GN ORFNames=CG8766 {ECO:0000312|FlyBase:FBgn0026619};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RC STRAIN=Canton-S;
RA Benevolenskaya E.V., Frolov M.V., Birchler J.A.;
RT "Drosophila homolog of the human G4.5 gene encoding tafazzin proteins.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39 (ISOFORM A).
RC STRAIN=Canton-S;
RX PubMed=11102369; DOI=10.1093/genetics/156.4.1727;
RA Frolov M.V., Benevolenskaya E.V., Birchler J.A.;
RT "The oxen gene of Drosophila encodes a homolog of subunit 9 of yeast
RT ubiquinol-cytochrome c oxidoreductase complex: evidence for modulation of
RT gene expression in response to mitochondrial activity.";
RL Genetics 156:1727-1736(2000).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY (ISOFORM A), DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17082194; DOI=10.1074/jbc.m606100200;
RA Xu Y., Malhotra A., Ren M., Schlame M.;
RT "The enzymatic function of tafazzin.";
RL J. Biol. Chem. 281:39217-39224(2006).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16855048; DOI=10.1073/pnas.0603242103;
RA Xu Y., Condell M., Plesken H., Edelman-Novemsky I., Ma J., Ren M.,
RA Schlame M.;
RT "A Drosophila model of Barth syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11584-11588(2006).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY (ISOFORM A).
RX PubMed=19416660; DOI=10.1016/j.bbalip.2009.01.004;
RA Malhotra A., Xu Y., Ren M., Schlame M.;
RT "Formation of molecular species of mitochondrial cardiolipin. 1. A novel
RT transacylation mechanism to shuttle fatty acids between sn-1 and sn-2
RT positions of multiple phospholipid species.";
RL Biochim. Biophys. Acta 1791:314-320(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY (ISOFORMS A; B AND C), SUBCELLULAR LOCATION
RP (ISOFORMS A; B AND C), DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=19700766; DOI=10.1074/jbc.m109.016642;
RA Xu Y., Zhang S., Malhotra A., Edelman-Novemsky I., Ma J., Kruppa A.,
RA Cernicica C., Blais S., Neubert T.A., Ren M., Schlame M.;
RT "Characterization of tafazzin splice variants from humans and fruit
RT flies.";
RL J. Biol. Chem. 284:29230-29239(2009).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19114128; DOI=10.1016/j.mito.2008.12.001;
RA Acehan D., Khuchua Z., Houtkooper R.H., Malhotra A., Kaufman J., Vaz F.M.,
RA Ren M., Rockman H.A., Stokes D.L., Schlame M.;
RT "Distinct effects of tafazzin deletion in differentiated and
RT undifferentiated mitochondria.";
RL Mitochondrion 9:86-95(2009).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=19164547; DOI=10.1073/pnas.0811224106;
RA Malhotra A., Edelman-Novemsky I., Xu Y., Plesken H., Ma J., Schlame M.,
RA Ren M.;
RT "Role of calcium-independent phospholipase A2 in the pathogenesis of Barth
RT syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2337-2341(2009).
RN [12]
RP FUNCTION, CATALYTIC ACTIVITY (ISOFORM A), AND SUBCELLULAR LOCATION.
RX PubMed=22941046; DOI=10.1038/nchembio.1064;
RA Schlame M., Acehan D., Berno B., Xu Y., Valvo S., Ren M., Stokes D.L.,
RA Epand R.M.;
RT "The physical state of lipid substrates provides transacylation specificity
RT for tafazzin.";
RL Nat. Chem. Biol. 8:862-869(2012).
RN [13]
RP SUBUNIT.
RX PubMed=25598000; DOI=10.1016/j.mito.2015.01.002;
RA Xu Y., Malhotra A., Claypool S.M., Ren M., Schlame M.;
RT "Tafazzins from Drosophila and mammalian cells assemble in large protein
RT complexes with a short half-life.";
RL Mitochondrion 21:27-32(2015).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=29405656; DOI=10.14814/phy2.13604;
RA Damschroder D., Reynolds C., Wessells R.;
RT "Drosophila tafazzin mutants have impaired exercise capacity.";
RL Physiol. Rep. 6:E13604-E13604(2018).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=31110016; DOI=10.1073/pnas.1900890116;
RA Xu Y., Anjaneyulu M., Donelian A., Yu W., Greenberg M.L., Ren M.,
RA Owusu-Ansah E., Schlame M.;
RT "Assembly of the complexes of oxidative phosphorylation triggers the
RT remodeling of cardiolipin.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:11235-11240(2019).
CC -!- FUNCTION: Acyltransferase required to remodel newly synthesized
CC phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-
CC glycerol or CL), a key component of the mitochondrial inner membrane,
CC with tissue specific acyl chains necessary for adequate mitochondrial
CC function. Its role in cellular physiology is to improve mitochondrial
CC performance (By similarity). CL is critical for the coassembly of
CC lipids and proteins in mitochondrial membranes(PubMed:17082194,
CC PubMed:16855048, PubMed:19416660, PubMed:19700766, PubMed:19114128).
CC For instance, remodeling of the acyl groups of CL in the mitochondrial
CC inner membrane affects the assembly and stability of respiratory chain
CC complex IV and its supercomplex forms (By similarity). Catalyzes the
CC transacylacion between phospholipids and lysophospholipids, with the
CC highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-
CC 3-phosphocholine or PC) and CL (PubMed:17082194, PubMed:19416660,
CC PubMed:22941046). Catalyzes both 1-acyl-sn-glycero-3-phosphocholine
CC (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation,
CC that means, it exchanges acyl groups between CL and PC by a combination
CC of forward and reverse transacylations. Also catalyzes transacylations
CC between other phospholipids such as phosphatidylethanolamine (1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and
CC PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate
CC or PA), although at lower rate (PubMed:17082194). Not regiospecific, it
CC transfers acyl groups into any of the sn-1 and sn-2 positions of the
CC monolysocardiolipin (MLCL), which is an important prerequisite for
CC uniformity and symmetry in CL acyl distribution. Cannot transacylate
CC dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of
CC an acyl acceptor (PubMed:19416660). CoA-independent, it can reshuffle
CC molecular species within a single phospholipid class (PubMed:17082194,
CC PubMed:22941046). Redistributes fatty acids between MLCL, CL, and other
CC lipids, which prolongs the half-life of CL (PubMed:31110016). Its
CC action is completely reversible, which allows for cyclic changes, such
CC as fission and fusion or bending and flattening of the membrane. Hence,
CC by contributing to the flexibility of the lipid composition, it plays
CC an important role in the dynamics of mitochondria membranes
CC (PubMed:22941046). Essential for the final stage of spermatogenesis,
CC spermatid individualization (PubMed:19164547). Required for the
CC initiation of mitophagy (By similarity). {ECO:0000250|UniProtKB:Q06510,
CC ECO:0000250|UniProtKB:Q16635, ECO:0000269|PubMed:16855048,
CC ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19114128,
CC ECO:0000269|PubMed:19164547, ECO:0000269|PubMed:19416660,
CC ECO:0000269|PubMed:19700766, ECO:0000269|PubMed:22941046,
CC ECO:0000269|PubMed:31110016}.
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:19700766,
CC ECO:0000269|PubMed:22941046, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:19700766,
CC ECO:0000269|PubMed:22941046, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:19700766,
CC ECO:0000269|PubMed:22941046, ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform B]:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000269|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform C]:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000269|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine =
CC 1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-
CC glycerol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:43796, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43797;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43798;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine =
CC 1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-
CC glycerol + 1-hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:43800, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:83581, ChEBI:CHEBI:83714;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43801;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43802;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1,2-di-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine = 1',3'-bis-
CC [1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67456, ChEBI:CHEBI:28733, ChEBI:CHEBI:42027,
CC ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67457;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67458;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-glycerol + 1-tetradecanoyl-sn-glycero-3-phosphocholine = 1'-
CC [1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1-tetradecanoyl-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67488, ChEBI:CHEBI:64489, ChEBI:CHEBI:83580,
CC ChEBI:CHEBI:83581, ChEBI:CHEBI:86094;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67489;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67490;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + 1-nonadecanoyl-sn-glycero-3-phosphocholine = 1'-[1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + 1-nonadecanoyl-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:67520, ChEBI:CHEBI:77253,
CC ChEBI:CHEBI:77259, ChEBI:CHEBI:131989, ChEBI:CHEBI:172373;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67521;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67522;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1-acyl-
CC sn-glycero-3-phosphocholine = 1-acyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol) + a 1,2-diacyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67676, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:64716, ChEBI:CHEBI:64840;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67677;
CC Evidence={ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67678;
CC Evidence={ECO:0000305|PubMed:19416660, ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho-(1'-sn-glycerol) + 1-hexadecanoyl-sn-glycero-3-phosphocholine
CC = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-
CC glycerol); Xref=Rhea:RHEA:43828, ChEBI:CHEBI:72840,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43829;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43830;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol)
CC + 1-nonadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho-(1'-sn-glycerol) + 1-nonadecanoyl-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:67516,
CC ChEBI:CHEBI:72828, ChEBI:CHEBI:75163, ChEBI:CHEBI:131989,
CC ChEBI:CHEBI:172373; Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67517;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67518;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + a 1-acyl-sn-glycero-3-
CC phosphocholine = a 1,2-diacyl-sn-glycero-3-phosphocholine + a 1-acyl-
CC sn-glycero-3-phosphate; Xref=Rhea:RHEA:67672, ChEBI:CHEBI:57643,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58168, ChEBI:CHEBI:58608;
CC Evidence={ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67673;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67674;
CC Evidence={ECO:0000269|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-
CC hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC 1-hexadecanoyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:43824,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72860, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73002; Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43825;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43826;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + 1-hexadecanoyl-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine = 1-(9Z)-
CC octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:65036,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74563; Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65037;
CC Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65038;
CC Evidence={ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + a 1-acyl-sn-
CC glycero-3-phosphocholine = a 1,2-diacyl-sn-glycero-3-phosphocholine +
CC a 1-acyl-sn-glycero-3-phosphoethanolamine; Xref=Rhea:RHEA:67668,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:64381,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:17082194,
CC ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67669;
CC Evidence={ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19416660,
CC ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67670;
CC Evidence={ECO:0000305|PubMed:17082194, ECO:0000305|PubMed:19416660,
CC ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1-
CC hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine;
CC Xref=Rhea:RHEA:43820, ChEBI:CHEBI:72998, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73008;
CC Evidence={ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43821;
CC Evidence={ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43822;
CC Evidence={ECO:0000269|PubMed:17082194, ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + 1-tetradecanoyl-sn-glycero-3-phosphocholine =
CC 1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphoethanolamine + 1-
CC tetradecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67584, ChEBI:CHEBI:64489, ChEBI:CHEBI:86094,
CC ChEBI:CHEBI:133732, ChEBI:CHEBI:172403;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67585;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67586;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a
CC 1-acyl-sn-glycero-3-phosphoethanolamine + a cardiolipin;
CC Xref=Rhea:RHEA:35843, ChEBI:CHEBI:62237, ChEBI:CHEBI:64381,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35844;
CC Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:35845;
CC Evidence={ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphoethanolamine + a tri-(9Z,12Z-octadecadienoyl)-
CC monolysocardiolipin = 1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-
CC glycero-3-phospho]-glycerol + 1-hexadecanoyl-sn-glycero-3-
CC phosphoethanolamine; Xref=Rhea:RHEA:65040, ChEBI:CHEBI:73004,
CC ChEBI:CHEBI:73008, ChEBI:CHEBI:83581, ChEBI:CHEBI:156311;
CC Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65041;
CC Evidence={ECO:0000269|PubMed:17082194};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:65042;
CC Evidence={ECO:0000305|PubMed:17082194};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-glycerol + 1'-[1-(9Z,12Z-octadecadienoyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-phospho]-glycerol = 1'-[1,2-di-(9Z,12Z-octadecadienoyl)-
CC sn-glycero-3-phospho]-3'-[1-(9Z,12Z-octadecadienoyl)-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + 1'-[1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-glycerol;
CC Xref=Rhea:RHEA:43804, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581,
CC ChEBI:CHEBI:83582, ChEBI:CHEBI:83715;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43805;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43806;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-hexadecenoyl)-sn-
CC glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:43808, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73851, ChEBI:CHEBI:74000, ChEBI:CHEBI:83717;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43809;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43810;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-dioctadecanoyl-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-hexadecanoyl-2-
CC octadecanoyl-sn-glycero-3-phosphocholine + 1-octadecanoyl-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:43812, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73000, ChEBI:CHEBI:73858, ChEBI:CHEBI:83718;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43813;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43814;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:43816, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000269|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000305|PubMed:19416660};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine +
CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1-(9Z)-
CC octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine +
CC 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67432, ChEBI:CHEBI:28610, ChEBI:CHEBI:28733,
CC ChEBI:CHEBI:42027, ChEBI:CHEBI:74670;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67433;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67434;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1,2-di-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine + 1-tetradecanoyl-sn-glycero-3-phosphocholine = 1-
CC (9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine + 1-
CC tetradecanoyl-2-(9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:67500, ChEBI:CHEBI:64489,
CC ChEBI:CHEBI:86095, ChEBI:CHEBI:86161, ChEBI:CHEBI:133456;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67501;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67502;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-nonadecanoyl-sn-glycero-3-phosphocholine + 1-octadecanoyl-2-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1-nonadecanoyl-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + 1-octadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:67504, ChEBI:CHEBI:73858,
CC ChEBI:CHEBI:75034, ChEBI:CHEBI:131989, ChEBI:CHEBI:172373;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67505;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67506;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- CATALYTIC ACTIVITY: [Isoform A]:
CC Reaction=1-(9Z)-octadecenoyl-2-octadecanoyl-sn-glycero-3-phosphocholine
CC + 1-nonadecanoyl-sn-glycero-3-phosphocholine = 1-nonadecanoyl-2-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphocholine + 2-octadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:67508, ChEBI:CHEBI:76073,
CC ChEBI:CHEBI:76076, ChEBI:CHEBI:131989, ChEBI:CHEBI:172373;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67509;
CC Evidence={ECO:0000269|PubMed:22941046};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67510;
CC Evidence={ECO:0000305|PubMed:22941046};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:17082194,
CC ECO:0000305|PubMed:19416660, ECO:0000305|PubMed:19700766,
CC ECO:0000305|PubMed:22941046}.
CC -!- SUBUNIT: Associates with multiple protein complexes (PubMed:25598000).
CC Association with large protein complexes occurs only in the presence of
CC cardiolipin (PubMed:25598000). {ECO:0000269|PubMed:25598000}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}. Mitochondrion
CC {ECO:0000269|PubMed:17082194, ECO:0000269|PubMed:22941046}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766}.
CC -!- SUBCELLULAR LOCATION: [Isoform B]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:19700766}. Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:19700766}.
CC -!- SUBCELLULAR LOCATION: [Isoform C]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q9V6G5-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q9V6G5-2; Sequence=VSP_004450;
CC Name=C;
CC IsoId=Q9V6G5-3; Sequence=VSP_007017;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DISRUPTION PHENOTYPE: Cardiolipin (CL) deficiency, faster turnover,
CC abnormal CL fatty acyl composition and abnormal muscle mitochondria
CC (PubMed:17082194, PubMed:16855048, PubMed:19700766, PubMed:19114128,
CC PubMed:31110016). Poor motor performance of flight muscles
CC (PubMed:16855048, PubMed:19114128, PubMed:29405656). Significantly
CC reduced climbing speed and endurance which does not improve with
CC endurance training in contrast to wild-type flies (PubMed:16855048,
CC PubMed:29405656). Normal response to cardiac pacing (PubMed:29405656).
CC Male sterility (PubMed:19164547). Male-sterile phenotype can be
CC suppressed by genetic inactivation of iPLA2-VIA, which prevents CL
CC depletion and monolyso-CL accumulation without correcting the abnormal
CC CL acyl composition, suggesting that the abnormal levels of CL and/or
CC monolyso-CL are important pathogenetic factors (PubMed:19164547).
CC {ECO:0000269|PubMed:16855048, ECO:0000269|PubMed:17082194,
CC ECO:0000269|PubMed:19114128, ECO:0000269|PubMed:19164547,
CC ECO:0000269|PubMed:19700766, ECO:0000269|PubMed:29405656,
CC ECO:0000269|PubMed:31110016}.
CC -!- MISCELLANEOUS: The enzyme was named after a masochistic character
CC Tafazzi, once popular on Italian television, apparently due to the
CC difficulty encountered for its identification and characterization.
CC {ECO:0000250|UniProtKB:Q16635}.
CC -!- SIMILARITY: Belongs to the taffazin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD48409.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF148684; AAD48409.1; ALT_FRAME; mRNA.
DR EMBL; AE013599; AAF58461.2; -; Genomic_DNA.
DR EMBL; AE013599; AAF58462.3; -; Genomic_DNA.
DR EMBL; AE013599; AAM68652.2; -; Genomic_DNA.
DR EMBL; AY071059; AAL48681.1; -; mRNA.
DR EMBL; AF017783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001188916.1; NM_001201987.2. [Q9V6G5-2]
DR RefSeq; NP_477432.3; NM_058084.5. [Q9V6G5-1]
DR RefSeq; NP_725226.2; NM_165947.2. [Q9V6G5-2]
DR RefSeq; NP_725227.2; NM_165948.2. [Q9V6G5-3]
DR AlphaFoldDB; Q9V6G5; -.
DR BioGRID; 62178; 4.
DR DIP; DIP-22278N; -.
DR IntAct; Q9V6G5; 2.
DR STRING; 7227.FBpp0086975; -.
DR SwissLipids; SLP:000000123; -.
DR PaxDb; Q9V6G5; -.
DR DNASU; 36405; -.
DR EnsemblMetazoa; FBtr0087862; FBpp0086975; FBgn0026619. [Q9V6G5-1]
DR EnsemblMetazoa; FBtr0087863; FBpp0086976; FBgn0026619. [Q9V6G5-2]
DR EnsemblMetazoa; FBtr0087864; FBpp0086977; FBgn0026619. [Q9V6G5-3]
DR EnsemblMetazoa; FBtr0302455; FBpp0291643; FBgn0026619. [Q9V6G5-2]
DR GeneID; 36405; -.
DR KEGG; dme:Dmel_CG8766; -.
DR UCSC; CG8766-RA; d. melanogaster. [Q9V6G5-1]
DR CTD; 36405; -.
DR FlyBase; FBgn0026619; Taz.
DR VEuPathDB; VectorBase:FBgn0026619; -.
DR eggNOG; KOG2847; Eukaryota.
DR GeneTree; ENSGT00390000018621; -.
DR InParanoid; Q9V6G5; -.
DR OMA; GWPSIMP; -.
DR PhylomeDB; Q9V6G5; -.
DR Reactome; R-DME-1268020; Mitochondrial protein import.
DR Reactome; R-DME-1482798; Acyl chain remodeling of CL.
DR BioGRID-ORCS; 36405; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 36405; -.
DR PRO; PR:Q9V6G5; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0026619; Expressed in capitellum (Drosophila) and 35 other tissues.
DR ExpressionAtlas; Q9V6G5; baseline and differential.
DR Genevisible; Q9V6G5; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:FlyBase.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IDA:FlyBase.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0032577; F:phosphatidylcholine:cardiolipin O-linoleoyltransferase activity; IDA:FlyBase.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032048; P:cardiolipin metabolic process; IDA:UniProtKB.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0007006; P:mitochondrial membrane organization; IDA:FlyBase.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:UniProtKB.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497; PTHR12497; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR SMART; SM00563; PlsC; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Alternative splicing; Endoplasmic reticulum;
KW Golgi apparatus; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Phospholipid metabolism; Reference proteome; Transferase.
FT CHAIN 1..378
FT /note="Tafazzin"
FT /id="PRO_0000220933"
FT TOPO_DOM 1..137
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT INTRAMEM 138..158
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..378
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 46..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 188..193
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT COMPBIAS 63..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_004450"
FT VAR_SEQ 1..41
FT /note="MFMVVCSNLRRPGHVGAASAARNINWLISEGYTPPIRAMAR -> M (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_007017"
SQ SEQUENCE 378 AA; 43016 MW; 88690B6E2731FFB9 CRC64;
MFMVVCSNLR RPGHVGAASA ARNINWLISE GYTPPIRAMA RPYVQAPEAR PVPDERYPGS
QQDRKDIATQ TVRSSKPKDL RPPSPPTPSQ TLNSSSLPPP MSDQDADPSL DVPTGVAMPY
NIDWIFPRLR NPSKFWYVVS QFVVSAVGIF SKVVLMFLNK PRVYNRERLI QLITKRPKGI
PLVTVSNHYS CFDDPGLWGC LPLGIVCNTY KIRWSMAAHD ICFTNKLHSL FFMFGKCIPV
VRGIGVYQDA INLCIEKAAL GHWIHVFPEG KVNMDKEELR LKWGVGRIIY ESPKIPIILP
MWHEGMDDLL PNVEPYVIQR GKQVTLNVGQ PLDLNDFILD LKKRQVPEPT ARKLITDKIQ
EAFRDLRAET EKLHRERN
