TAZ_MOUSE
ID TAZ_MOUSE Reviewed; 262 AA.
AC Q91WF0; Q810E8;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Tafazzin {ECO:0000312|MGI:MGI:109626};
DE Short=Taz;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q16635};
GN Name=Tafazzin; Synonyms=Taz {ECO:0000312|MGI:MGI:109626};
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 {ECO:0000312|EMBL:AAH15305.1};
RN [1] {ECO:0000312|EMBL:AAO84333.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAO84333.1};
RA Lu B., Gong Y., Hatch G.M., Choy P.C.;
RT "Identification and characterization of murine tafazzins.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35860.1};
RC TISSUE=Spleen {ECO:0000312|EMBL:BAC35860.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000312|EMBL:AAH15305.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH15305.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH15305.1};
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 [5] {ECO:0000305}
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=15499385; DOI=10.1139/o04-055;
RA Lu B., Kelher M.R., Lee D.P., Lewin T.M., Coleman R.A., Choy P.C.,
RA Hatch G.M.;
RT "Complex expression pattern of the Barth syndrome gene product tafazzin in
RT human cell lines and murine tissues.";
RL Biochem. Cell Biol. 82:569-576(2004).
RN [6] {ECO:0000305}
RP FUNCTION.
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 [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21091282; DOI=10.1089/hum.2010.199;
RA Soustek M.S., Falk D.J., Mah C.S., Toth M.J., Schlame M., Lewin A.S.,
RA Byrne B.J.;
RT "Characterization of a transgenic short hairpin RNA-induced murine model of
RT Tafazzin deficiency.";
RL Hum. Gene Ther. 22:865-871(2011).
RN [8] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21068380; DOI=10.1074/jbc.m110.171439;
RA Acehan D., Vaz F., Houtkooper R.H., James J., Moore V., Tokunaga C.,
RA Kulik W., Wansapura J., Toth M.J., Strauss A., Khuchua Z.;
RT "Cardiac and skeletal muscle defects in a mouse model of human Barth
RT syndrome.";
RL J. Biol. Chem. 286:899-908(2011).
RN [9] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23130124; DOI=10.1161/jaha.111.000455;
RA Phoon C.K., Acehan D., Schlame M., Stokes D.L., Edelman-Novemsky I., Yu D.,
RA Xu Y., Viswanathan N., Ren M.;
RT "Tafazzin knockdown in mice leads to a developmental cardiomyopathy with
RT early diastolic dysfunction preceding myocardial noncompaction.";
RL J. Am. Heart Assoc. 1:e000455-e000455(2012).
RN [10] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=23616771; DOI=10.3389/fphys.2013.00074;
RA Powers C., Huang Y., Strauss A., Khuchua Z.;
RT "Diminished Exercise Capacity and Mitochondrial bc1 Complex Deficiency in
RT Tafazzin-Knockdown Mice.";
RL Front. Physiol. 4:74-74(2013).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=25919711; DOI=10.1080/15548627.2015.1023984;
RA Hsu P., Liu X., Zhang J., Wang H.G., Ye J.M., Shi Y.;
RT "Cardiolipin remodeling by TAZ/tafazzin is selectively required for the
RT initiation of mitophagy.";
RL Autophagy 11:643-652(2015).
RN [12] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26114544; DOI=10.1371/journal.pone.0131066;
RA Cadalbert L.C., Ghaffar F.N., Stevenson D., Bryson S., Vaz F.M.,
RA Gottlieb E., Strathdee D.;
RT "Mouse Tafazzin Is Required for Male Germ Cell Meiosis and
RT Spermatogenesis.";
RL PLoS ONE 10:e0131066-e0131066(2015).
RN [13] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30055293; DOI=10.1016/j.bbadis.2018.07.022;
RA Cole L.K., Kim J.H., Amoscato A.A., Tyurina Y.Y., Bay R.H., Karimi B.,
RA Siddiqui T.J., Kagan V.E., Hatch G.M., Kauppinen T.M.;
RT "Aberrant cardiolipin metabolism is associated with cognitive deficiency
RT and hippocampal alteration in tafazzin knockdown mice.";
RL Biochim. Biophys. Acta 1864:3353-3367(2018).
RN [14] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30389594; DOI=10.1016/j.mito.2018.10.005;
RA Kim J., Lee K., Fujioka H., Tandler B., Hoppel C.L.;
RT "Cardiac mitochondrial structure and function in tafazzin-knockdown mice.";
RL Mitochondrion 43:53-62(2018).
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 (PubMed:19114128, PubMed:21091282, PubMed:21068380,
CC PubMed:23130124, PubMed:26114544, PubMed:30055293, PubMed:30389594).
CC Its role in cellular physiology is to improve mitochondrial performance
CC (By similarity). CL is critical for the coassembly of lipids and
CC proteins in mitochondrial membranes, for instance, remodeling of the
CC acyl groups of CL in the mitochondrial inner membrane affects the
CC assembly and stability of respiratory chain complex IV and its
CC supercomplex forms (By similarity). Catalyzes the transacylacion
CC between phospholipids and lysophospholipids, with the highest rate
CC being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-
CC phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-
CC phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL
CC transacylation, that means, it exchanges acyl groups between CL and PC
CC by a combination of forward and reverse transacylations. Also catalyzes
CC transacylations between other phospholipids such as
CC phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine
CC or PE) and CL, between PC and PE, and between PC and phosphatidate
CC (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not
CC regiospecific, it transfers acyl groups into any of the sn-1 and sn-2
CC positions of the monolysocardiolipin (MLCL), which is an important
CC prerequisite for uniformity and symmetry in CL acyl distribution.
CC Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is
CC limited to that of an acyl acceptor. CoA-independent, it can reshuffle
CC molecular species within a single phospholipid class. Redistributes
CC fatty acids between MLCL, CL, and other lipids, which prolongs the
CC half-life of CL. Its action is completely reversible, which allows for
CC cyclic changes, such as fission and fusion or bending and flattening of
CC the membrane. Hence, by contributing to the flexibility of the lipid
CC composition, it plays an important role in the dynamics of mitochondria
CC membranes. Essential for the final stage of spermatogenesis, spermatid
CC individualization (By similarity). Required for the initiation of
CC mitophagy (PubMed:25919711). Required to ensure progression of
CC spermatocytes through meiosis (PubMed:26114544).
CC {ECO:0000250|UniProtKB:Q06510, ECO:0000250|UniProtKB:Q16635,
CC ECO:0000250|UniProtKB:Q9V6G5, ECO:0000269|PubMed:19114128,
CC ECO:0000269|PubMed:21068380, ECO:0000269|PubMed:21091282,
CC ECO:0000269|PubMed:23130124, ECO:0000269|PubMed:25919711,
CC ECO:0000269|PubMed:26114544, ECO:0000269|PubMed:30055293,
CC ECO:0000269|PubMed:30389594}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1-acyl-
CC sn-glycero-3-phosphate = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)
CC + a 1,2-diacyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:67748,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58608, ChEBI:CHEBI:64716,
CC ChEBI:CHEBI:64840; Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + 1-hexadecanoyl-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-
CC (9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate +
CC 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol);
CC Xref=Rhea:RHEA:67752, ChEBI:CHEBI:72840, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74563, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
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:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + 2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:68988,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
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:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q16635}.
CC -!- SUBUNIT: Associates with multiple protein complexes.
CC {ECO:0000250|UniProtKB:Q16635}.
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Full-length {ECO:0000303|PubMed:15499385};
CC IsoId=Q91WF0-1; Sequence=Displayed;
CC Name=2; Synonyms=Exon-9-deleted {ECO:0000303|PubMed:15499385};
CC IsoId=Q91WF0-2; Sequence=VSP_061044, VSP_061045;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest expression in
CC skeletal muscle and kidney. {ECO:0000269|PubMed:15499385}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DISRUPTION PHENOTYPE: Impaired cardiolipin (CL) metabolism with
CC accumulation of monolysocardiolipin (MLCL) and reduction of mature CL
CC in embryonic stem cells, male sterility, reduced testis size and
CC disruption in progression of spermatocytes through meiosis
CC (PubMed:26114544). Spermatocytes fail to progress past the pachytene
CC stage of meiosis and have higher levels of DNA double strand damage and
CC increased levels of endogenous retrotransposon activity
CC (PubMed:26114544). RNAi-mediated knockdown results in prenatal and
CC perinatal lethality, impaired CL metabolism resulting in absence of
CC tetralineoyl-cardiolipin and accumulation of MLCL in cardiac and
CC skeletal muscle, abnormal ultrastructure of mitochondria and
CC mitochondrial-associated membranes, impaired skeletal muscle
CC contractile properties, early diastolic dysfunction, and cardiac
CC abnormalities such as myocardial thinning, hypertrabeculation, non-
CC compaction, defective ventricular septation and left ventricular
CC dilation (PubMed:21091282, PubMed:21068380, PubMed:23130124,
CC PubMed:30389594). RNAi-mediated knockdown also results in impaired CL
CC metabolism in the brain with reduced total CL levels and significantly
CC increased MLCL levels, impaired brain mitochondrial respiration,
CC elevated brain production of reactive oxygen species, significant
CC memory deficiency, derangement of the hippocampal CA1 neuronal layer
CC and elevated microglia activity (PubMed:30055293). Hepatic CL levels
CC remain normal (PubMed:30055293). RNAi-mediated knockdown does not
CC affect resting metabolic rate but markedly impairs oxygen consumption
CC rates during exercise and diminishes mitochondrial complex III activity
CC (PubMed:23616771). {ECO:0000269|PubMed:21068380,
CC ECO:0000269|PubMed:21091282, ECO:0000269|PubMed:23130124,
CC ECO:0000269|PubMed:23616771, ECO:0000269|PubMed:26114544,
CC ECO:0000269|PubMed:30055293, ECO:0000269|PubMed:30389594}.
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.
CC {ECO:0000255|RuleBase:RU365062}.
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DR EMBL; AY231459; AAO84333.1; -; mRNA.
DR EMBL; AY231460; AAO84334.1; -; mRNA.
DR EMBL; AK075615; BAC35860.1; -; mRNA.
DR EMBL; AK160327; BAE35740.1; -; mRNA.
DR EMBL; AL807376; CAM24340.1; -; Genomic_DNA.
DR EMBL; BC015305; AAH15305.1; -; mRNA.
DR CCDS; CCDS30224.1; -. [Q91WF0-1]
DR CCDS; CCDS57764.1; -. [Q91WF0-2]
DR RefSeq; NP_001229545.1; NM_001242616.2. [Q91WF0-2]
DR RefSeq; NP_001277667.1; NM_001290738.1.
DR RefSeq; NP_852657.1; NM_181516.6. [Q91WF0-1]
DR RefSeq; XP_006528309.1; XM_006528246.2. [Q91WF0-1]
DR RefSeq; XP_006528313.1; XM_006528250.3. [Q91WF0-2]
DR AlphaFoldDB; Q91WF0; -.
DR MaxQB; Q91WF0; -.
DR ProteomicsDB; 330377; -.
DR ProteomicsDB; 335234; -.
DR Antibodypedia; 31212; 457 antibodies from 37 providers.
DR DNASU; 66826; -.
DR Ensembl; ENSMUST00000069722; ENSMUSP00000065270; ENSMUSG00000009995. [Q91WF0-1]
DR Ensembl; ENSMUST00000124200; ENSMUSP00000134745; ENSMUSG00000009995. [Q91WF0-2]
DR GeneID; 66826; -.
DR KEGG; mmu:66826; -.
DR UCSC; uc009tog.3; mouse. [Q91WF0-1]
DR UCSC; uc009toi.3; mouse.
DR CTD; 6901; -.
DR MGI; MGI:109626; Taz.
DR VEuPathDB; HostDB:ENSMUSG00000009995; -.
DR GeneTree; ENSGT00390000018621; -.
DR PhylomeDB; Q91WF0; -.
DR BioGRID-ORCS; 66826; 19 hits in 75 CRISPR screens.
DR ChiTaRS; Taz; mouse.
DR Proteomes; UP000000589; Chromosome X.
DR Bgee; ENSMUSG00000009995; Expressed in retinal neural layer and 248 other tissues.
DR ExpressionAtlas; Q91WF0; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISO:MGI.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR GO; GO:0048738; P:cardiac muscle tissue development; ISO:MGI.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; ISO:MGI.
DR GO; GO:0032048; P:cardiolipin metabolic process; IMP:UniProtKB.
DR GO; GO:0042407; P:cristae formation; ISO:MGI.
DR GO; GO:0007507; P:heart development; ISO:MGI.
DR GO; GO:0003007; P:heart morphogenesis; IMP:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISO:MGI.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISO:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; ISO:MGI.
DR GO; GO:0046471; P:phosphatidylglycerol metabolic process; ISO:MGI.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI.
DR GO; GO:1900210; P:positive regulation of cardiolipin metabolic process; ISO:MGI.
DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:MGI.
DR GO; GO:0048137; P:spermatocyte division; 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 2: Evidence at transcript level;
KW Acyltransferase; Alternative splicing; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..262
FT /note="Tafazzin"
FT /id="PRO_0000452721"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT INTRAMEM 15..35
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..262
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 82..92
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 155..190
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT MOTIF 69..74
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT VAR_SEQ 186..201
FT /note="GMNDVLPNSPPYFPRF -> ENHRADWEALQYTPCA (in isoform 2)"
FT /id="VSP_061044"
FT VAR_SEQ 202..262
FT /note="Missing (in isoform 2)"
FT /id="VSP_061045"
SQ SEQUENCE 262 AA; 30334 MW; C13EFE1B933957BA CRC64;
MPLHVKWPFP AVPRLTWTLA SSVVMGLVGT YSCFWTKYMN HLTVHNKEVL YELIENRGPA
TPLITVSNHQ SCMDDPHLWG ILKLRHIWNL KLMRWTPAAA DICFTKELHS HFFSLGKCVP
VCRGDGVYQK GMDFILEKLN HGDWVHIFPE GKVNMSSEFL RFKWGIGRLI AECHLNPIIL
PLWHVGMNDV LPNSPPYFPR FGQKITVLIG KPFSTLPVLE RLRAENKSAV EMRKALTDFI
QEEFQRLKMQ AEQLHNHFQP GR
