TAZ_HUMAN
ID TAZ_HUMAN Reviewed; 262 AA.
AC Q16635; A3KQT2; D3DWX2; Q5HY43; Q5HY44; Q5HY45; Q5HY48; Q86XQ6; Q86XQ7;
AC Q86XQ8; Q86XQ9; Q86XR0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Tafazzin {ECO:0000303|PubMed:19700766, ECO:0000303|PubMed:25598000, ECO:0000303|PubMed:29129703, ECO:0000303|PubMed:33096711};
DE Short=Taz;
DE EC=2.3.1.- {ECO:0000269|PubMed:19700766};
DE AltName: Full=Protein G4.5 {ECO:0000303|PubMed:8630491};
GN Name=TAFAZZIN {ECO:0000312|HGNC:HGNC:11577};
GN Synonyms=EFE2, G4.5 {ECO:0000303|PubMed:8630491},
GN TAZ {ECO:0000303|PubMed:12930833};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Heart, and Skeletal muscle;
RX PubMed=8630491; DOI=10.1038/ng0496-385;
RA Bione S., D'Adamo P., Maestrini E., Gedeon A.K., Bolhuis P.A., Toniolo D.;
RT "A novel X-linked gene, G4.5. is responsible for Barth syndrome.";
RL Nat. Genet. 12:385-389(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5; 6; 7; 8 AND 9).
RA Lu B., Gong Y., Hatch G.M., Choy P.C.;
RT "Identification and characterization of human tafazzins.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION (ISOFORMS 1; 3 AND 5), CATALYTIC ACTIVITY (ISOFORMS 1 AND 3), AND
RP PATHWAY.
RX PubMed=12930833; DOI=10.1074/jbc.m305956200;
RA Vaz F.M., Houtkooper R.H., Valianpour F., Barth P.G., Wanders R.J.;
RT "Only one splice variant of the human TAZ gene encodes a functional protein
RT with a role in cardiolipin metabolism.";
RL J. Biol. Chem. 278:43089-43094(2003).
RN [7]
RP ALTERNATIVE SPLICING (ISOFORMS 1; 3; 5 AND 7).
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 [8]
RP FUNCTION (ISOFORM 3), AND CATALYTIC ACTIVITY (ISOFORM 3).
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 (ISOFORMS 1; 3; 5 AND 7), SUBUNIT, CATALYTIC ACTIVITY (ISOFORMS 1
RP AND 3), SUBCELLULAR LOCATION (ISOFORMS 1; 3; 5 AND 7), 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.
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 [11]
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 [12]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS
RP BTHS LEU-57 AND GLN-69.
RX PubMed=26908608; DOI=10.1093/hmg/ddw046;
RA Lu Y.W., Galbraith L., Herndon J.D., Lu Y.L., Pras-Raves M., Vervaart M.,
RA Van Kampen A., Luyf A., Koehler C.M., McCaffery J.M., Gottlieb E.,
RA Vaz F.M., Claypool S.M.;
RT "Defining functional classes of Barth syndrome mutation in humans.";
RL Hum. Mol. Genet. 25:1754-1770(2016).
RN [13]
RP SUBCELLULAR LOCATION (ISOFORMS 1 AND 3), MITOCHONDRIAL TARGETING SEQUENCES,
RP AND CHARACTERIZATION OF VARIANTS BTHS SER-94; ARG-167; ASN-179; ARG-180;
RP PRO-182 AND ARG-184.
RX PubMed=29129703; DOI=10.1016/j.yjmcc.2017.11.005;
RA Dinca A.A., Chien W.M., Chin M.T.;
RT "Identification of novel mitochondrial localization signals in human
RT Tafazzin, the cause of the inherited cardiomyopathic disorder Barth
RT syndrome.";
RL J. Mol. Cell. Cardiol. 114:83-92(2018).
RN [14]
RP FUNCTION.
RX PubMed=32234310; DOI=10.1016/j.jmb.2020.03.026;
RA Schlame M., Xu Y.;
RT "The Function of Tafazzin, a Mitochondrial Phospholipid-Lysophospholipid
RT Acyltransferase.";
RL J. Mol. Biol. 432:5043-5051(2020).
RN [15]
RP FUNCTION.
RX PubMed=33096711; DOI=10.3390/cells9102333;
RA Petit P.X., Ardilla-Osorio H., Penalvia L., Rainey N.E.;
RT "Tafazzin Mutation Affecting Cardiolipin Leads to Increased Mitochondrial
RT Superoxide Anions and Mitophagy Inhibition in Barth Syndrome.";
RL Cells 9:2333-2333(2020).
RN [16]
RP 3D-STRUCTURE MODELING.
RX PubMed=25941633; DOI=10.1016/j.mgene.2015.04.001;
RA Hijikata A., Yura K., Ohara O., Go M.;
RT "Structural and functional analyses of Barth syndrome-causing mutations and
RT alternative splicing in the tafazzin acyltransferase domain.";
RL Meta Gene 4:92-106(2015).
RN [17]
RP VARIANT BTHS ARG-210.
RX PubMed=9382096; DOI=10.1086/514886;
RA D'Adamo P., Fassone L., Gedeon A., Janssen E.A., Bione S., Bolhuis P.A.,
RA Barth P.G., Wilson M., Haan E., Orstavik K.H., Patton M.A., Green A.J.,
RA Zammarchi E., Donati M.A., Toniolo D.;
RT "The X-linked gene G4.5 is responsible for different infantile dilated
RT cardiomyopathies.";
RL Am. J. Hum. Genet. 61:862-867(1997).
RN [18]
RP VARIANT BTHS ARG-167.
RX PubMed=9382097; DOI=10.1086/514879;
RA Bleyl S.B., Mumford B.R., Thompson V., Carey J.C., Pysher T.J., Chin T.K.,
RA Ward K.;
RT "Neonatal, lethal noncompaction of the left ventricular myocardium is
RT allelic with Barth syndrome.";
RL Am. J. Hum. Genet. 61:868-872(1997).
RN [19]
RP VARIANT BTHS ARG-118.
RX PubMed=11238270; DOI=10.1161/01.cir.103.9.1256;
RA Ichida F., Tsubata S., Bowles K.R., Haneda N., Uese K., Miyawaki T.,
RA Dreyer W.J., Messina J., Li H., Bowles N.E., Towbin J.A.;
RT "Novel gene mutations in patients with left ventricular noncompaction or
RT Barth syndrome.";
RL Circulation 103:1256-1263(2001).
RN [20]
RP VARIANT BTHS SER-94.
RX PubMed=12032589; DOI=10.1007/s100380200030;
RA Sakamoto O., Kitoh T., Ohura T., Ohya N., Iinuma K.;
RT "Novel missense mutation (R94S) in the TAZ (G4.5) gene in a Japanese
RT patient with Barth syndrome.";
RL J. Hum. Genet. 47:229-231(2002).
RN [21]
RP VARIANTS BTHS 123-ARG--ARG-292 DEL AND ARG-184.
RX PubMed=23409742; DOI=10.1186/1750-1172-8-27;
RA Ferri L., Donati M.A., Funghini S., Malvagia S., Catarzi S., Lugli L.,
RA Ragni L., Bertini E., Vaz F.M., Cooper D.N., Guerrini R., Morrone A.;
RT "New clinical and molecular insights on Barth syndrome.";
RL Orphanet J. Rare Dis. 8:27-27(2013).
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:12930833, PubMed:19700766, PubMed:19164547,
CC PubMed:26908608, PubMed:33096711). Its role in cellular physiology is
CC to improve mitochondrial performance (PubMed:32234310). CL is critical
CC for the coassembly of lipids and proteins in mitochondrial membranes,
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. 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:33096711). Required to ensure progression of
CC spermatocytes through meiosis (By similarity). Exon 7 of human tafazzin
CC is essential for catalysis (PubMed:19700766).
CC {ECO:0000250|UniProtKB:Q06510, ECO:0000250|UniProtKB:Q91WF0,
CC ECO:0000250|UniProtKB:Q9V6G5, ECO:0000269|PubMed:12930833,
CC ECO:0000269|PubMed:19164547, ECO:0000269|PubMed:19700766,
CC ECO:0000269|PubMed:26908608, ECO:0000269|PubMed:33096711,
CC ECO:0000303|PubMed:19700766, ECO:0000303|PubMed:32234310}.
CC -!- FUNCTION: [Isoform 1]: Catalyzes the transacylation between
CC lysophosphatidate (such as 1-acyl-sn-glycero-3-phosphate) and
CC phosphatidylglycerol (1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol))
CC (PubMed:19700766). Contributes to cardiolipin (1',3'-bis-[1,2-diacyl-
CC sn-glycero-3-phospho]-glycerol or CL) remodeling (PubMed:12930833,
CC PubMed:19700766). {ECO:0000269|PubMed:12930833,
CC ECO:0000269|PubMed:19700766}.
CC -!- FUNCTION: [Isoform 3]: Catalyzes the transacylation between
CC lysophospholipids and phospholipids, and plays a fundamental role in
CC cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or
CC CL) metabolism and remodeling. {ECO:0000269|PubMed:12930833,
CC ECO:0000269|PubMed:19416660, ECO:0000269|PubMed:19700766}.
CC -!- FUNCTION: [Isoform 5]: Catalytically inactive.
CC {ECO:0000269|PubMed:12930833, ECO:0000269|PubMed:19700766}.
CC -!- FUNCTION: [Isoform 7]: Catalytically inactive.
CC {ECO:0000269|PubMed:19700766}.
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
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:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:0000269|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000269|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:0000305|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989;
CC Evidence={ECO:0000305|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:0000305|PubMed:19700766};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000305|PubMed:19700766};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000305|PubMed:19700766};
CC -!- CATALYTIC ACTIVITY: [Isoform 3]:
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:0000305|PubMed:12930833, ECO:0000305|PubMed:19416660};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000305|PubMed:12930833, ECO:0000305|PubMed:19416660};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000305|PubMed:12930833, ECO:0000305|PubMed:19416660};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:12930833,
CC ECO:0000305|PubMed:19700766}.
CC -!- SUBUNIT: Associates with multiple protein complexes.
CC {ECO:0000269|PubMed:19700766, ECO:0000269|PubMed:25598000,
CC ECO:0000269|PubMed:26908608}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:26908608}; Peripheral membrane protein
CC {ECO:0000305|PubMed:26908608}; Intermembrane side
CC {ECO:0000305|PubMed:26908608}. Mitochondrion inner membrane
CC {ECO:0000269|PubMed:26908608}; Peripheral membrane protein
CC {ECO:0000305|PubMed:26908608}; Intermembrane side
CC {ECO:0000305|PubMed:26908608}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766, ECO:0000269|PubMed:29129703}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766, ECO:0000269|PubMed:29129703}.
CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 7]: Mitochondrion membrane
CC {ECO:0000269|PubMed:19700766}.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Cytoplasm {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 9]: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=3; Synonyms=Del_exon_5, TAZ-delta5 {ECO:0000303|PubMed:19700766},
CC Exon-5-deleted {ECO:0000303|PubMed:15499385};
CC IsoId=Q16635-3; Sequence=Displayed;
CC Name=1; Synonyms=TAZ-FL {ECO:0000303|PubMed:19700766}, Full-length
CC {ECO:0000303|PubMed:15499385};
CC IsoId=Q16635-1; Sequence=VSP_061366;
CC Name=2; Synonyms=Short;
CC IsoId=Q16635-2; Sequence=VSP_061365, VSP_061366;
CC Name=4; Synonyms=Del_exon_6;
CC IsoId=Q16635-4; Sequence=VSP_061367;
CC Name=5; Synonyms=Del_exon_7, TAZ-delta7 {ECO:0000303|PubMed:19700766},
CC Exon-7-deleted {ECO:0000303|PubMed:15499385};
CC IsoId=Q16635-5; Sequence=VSP_061366, VSP_061368;
CC Name=6;
CC IsoId=Q16635-6; Sequence=VSP_061365, VSP_061366, VSP_061368;
CC Name=7; Synonyms=TAZ-delta5-delta7 {ECO:0000303|PubMed:19700766},
CC Exons-5+7-deleted {ECO:0000303|PubMed:15499385};
CC IsoId=Q16635-7; Sequence=VSP_061368;
CC Name=8;
CC IsoId=Q16635-8; Sequence=VSP_061365;
CC Name=9;
CC IsoId=Q16635-9; Sequence=VSP_061365, VSP_061368;
CC -!- TISSUE SPECIFICITY: High levels in cardiac and skeletal muscle. Up to
CC 10 isoforms can be present in different amounts in different tissues.
CC Most isoforms are ubiquitous. Isoforms that lack the N-terminus are
CC found in leukocytes and fibroblasts, but not in heart and skeletal
CC muscle. Some forms appear restricted to cardiac and skeletal muscle or
CC to leukocytes.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DISEASE: Barth syndrome (BTHS) [MIM:302060]: An X-linked disease
CC characterized by dilated cardiomyopathy with endocardial
CC fibroelastosis, a predominantly proximal skeletal myopathy, growth
CC retardation, neutropenia, and organic aciduria, particularly excess of
CC 3-methylglutaconic acid. Additional features include hypertrophic
CC cardiomyopathy, isolated left ventricular non-compaction, ventricular
CC arrhythmia, motor delay, poor appetite, fatigue and exercise
CC intolerance, hypoglycemia, lactic acidosis, hyperammonemia, and
CC dramatic late catch-up growth after growth delay throughout childhood.
CC {ECO:0000269|PubMed:11238270, ECO:0000269|PubMed:12032589,
CC ECO:0000269|PubMed:23409742, ECO:0000269|PubMed:26908608,
CC ECO:0000269|PubMed:29129703, ECO:0000269|PubMed:9382096,
CC ECO:0000269|PubMed:9382097}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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:0000303|PubMed:8630491}.
CC -!- SIMILARITY: Belongs to the taffazin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=TAZbase; Note=TAZ mutation db;
CC URL="http://structure.bmc.lu.se/idbase/TAZbase/";
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DR EMBL; X92763; CAA63419.1; -; Genomic_DNA.
DR EMBL; X92764; CAA63419.1; JOINED; Genomic_DNA.
DR EMBL; X92762; CAA63418.1; -; mRNA.
DR EMBL; AY231461; AAO84335.1; -; mRNA.
DR EMBL; AY231462; AAO84336.1; -; mRNA.
DR EMBL; AY231463; AAO84337.1; -; mRNA.
DR EMBL; AY231464; AAO84338.1; -; mRNA.
DR EMBL; AY258036; AAO84339.1; -; mRNA.
DR EMBL; AY258037; AAO84340.1; -; mRNA.
DR EMBL; AY258038; AAO84341.1; -; mRNA.
DR EMBL; AY258039; AAO84342.1; -; mRNA.
DR EMBL; AK291848; BAF84537.1; -; mRNA.
DR EMBL; BX936347; CAI43207.1; -; Genomic_DNA.
DR EMBL; BX936347; CAI43208.1; -; Genomic_DNA.
DR EMBL; BX936347; CAI43209.1; -; Genomic_DNA.
DR EMBL; BX936347; CAI43211.1; -; Genomic_DNA.
DR EMBL; BX936347; CAM45851.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72720.1; -; Genomic_DNA.
DR EMBL; CH471172; EAW72728.1; -; Genomic_DNA.
DR CCDS; CCDS14748.1; -. [Q16635-1]
DR CCDS; CCDS14749.1; -. [Q16635-3]
DR CCDS; CCDS14750.1; -. [Q16635-5]
DR CCDS; CCDS35450.1; -. [Q16635-7]
DR RefSeq; NP_000107.1; NM_000116.4. [Q16635-1]
DR RefSeq; NP_001290394.1; NM_001303465.1.
DR RefSeq; NP_851828.1; NM_181311.3. [Q16635-3]
DR RefSeq; NP_851829.1; NM_181312.3. [Q16635-5]
DR RefSeq; NP_851830.1; NM_181313.3. [Q16635-7]
DR AlphaFoldDB; Q16635; -.
DR BioGRID; 112764; 206.
DR IntAct; Q16635; 69.
DR STRING; 9606.ENSP00000469981; -.
DR iPTMnet; Q16635; -.
DR PhosphoSitePlus; Q16635; -.
DR BioMuta; TAZ; -.
DR DMDM; 2498992; -.
DR EPD; Q16635; -.
DR jPOST; Q16635; -.
DR MassIVE; Q16635; -.
DR MaxQB; Q16635; -.
DR PaxDb; Q16635; -.
DR PeptideAtlas; Q16635; -.
DR PRIDE; Q16635; -.
DR ProteomicsDB; 60983; -. [Q16635-1]
DR ProteomicsDB; 60984; -. [Q16635-2]
DR ProteomicsDB; 60985; -. [Q16635-3]
DR ProteomicsDB; 60986; -. [Q16635-4]
DR ProteomicsDB; 60987; -. [Q16635-5]
DR ProteomicsDB; 60988; -. [Q16635-6]
DR ProteomicsDB; 60989; -. [Q16635-7]
DR ProteomicsDB; 60990; -. [Q16635-8]
DR ProteomicsDB; 60991; -. [Q16635-9]
DR ABCD; Q16635; 1 sequenced antibody.
DR Antibodypedia; 31212; 457 antibodies from 37 providers.
DR DNASU; 6901; -.
DR Ensembl; ENST00000601016.6; ENSP00000469981.1; ENSG00000102125.16. [Q16635-1]
DR Ensembl; ENST00000612012.5; ENSP00000482070.2; ENSG00000102125.16. [Q16635-5]
DR Ensembl; ENST00000612460.5; ENSP00000481037.1; ENSG00000102125.16. [Q16635-3]
DR Ensembl; ENST00000613002.4; ENSP00000478154.1; ENSG00000102125.16. [Q16635-7]
DR GeneID; 6901; -.
DR KEGG; hsa:6901; -.
DR MANE-Select; ENST00000601016.6; ENSP00000469981.1; NM_000116.5; NP_000107.1. [Q16635-1]
DR UCSC; uc033fbm.2; human. [Q16635-3]
DR CTD; 6901; -.
DR DisGeNET; 6901; -.
DR GeneCards; TAFAZZIN; -.
DR GeneReviews; TAFAZZIN; -.
DR HGNC; HGNC:11577; TAFAZZIN.
DR HPA; ENSG00000102125; Low tissue specificity.
DR MalaCards; TAFAZZIN; -.
DR MIM; 300394; gene.
DR MIM; 302060; phenotype.
DR neXtProt; NX_Q16635; -.
DR OpenTargets; ENSG00000102125; -.
DR Orphanet; 111; Barth syndrome.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR VEuPathDB; HostDB:ENSG00000102125; -.
DR eggNOG; KOG2847; Eukaryota.
DR GeneTree; ENSGT00390000018621; -.
DR InParanoid; Q16635; -.
DR OrthoDB; 215180at2759; -.
DR PhylomeDB; Q16635; -.
DR TreeFam; TF313862; -.
DR PathwayCommons; Q16635; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-1482798; Acyl chain remodeling of CL.
DR SignaLink; Q16635; -.
DR BioGRID-ORCS; 6901; 137 hits in 725 CRISPR screens.
DR ChiTaRS; TAZ; human.
DR GeneWiki; Tafazzin; -.
DR GenomeRNAi; 6901; -.
DR Pharos; Q16635; Tbio.
DR PRO; PR:Q16635; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q16635; protein.
DR Bgee; ENSG00000102125; Expressed in apex of heart and 161 other tissues.
DR ExpressionAtlas; Q16635; baseline and differential.
DR Genevisible; Q16635; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:BHF-UCL.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; TAS:Reactome.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:BHF-UCL.
DR GO; GO:0048738; P:cardiac muscle tissue development; IMP:HGNC-UCL.
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:0042407; P:cristae formation; IMP:HGNC-UCL.
DR GO; GO:0007507; P:heart development; IMP:HGNC-UCL.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IMP:HGNC-UCL.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IDA:BHF-UCL.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:HGNC-UCL.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; IMP:UniProtKB.
DR GO; GO:0006936; P:muscle contraction; IMP:HGNC-UCL.
DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IEA:Ensembl.
DR GO; GO:1900210; P:positive regulation of cardiolipin metabolic process; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:HGNC-UCL.
DR GO; GO:0048137; P:spermatocyte division; ISS: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; Cardiomyopathy; Cytoplasm;
KW Disease variant; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..262
FT /note="Tafazzin"
FT /id="PRO_0000220928"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:26908608"
FT INTRAMEM 15..35
FT /evidence="ECO:0000305|PubMed:26908608"
FT TOPO_DOM 36..262
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:26908608"
FT REGION 82..92
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000269|PubMed:29129703"
FT REGION 155..190
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000269|PubMed:29129703"
FT MOTIF 69..74
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 2, isoform 6, isoform 8 and
FT isoform 9)"
FT /id="VSP_061365"
FT VAR_SEQ 123
FT /note="R -> RGAEFFQAENEGKGVLDTGRHMPGAGKRREK (in isoform 1,
FT isoform 2, isoform 5 and isoform 6)"
FT /id="VSP_061366"
FT VAR_SEQ 125..150
FT /note="DGVYQKGMDFILEKLNHGDWVHIFPE -> AEFFQAENEGKGVLDTGRHMPG
FT AGKRREK (in isoform 4)"
FT /id="VSP_061367"
FT VAR_SEQ 151..164
FT /note="Missing (in isoform 5, isoform 6, isoform 7 and
FT isoform 9)"
FT /id="VSP_061368"
FT VARIANT 57
FT /note="R -> L (in BTHS; unstable protein)"
FT /evidence="ECO:0000269|PubMed:26908608"
FT /id="VAR_084500"
FT VARIANT 69
FT /note="H -> Q (in BTHS; abolishes catalytic activity;
FT dbSNP:rs1557191125)"
FT /evidence="ECO:0000269|PubMed:26908608"
FT /id="VAR_084501"
FT VARIANT 94
FT /note="R -> S (in BTHS; does not affect mitochondrial
FT localization; dbSNP:rs104894942)"
FT /evidence="ECO:0000269|PubMed:12032589,
FT ECO:0000269|PubMed:29129703"
FT /id="VAR_014110"
FT VARIANT 118
FT /note="C -> R (in BTHS; dbSNP:rs104894937)"
FT /evidence="ECO:0000269|PubMed:11238270"
FT /id="VAR_014111"
FT VARIANT 123..262
FT /note="Missing (in BTHS)"
FT /evidence="ECO:0000269|PubMed:23409742"
FT /id="VAR_084502"
FT VARIANT 167
FT /note="G -> R (in BTHS; does not affect mitochondrial
FT localization; dbSNP:rs132630277)"
FT /evidence="ECO:0000269|PubMed:29129703,
FT ECO:0000269|PubMed:9382097"
FT /id="VAR_014112"
FT VARIANT 179
FT /note="I -> N (in BTHS; does not affect mitochondrial
FT localization)"
FT /evidence="ECO:0000269|PubMed:29129703"
FT /id="VAR_084503"
FT VARIANT 180
FT /note="L -> R (in BTHS; does not affect mitochondrial
FT localization)"
FT /evidence="ECO:0000269|PubMed:29129703"
FT /id="VAR_084504"
FT VARIANT 182
FT /note="L -> P (in BTHS; does not affect mitochondrial
FT localization)"
FT /evidence="ECO:0000269|PubMed:29129703"
FT /id="VAR_084505"
FT VARIANT 184
FT /note="H -> R (in BTHS; does not affect mitochondrial
FT localization)"
FT /evidence="ECO:0000269|PubMed:23409742,
FT ECO:0000269|PubMed:29129703"
FT /id="VAR_084506"
FT VARIANT 210
FT /note="G -> R (in BTHS; dbSNP:rs387907218)"
FT /evidence="ECO:0000269|PubMed:9382096"
FT /id="VAR_068434"
SQ SEQUENCE 262 AA; 30203 MW; AE7F4EBF505C7F63 CRC64;
MPLHVKWPFP AVPPLTWTLA SSVVMGLVGT YSCFWTKYMN HLTVHNREVL YELIEKRGPA
TPLITVSNHQ SCMDDPHLWG ILKLRHIWNL KLMRWTPAAA DICFTKELHS HFFSLGKCVP
VCRGDGVYQK GMDFILEKLN HGDWVHIFPE GKVNMSSEFL RFKWGIGRLI AECHLNPIIL
PLWHVGMNDV LPNSPPYFPR FGQKITVLIG KPFSALPVLE RLRAENKSAV EMRKALTDFI
QEEFQHLKTQ AEQLHNHLQP GR
