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 27-MAR-2024, entry version 192. 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}, TAZ GN {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 transacylation 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/"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; Q16635; -. DR BioGRID; 112764; 215. DR IntAct; Q16635; 70. DR MINT; Q16635; -. 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; 9606-ENSP00000469981; -. DR PeptideAtlas; 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 Pumba; Q16635; -. DR ABCD; Q16635; 1 sequenced antibody. DR Antibodypedia; 31212; 488 antibodies from 37 providers. DR DNASU; 6901; -. DR Ensembl; ENST00000601016.6; ENSP00000469981.1; ENSG00000102125.17. [Q16635-1] DR Ensembl; ENST00000612012.5; ENSP00000482070.2; ENSG00000102125.17. [Q16635-5] DR Ensembl; ENST00000612460.5; ENSP00000481037.1; ENSG00000102125.17. [Q16635-3] DR Ensembl; ENST00000613002.4; ENSP00000478154.1; ENSG00000102125.17. [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 AGR; HGNC:11577; -. 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; 1387at2759; -. 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; 148 hits in 801 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 163 other cell types or tissues. DR ExpressionAtlas; Q16635; baseline and differential. 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; TAS:Reactome. 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 CDD; cd07989; LPLAT_AGPAT-like; 1. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR InterPro; IPR000872; Tafazzin. DR PANTHER; PTHR12497:SF0; TAFAZZIN; 1. DR PANTHER; PTHR12497; TAZ PROTEIN TAFAZZIN; 1. DR Pfam; PF01553; Acyltransferase; 1. DR PRINTS; PR00979; TAFAZZIN. DR SMART; SM00563; PlsC; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. DR Genevisible; Q16635; HS. 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 //