TAZ_YEAST
ID TAZ_YEAST Reviewed; 381 AA.
AC Q06510; D6W4D8; Q6B2J1;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Tafazzin {ECO:0000303|PubMed:15588229, ECO:0000303|PubMed:28202545, ECO:0000303|PubMed:29091407};
DE Short=Taz {ECO:0000303|PubMed:16135531};
DE EC=2.3.1.- {ECO:0000269|PubMed:15588229, ECO:0000269|PubMed:28202545, ECO:0000269|PubMed:29091407};
GN Name=TAZ1; OrderedLocusNames=YPR140W {ECO:0000303|PubMed:15588229};
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP FUNCTION IN CARDIOLIPIN METABOLISM.
RX PubMed=14651618; DOI=10.1046/j.1365-2958.2003.03802.x;
RA Gu Z., Valianpour F., Chen S., Vaz F.M., Hakkaart G.A., Wanders R.J.,
RA Greenberg M.L.;
RT "Aberrant cardiolipin metabolism in the yeast taz1 mutant: a model for
RT Barth syndrome.";
RL Mol. Microbiol. 51:149-158(2004).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=15588229; DOI=10.1042/bj20041491;
RA Testet E., Laroche-Traineau J., Noubhani A., Coulon D., Bunoust O.,
RA Camougrand N., Manon S., Lessire R., Bessoule J.J.;
RT "Ypr140wp, 'the yeast tafazzin', displays a mitochondrial
RT lysophosphatidylcholine (lyso-PC) acyltransferase activity related to
RT triacylglycerol and mitochondrial lipid synthesis.";
RL Biochem. J. 387:617-626(2005).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16135531; DOI=10.1091/mbc.e05-03-0256;
RA Brandner K., Mick D.U., Frazier A.E., Taylor R.D., Meisinger C.,
RA Rehling P.;
RT "Taz1, an outer mitochondrial membrane protein, affects stability and
RT assembly of inner membrane protein complexes: implications for Barth
RT Syndrome.";
RL Mol. Biol. Cell 16:5202-5214(2005).
RN [10]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF VAL-223; VAL-224;
RP ILE-226 AND GLY-230.
RX PubMed=16880272; DOI=10.1083/jcb.200605043;
RA Claypool S.M., McCaffery J.M., Koehler C.M.;
RT "Mitochondrial mislocalization and altered assembly of a cluster of Barth
RT syndrome mutant tafazzins.";
RL J. Cell Biol. 174:379-390(2006).
RN [11]
RP SUBCELLULAR LOCATION, REGION, AND MUTAGENESIS OF 215-LEU--GLU-232 AND
RP VAL-224.
RX PubMed=24078306; DOI=10.1128/ec.00237-13;
RA Herndon J.D., Claypool S.M., Koehler C.M.;
RT "The Taz1p transacylase is imported and sorted into the outer mitochondrial
RT membrane via a membrane anchor domain.";
RL Eukaryot. Cell 12:1600-1608(2013).
RN [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28202545; DOI=10.1074/jbc.m116.769182;
RA Schlame M., Xu Y., Ren M.;
RT "The Basis for Acyl Specificity in the Tafazzin Reaction.";
RL J. Biol. Chem. 292:5499-5506(2017).
RN [13]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29091407; DOI=10.1021/acs.biochem.7b00941;
RA Abe M., Sawada Y., Uno S., Chigasaki S., Oku M., Sakai Y., Miyoshi H.;
RT "Role of Acyl Chain Composition of Phosphatidylcholine in Tafazzin-Mediated
RT Remodeling of Cardiolipin in Liposomes.";
RL Biochemistry 56:6268-6280(2017).
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:14651618, PubMed:28202545, PubMed:29091407). Its role
CC in cellular physiology is to improve mitochondrial performance (By
CC similarity). CL is critical for the coassembly of lipids and proteins
CC in mitochondrial membranes, for instance, remodeling of the acyl groups
CC of CL in the mitochondrial inner membrane affects the assembly and
CC stability of respiratory chain complex IV and its supercomplex forms
CC (PubMed:16135531). Catalyzes the transacylacion between phospholipids
CC and lysophospholipids, with the highest rate being between
CC phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and
CC CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine
CC (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation,
CC that means, it exchanges acyl groups between CL and PC by a combination
CC of forward and reverse transacylations. Also catalyzes transacylations
CC between other phospholipids such as phosphatidylethanolamine (1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and
CC PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate
CC or PA), although at lower rate. Not regiospecific, it transfers acyl
CC groups into any of the sn-1 and sn-2 positions of the
CC monolysocardiolipin (MLCL), which is an important prerequisite for
CC uniformity and symmetry in CL acyl distribution. Cannot transacylate
CC dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of
CC an acyl acceptor (By similarity). CoA-independent, it can reshuffle
CC molecular species within a single phospholipid class (PubMed:15588229).
CC Redistributes fatty acids between MLCL, CL, and other lipids, which
CC prolongs the half-life of CL. Its action is completely reversible,
CC which allows for cyclic changes, such as fission and fusion or bending
CC and flattening of the membrane. Hence, by contributing to the
CC flexibility of the lipid composition, it plays an important role in the
CC dynamics of mitochondria membranes. Essential for the final stage of
CC spermatogenesis, spermatid individualization (By similarity). Required
CC for the initiation of mitophagy (By similarity).
CC {ECO:0000250|UniProtKB:Q16635, ECO:0000250|UniProtKB:Q9V6G5,
CC ECO:0000269|PubMed:14651618, ECO:0000269|PubMed:15588229,
CC ECO:0000269|PubMed:16135531, ECO:0000269|PubMed:28202545,
CC ECO:0000269|PubMed:29091407}.
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:0000269|PubMed:28202545, ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000269|PubMed:28202545, ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000305|PubMed:28202545, ECO:0000305|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1,2-di-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphocholine = 1',3'-bis-
CC [1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC (9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67456, ChEBI:CHEBI:28733, ChEBI:CHEBI:42027,
CC ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000269|PubMed:28202545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67457;
CC Evidence={ECO:0000269|PubMed:28202545};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67458;
CC Evidence={ECO:0000305|PubMed:28202545};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phospho]-glycerol + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1'-[1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + 1,2-dihexadecanoyl-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:67756, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:72999, ChEBI:CHEBI:77259, ChEBI:CHEBI:173221;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67757;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67758;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-2-(9Z-hexadecenoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC (9Z-hexadecenoyl)-sn-glycero-3-phosphocholine = 1'-[1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + 1,2-di-(9Z-hexadecenoyl)-sn-glycero-3-
CC phosphocholine; Xref=Rhea:RHEA:67760, ChEBI:CHEBI:73851,
CC ChEBI:CHEBI:77259, ChEBI:CHEBI:83717, ChEBI:CHEBI:173222;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67761;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67762;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1'-[1,2-
CC di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho]-glycerol + 1,2-di-(9Z-octadecenoyl)-sn-glycero-
CC 3-phosphocholine; Xref=Rhea:RHEA:67764, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:74669, ChEBI:CHEBI:77253, ChEBI:CHEBI:77259;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67765;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67766;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-
CC glycerol + 1-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine =
CC 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + 1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:67768,
CC ChEBI:CHEBI:28733, ChEBI:CHEBI:42027, ChEBI:CHEBI:77259,
CC ChEBI:CHEBI:173223; Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67769;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67770;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-2-(9Z-hexadecenoyl)-sn-glycero-3-phospho]-glycerol + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1'-[1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:67780, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:74000, ChEBI:CHEBI:77259, ChEBI:CHEBI:173222;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67781;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67782;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-2-hexadecanoyl-sn-glycero-3-phospho]-glycerol + 1-(9Z-
CC hexadecenoyl)-sn-glycero-3-phosphocholine = 1'-[1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-
CC glycero-3-phospho]-glycerol + 1-(9Z-hexadecenoyl)-2-hexadecanoyl-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:67820, ChEBI:CHEBI:73851,
CC ChEBI:CHEBI:77259, ChEBI:CHEBI:89731, ChEBI:CHEBI:173221;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67821;
CC Evidence={ECO:0000305|PubMed:29091407};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67822;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-
CC 3-phospho]-glycerol = 1',3'-bis-[1-acyl-sn-glycero-3-phospho]-
CC glycerol + a cardiolipin; Xref=Rhea:RHEA:67788, ChEBI:CHEBI:62237,
CC ChEBI:CHEBI:64743, ChEBI:CHEBI:75137;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67789;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-
CC (9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol = 1',3'-bis-[1-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + 1',3'-bis[1,2-di-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol; Xref=Rhea:RHEA:67784,
CC ChEBI:CHEBI:77253, ChEBI:CHEBI:77256, ChEBI:CHEBI:77259;
CC Evidence={ECO:0000269|PubMed:29091407};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67785;
CC Evidence={ECO:0000269|PubMed:29091407};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-hexadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-hexadecenoyl)-sn-
CC glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-hexadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:43808, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73851, ChEBI:CHEBI:74000, ChEBI:CHEBI:83717;
CC Evidence={ECO:0000250|UniProtKB:Q9V6G5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43809;
CC Evidence={ECO:0000250|UniProtKB:Q9V6G5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43810;
CC Evidence={ECO:0000250|UniProtKB:Q9V6G5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-
CC [1-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-glycerol + 1,2-di-
CC (9Z-octadecenoyl)-sn-glycero-3-phosphocholine = 1'-[1,2-di-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-2-(9Z-octadecenoyl)-sn-glycero-3-phospho]-glycerol +
CC 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:67836, ChEBI:CHEBI:28610, ChEBI:CHEBI:74669,
CC ChEBI:CHEBI:83580, ChEBI:CHEBI:83582;
CC Evidence={ECO:0000269|PubMed:28202545};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67837;
CC Evidence={ECO:0000269|PubMed:28202545};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67838;
CC Evidence={ECO:0000305|PubMed:28202545};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7 uM for lysophosphatidylcholine {ECO:0000269|PubMed:15588229};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000305|PubMed:15588229,
CC ECO:0000305|PubMed:28202545, ECO:0000305|PubMed:29091407}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:15588229, ECO:0000269|PubMed:16135531,
CC ECO:0000269|PubMed:16880272, ECO:0000269|PubMed:24078306}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16880272}; Intermembrane side
CC {ECO:0000269|PubMed:16135531, ECO:0000269|PubMed:16880272}.
CC Mitochondrion inner membrane {ECO:0000269|PubMed:16880272,
CC ECO:0000269|PubMed:24078306}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16880272}; Intermembrane side
CC {ECO:0000269|PubMed:16880272}. Note=Imported into mitochondria by the
CC TOM complex and is first imported into the mitochondrion outer membrane
CC in a TIM9-TIM10-dependent manner followed by insertion into the
CC mitochondrion inner membrane. {ECO:0000269|PubMed:24078306}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- MISCELLANEOUS: Present with 1340 molecules/cell in log phase SD medium
CC (PubMed:14562106). 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 (By
CC similarity). {ECO:0000250|UniProtKB:Q16635,
CC ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the taffazin family. {ECO:0000305}.
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; U40829; AAB68280.1; -; Genomic_DNA.
DR EMBL; AY692739; AAT92758.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11554.1; -; Genomic_DNA.
DR PIR; S69029; S69029.
DR RefSeq; NP_015466.1; NM_001184237.1.
DR AlphaFoldDB; Q06510; -.
DR BioGRID; 36309; 91.
DR MINT; Q06510; -.
DR STRING; 4932.YPR140W; -.
DR SwissLipids; SLP:000000064; -.
DR MaxQB; Q06510; -.
DR PaxDb; Q06510; -.
DR PRIDE; Q06510; -.
DR EnsemblFungi; YPR140W_mRNA; YPR140W; YPR140W.
DR GeneID; 856262; -.
DR KEGG; sce:YPR140W; -.
DR SGD; S000006344; TAZ1.
DR VEuPathDB; FungiDB:YPR140W; -.
DR eggNOG; KOG2847; Eukaryota.
DR GeneTree; ENSGT00390000018621; -.
DR HOGENOM; CLU_046747_1_1_1; -.
DR InParanoid; Q06510; -.
DR OMA; SVMDDPI; -.
DR BioCyc; MetaCyc:G3O-34275-MON; -.
DR BioCyc; YEAST:G3O-34275-MON; -.
DR Reactome; R-SCE-1268020; Mitochondrial protein import.
DR Reactome; R-SCE-1482798; Acyl chain remodeling of CL.
DR PRO; PR:Q06510; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06510; protein.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:SGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005758; C:mitochondrial intermembrane space; TAS:Reactome.
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:SGD.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IDA:SGD.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IDA:SGD.
DR GO; GO:0032048; P:cardiolipin metabolic process; IMP:SGD.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IMP:SGD.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IMP:SGD.
DR GO; GO:0097250; P:mitochondrial respirasome assembly; IMP:SGD.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IMP:SGD.
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; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..381
FT /note="Tafazzin"
FT /id="PRO_0000220934"
FT TOPO_DOM 1..25
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:16880272"
FT INTRAMEM 26..47
FT /evidence="ECO:0000305|PubMed:16880272"
FT TOPO_DOM 48..381
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305|PubMed:16880272"
FT REGION 215..232
FT /note="Required for membrane insertion"
FT /evidence="ECO:0000269|PubMed:24078306"
FT MOTIF 77..82
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT MUTAGEN 215..232
FT /note="Missing: Abolishes insertion into mitochondrial
FT membranes."
FT /evidence="ECO:0000269|PubMed:24078306"
FT MUTAGEN 223
FT /note="V->D: Greatly reduced expression. Mislocalization to
FT mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:16880272"
FT MUTAGEN 224
FT /note="V->R: Greatly reduced expression. Mislocalization to
FT mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:16880272,
FT ECO:0000269|PubMed:24078306"
FT MUTAGEN 226
FT /note="I->P: Greatly reduced expression. Mislocalization to
FT mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:16880272"
FT MUTAGEN 230
FT /note="G->R: Slightly reduced expression. Does not affect
FT mitochondrial membrane localization but shows weaker
FT membrane association."
FT /evidence="ECO:0000269|PubMed:16880272"
FT CONFLICT 11
FT /note="D -> Y (in Ref. 3; AAT92758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 381 AA; 44188 MW; 76964FA6C77989B2 CRC64;
MSFRDVLERG DEFLEAYPRR SPLWRFLSYS TSLLTFGVSK LLLFTCYNVK LNGFEKLETA
LERSKRENRG LMTVMNHMSM VDDPLVWATL PYKLFTSLDN IRWSLGAHNI CFQNKFLANF
FSLGQVLSTE RFGVGPFQGS IDASIRLLSP DDTLDLEWTP HSEVSSSLKK AYSPPIIRSK
PSWVHVYPEG FVLQLYPPFE NSMRYFKWGI TRMILEATKP PIVVPIFATG FEKIASEAVT
DSMFRQILPR NFGSEINVTI GDPLNDDLID RYRKEWTHLV EKYYDPKNPN DLSDELKYGK
EAQDLRSRLA AELRAHVAEI RNEVRKLPRE DPRFKSPSWW KRFNTTEGKS DPDVKVIGEN
WAIRRMQKFL PPEGKPKGKD D
