TAZ_DANRE
ID TAZ_DANRE Reviewed; 262 AA.
AC F1QCP6; Q6PUS0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Tafazzin {ECO:0000312|ZFIN:ZDB-GENE-030131-684};
DE Short=Taz;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q16635};
GN Name=tafazzin {ECO:0000312|ZFIN:ZDB-GENE-030131-684}; Synonyms=taz;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955 {ECO:0000312|Proteomes:UP000000437};
RN [1] {ECO:0000312|EMBL:AAS92633.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang G.W., Sun X.J., Wu X.Y., Song H.D., Liu T.X., Zhou Y., Sheng Y.,
RA Chen Y., Ruan Z., Jiang C.L., Fan H.Y., Zon L.I., Kanki J.P., Look A.T.,
RA Chen Z.;
RT "Gene Expression Profiling in the Zebrafish Kidney Marrow Tissue.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|Proteomes:UP000000437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen {ECO:0000312|Proteomes:UP000000437};
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=16794186; DOI=10.1161/01.res.0000233378.95325.ce;
RA Khuchua Z., Yue Z., Batts L., Strauss A.W.;
RT "A zebrafish model of human Barth syndrome reveals the essential role of
RT tafazzin in cardiac development and function.";
RL Circ. Res. 99:201-208(2006).
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 (By similarity). Its role in cellular physiology is to improve
CC mitochondrial performance (By similarity). CL is critical for the
CC coassembly of lipids and proteins in mitochondrial membranes, for
CC 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 (By similarity). Required to ensure progression of
CC spermatocytes through meiosis (By similarity).
CC {ECO:0000250|UniProtKB:Q06510, ECO:0000250|UniProtKB:Q16635,
CC ECO:0000250|UniProtKB:Q91WF0, ECO:0000250|UniProtKB:Q9V6G5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1-acyl-
CC sn-glycero-3-phosphate = 1-acyl-sn-glycero-3-phospho-(1'-sn-glycerol)
CC + a 1,2-diacyl-sn-glycero-3-phosphate; Xref=Rhea:RHEA:67748,
CC ChEBI:CHEBI:57970, ChEBI:CHEBI:58608, ChEBI:CHEBI:64716,
CC ChEBI:CHEBI:64840; Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + 1-hexadecanoyl-2-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) = 1-
CC (9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphate +
CC 1-hexadecanoyl-sn-glycero-3-phospho-(1'-sn-glycerol);
CC Xref=Rhea:RHEA:67752, ChEBI:CHEBI:72840, ChEBI:CHEBI:74544,
CC ChEBI:CHEBI:74563, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-
CC phospho]-glycerol + a 1,2-diacyl-sn-glycero-3-phosphocholine = a 1-
CC acyl-sn-glycero-3-phosphocholine + a cardiolipin;
CC Xref=Rhea:RHEA:33731, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64743;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + 1-hexadecanoyl-sn-glycero-3-phosphocholine = 1,2-
CC dihexadecanoyl-sn-glycero-3-phosphocholine + 2-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phosphocholine; Xref=Rhea:RHEA:68988,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:72999, ChEBI:CHEBI:73002,
CC ChEBI:CHEBI:76084; Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine = 1-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine + 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-
CC glycero-3-phosphocholine; Xref=Rhea:RHEA:43816, ChEBI:CHEBI:28610,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73001, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000250|UniProtKB:Q16635};
CC -!- PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q16635}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}.
CC -!- TISSUE SPECIFICITY: At 10 hours post-fertilization (hpf), expressed
CC ubiquitously, including in cardiac progenitor regions, with strongest
CC expression in the head area. By 24 hpf, highly expressed in the head,
CC eyes, and tail. By 30 hpf, expression is restricted to the head, heart,
CC eyes, and the region next to the yolk corresponding to endodermal
CC tissue. At 51 hpf, expression is restricted to the heart.
CC {ECO:0000269|PubMed:16794186}.
CC -!- DEVELOPMENTAL STAGE: Before gastrulation, expression is barely
CC detectable. At 7 hours post-fertilization (hpf), sharply up-regulated.
CC High-level expression continues throughout the segmentation (12 hpf)
CC and pharyngula (24 to 30 hpf) stages. At hatching at 51 hpf, expression
CC declines dramatically. {ECO:0000269|PubMed:16794186}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown results in dose-dependent
CC lethality, severe developmental and growth retardation, marked
CC bradycardia and pericardial effusions, and generalized edema.
CC {ECO:0000269|PubMed:16794186}.
CC -!- MISCELLANEOUS: The enzyme was named after a masochistic character
CC Tafazzi, once popular on Italian television, apparently due to the
CC difficulty encountered for its identification and characterization.
CC {ECO:0000250|UniProtKB:Q16635}.
CC -!- SIMILARITY: Belongs to the taffazin family.
CC {ECO:0000255|RuleBase:RU365062}.
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DR EMBL; AY576995; AAS92633.1; -; mRNA.
DR EMBL; CR354596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001001814.1; NM_001001814.1.
DR AlphaFoldDB; F1QCP6; -.
DR STRING; 7955.ENSDARP00000120241; -.
DR PaxDb; F1QCP6; -.
DR Ensembl; ENSDART00000060718; ENSDARP00000060717; ENSDARG00000041421.
DR Ensembl; ENSDART00000140861; ENSDARP00000120241; ENSDARG00000041421.
DR GeneID; 321965; -.
DR KEGG; dre:321965; -.
DR CTD; 6901; -.
DR ZFIN; ZDB-GENE-030131-684; tafazzin.
DR eggNOG; KOG2847; Eukaryota.
DR GeneTree; ENSGT00390000018621; -.
DR InParanoid; F1QCP6; -.
DR OMA; GWPSIMP; -.
DR OrthoDB; 589285at2759; -.
DR PhylomeDB; F1QCP6; -.
DR TreeFam; TF313862; -.
DR Reactome; R-DRE-1268020; Mitochondrial protein import.
DR Reactome; R-DRE-1482798; Acyl chain remodeling of CL.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 23.
DR ExpressionAtlas; F1QCP6; baseline and differential.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031966; C:mitochondrial membrane; IBA:GO_Central.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0008374; F:O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0032048; P:cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:ZFIN.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
DR GO; GO:0045823; P:positive regulation of heart contraction; IMP:ZFIN.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497; PTHR12497; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR SMART; SM00563; PlsC; 1.
PE 2: Evidence at transcript level;
KW Acyltransferase; 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_0000452722"
FT TOPO_DOM 1..18
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT INTRAMEM 19..35
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..262
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 82..92
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 155..190
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT MOTIF 69..74
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT CONFLICT 98
FT /note="T -> A (in Ref. 1; AAS92633)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="L -> I (in Ref. 1; AAS92633)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 262 AA; 30574 MW; 7CB510E5D3292C33 CRC64;
MPLEVTWPFP QCPRLGWRIS SRVVMGMVGS YSYLWTKYFN SLMVHNQDVL LNLVDERPQD
TPLITVCNHQ SCMDDPHIWG VLKFRQLWNL NKMRWTPTAS DICFTREFHS SFFSRGKCVP
VVRGDGVYQK GMDFLLERLN QGEWIHIFPE GRVNMSGEFM RIKWGIGRLI AECSLHPIIL
PMWHIGMNDV LPNETPYIPR VGQRITVLVG KPFTVRHLVN ALRAENTNPT EMRKTVTDYI
QDEFRSLKAQ AEALHHRLQN HT
