TAZ_GORGO
ID TAZ_GORGO Reviewed; 262 AA.
AC Q6IV83; A0A2I2Y2I5;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=Tafazzin;
DE Short=Taz;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q16635};
GN Name=TAFAZZIN; Synonyms=TAZ;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15793838; DOI=10.1002/ajmg.a.30661;
RA Gonzalez I.L.;
RT "Barth syndrome: TAZ gene mutations, mRNAs, and evolution.";
RL Am. J. Med. Genet. A 134:409-414(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
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:Q06510}.
CC -!- SUBUNIT: Associates with multiple protein complexes.
CC {ECO:0000250|UniProtKB:Q16635}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}. Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q16635}; Intermembrane side
CC {ECO:0000250|UniProtKB:Q16635}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q6IV83-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q6IV83-1; Sequence=VSP_061372;
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity.
CC {ECO:0000250|UniProtKB:Q3TFD2}.
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. {ECO:0000305}.
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DR EMBL; AY621043; AAT45905.1; -; Genomic_DNA.
DR EMBL; AY621041; AAT45905.1; JOINED; Genomic_DNA.
DR EMBL; AY621042; AAT45905.1; JOINED; Genomic_DNA.
DR EMBL; CABD030129302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004065193.2; XM_004065145.2.
DR AlphaFoldDB; Q6IV83; -.
DR STRING; 9593.ENSGGOP00000011653; -.
DR Ensembl; ENSGGOT00000065388; ENSGGOP00000029115; ENSGGOG00000011947. [Q6IV83-2]
DR GeneID; 101147380; -.
DR KEGG; ggo:101147380; -.
DR CTD; 6901; -.
DR GeneTree; ENSGT00390000018621; -.
DR InParanoid; Q6IV83; -.
DR Proteomes; UP000001519; Chromosome X.
DR Bgee; ENSGGOG00000011947; Expressed in heart and 6 other tissues.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032048; P:cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:0003007; P:heart morphogenesis; ISS:UniProtKB.
DR GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR GO; GO:0000423; P:mitophagy; ISS:UniProtKB.
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 3: Inferred from homology;
KW Acyltransferase; Alternative splicing; Lipid metabolism; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..262
FT /note="Tafazzin"
FT /id="PRO_0000220927"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT INTRAMEM 15..35
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..262
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 82..92
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT REGION 155..190
FT /note="Mitochondrial targeting sequence"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT MOTIF 69..74
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT VAR_SEQ 123
FT /note="R -> RGAEFFQAENEGKGVLDTGRHMPGAGKRREK (in isoform 1)"
FT /id="VSP_061372"
SQ SEQUENCE 262 AA; 30180 MW; C1B4E4AB9CA66AAB CRC64;
MPLHVKWPFP AVPPLTWTLA SSVVMGLVGT YSCFWTKYMN HLTVHNKEVL YELIENRGPA
TPLITVSNHQ SCMDDPHLWG ILKLRHIWNL KLMRWTPAAA DICFTKELHS HFFSLGKCVP
VCRGDGVYQK GMDFILEKLN HGDWVHIFPE GKVNMSSEFL RFKWGIGRLI AECHLNPIIL
PLWHVGMNDV LPNSPPYFPR FGQKITVLIG KPFSALPVLE RLRAENKSAV EMRKALTDFI
QEEFQRLKTQ AEQLHNHLQP GR
