TAZ_DICDI
ID TAZ_DICDI Reviewed; 285 AA.
AC Q54DX7;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Taffazin;
DE Short=Taz;
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q16635};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
GN Name=taz; ORFNames=DDB_G0291922;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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 (By similarity). {ECO:0000250|UniProtKB:Q06510,
CC ECO:0000250|UniProtKB:Q16635, 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 -!- 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; AAFI02000186; EAL61491.1; -; Genomic_DNA.
DR RefSeq; XP_629919.1; XM_629917.1.
DR AlphaFoldDB; Q54DX7; -.
DR STRING; 44689.DDB0237792; -.
DR PaxDb; Q54DX7; -.
DR PRIDE; Q54DX7; -.
DR EnsemblProtists; EAL61491; EAL61491; DDB_G0291922.
DR GeneID; 8628420; -.
DR KEGG; ddi:DDB_G0291922; -.
DR dictyBase; DDB_G0291922; taz.
DR eggNOG; KOG2847; Eukaryota.
DR HOGENOM; CLU_046747_3_0_1; -.
DR InParanoid; Q54DX7; -.
DR OMA; ARMIMES; -.
DR PhylomeDB; Q54DX7; -.
DR Reactome; R-DDI-1482798; Acyl chain remodeling of CL.
DR PRO; PR:Q54DX7; -.
DR Proteomes; UP000002195; Chromosome 6.
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:dictyBase.
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:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
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; Lipid metabolism; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Mitochondrion outer membrane;
KW Reference proteome; Transferase.
FT CHAIN 1..285
FT /note="Taffazin"
FT /id="PRO_0000328231"
FT TOPO_DOM 1..23
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT INTRAMEM 24..42
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..285
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000250|UniProtKB:Q16635"
FT MOTIF 74..79
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
SQ SEQUENCE 285 AA; 32784 MW; 8CE1C94790B76524 CRC64;
MDSNNSNNNN KNLKQICDIP KPQFLSKGVF TLVGVLCKFW ISMNTVTTSG IDKLVNEIDK
THQLKRPMIT IANHSSNLDD PLLWGVLPNR ILMDPSKQRW TLGASNILFT NWFYSKFFSL
GKCIKIVRGD GIYQDGMNES IDRLSEGQWL HIFPEGRISQ QTQLLYFKWG LGRLVGECYR
RTGVVPLVVP IYHQGMEKSM PLAKLPIPRV GINLDIKVGD NIYCDQVISK YIDDNKISDL
TDYLSQDDKK RKDFYKTITL HIEDEYQKII PPTNRGRFSH PTIKD
