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TAZ_ERYPA
ID   TAZ_ERYPA               Reviewed;         262 AA.
AC   Q6IV76;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Tafazzin;
DE            Short=Taz;
DE            EC=2.3.1.- {ECO:0000250|UniProtKB:Q16635};
GN   Name=TAZ;
OS   Erythrocebus patas (Red guenon) (Cercopithecus patas).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Erythrocebus.
OX   NCBI_TaxID=9538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
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).
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   -!- 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; AY621060; AAT45912.1; -; mRNA.
DR   EMBL; AY621055; AAT45909.1; -; Genomic_DNA.
DR   EMBL; AY621053; AAT45909.1; JOINED; Genomic_DNA.
DR   EMBL; AY621054; AAT45909.1; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q6IV76; -.
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   2: Evidence at transcript level;
KW   Acyltransferase; Lipid metabolism; Membrane; Mitochondrion;
KW   Mitochondrion inner membrane; Mitochondrion outer membrane; Transferase.
FT   CHAIN           1..262
FT                   /note="Tafazzin"
FT                   /id="PRO_0000220926"
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"
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
 
 
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