ID M3X025_FELCA Unreviewed; 262 AA.
AC M3X025;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Tafazzin family protein {ECO:0000256|RuleBase:RU365062};
GN Name=TAFAZZIN {ECO:0000313|Ensembl:ENSFCAP00000019966.2,
GN ECO:0000313|VGNC:VGNC:65967};
GN Synonyms=TAZ {ECO:0000256|RuleBase:RU365062};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000019966.2, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000019966.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019966.2,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000019966.2, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019966.2,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000019966.2}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000019966.2};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Acyltransferase which is required to remodel newly
CC synthesized phospholipid cardiolipin, a key component of the
CC mitochondrial inner membrane. Required for the initiation of mitophagy.
CC Required to ensure progression of spermatocytes through meiosis.
CC {ECO:0000256|RuleBase:RU365062}.
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:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33732;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:33733;
CC Evidence={ECO:0000256|ARBA:ARBA00024570};
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:0000256|ARBA:ARBA00024577};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43817;
CC Evidence={ECO:0000256|ARBA:ARBA00024577};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:43818;
CC Evidence={ECO:0000256|ARBA:ARBA00024577};
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:0000256|ARBA:ARBA00024592};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67749;
CC Evidence={ECO:0000256|ARBA:ARBA00024592};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67750;
CC Evidence={ECO:0000256|ARBA:ARBA00024592};
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:0000256|ARBA:ARBA00024553};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67753;
CC Evidence={ECO:0000256|ARBA:ARBA00024553};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:67754;
CC Evidence={ECO:0000256|ARBA:ARBA00024553};
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:0000256|ARBA:ARBA00029361};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68989;
CC Evidence={ECO:0000256|ARBA:ARBA00029361};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:68990;
CC Evidence={ECO:0000256|ARBA:ARBA00029361};
CC -!- SUBUNIT: Associates with multiple protein complexes.
CC {ECO:0000256|ARBA:ARBA00024371}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004137}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004137}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00004137}. Mitochondrion outer membrane
CC {ECO:0000256|ARBA:ARBA00024323}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00024323}; Intermembrane side
CC {ECO:0000256|ARBA:ARBA00024323}.
CC -!- SIMILARITY: Belongs to the taffazin family.
CC {ECO:0000256|ARBA:ARBA00010524, ECO:0000256|RuleBase:RU365062}.
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DR EMBL; AANG04001886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004001069.1; XM_004001020.3.
DR AlphaFoldDB; M3X025; -.
DR STRING; 9685.ENSFCAP00000019966; -.
DR PaxDb; 9685-ENSFCAP00000019966; -.
DR Ensembl; ENSFCAT00000027011.4; ENSFCAP00000019966.2; ENSFCAG00000023652.4.
DR GeneID; 101084092; -.
DR KEGG; fca:101084092; -.
DR CTD; 6901; -.
DR VGNC; VGNC:65967; TAFAZZIN.
DR eggNOG; KOG2847; Eukaryota.
DR GeneTree; ENSGT00390000018621; -.
DR HOGENOM; CLU_046747_3_0_1; -.
DR InParanoid; M3X025; -.
DR OMA; GWPSIMP; -.
DR OrthoDB; 1387at2759; -.
DR Proteomes; UP000011712; Chromosome X.
DR Bgee; ENSFCAG00000023652; Expressed in adult mammalian kidney and 10 other cell types or tissues.
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:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; IBA:GO_Central.
DR GO; GO:0060048; P:cardiac muscle contraction; IEA:Ensembl.
DR GO; GO:0048738; P:cardiac muscle tissue development; IEA:Ensembl.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IBA:GO_Central.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR GO; GO:0042407; P:cristae formation; IEA:Ensembl.
DR GO; GO:0030097; P:hemopoiesis; IEA:Ensembl.
DR GO; GO:0007007; P:inner mitochondrial membrane organization; IBA:GO_Central.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:Ensembl.
DR GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl.
DR CDD; cd07989; LPLAT_AGPAT-like; 1.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR000872; Tafazzin.
DR PANTHER; PTHR12497:SF0; TAFAZZIN; 1.
DR PANTHER; PTHR12497; TAZ PROTEIN TAFAZZIN; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR PRINTS; PR00979; TAFAZZIN.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|RuleBase:RU365062};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
KW Transmembrane {ECO:0000256|RuleBase:RU365062};
KW Transmembrane helix {ECO:0000256|RuleBase:RU365062}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU365062"
FT DOMAIN 63..187
FT /note="Phospholipid/glycerol acyltransferase"
FT /evidence="ECO:0000259|SMART:SM00563"
SQ SEQUENCE 262 AA; 30293 MW; FD10496D60261060 CRC64;
MPLRVKWPFP AVPPFTWTLA SSVVMGLVGT YSCFWTKYMN HLTVHNKEVL YELIENRGPA
TPLITVSNHQ SCMDDPHLWG ILKLRHIWNL KLMRWTPAAA DICFTRELHS RFFSLGKCVP
VCRGDGVYQK GMDFILEKLN HGDWVHIFPE GKVNMSSEFL RFKWGIGRLI AECHLNPVIL
PLWHVGMNDV LPNSPPYFPR FGQKITVLIG KPFSAVPVLE RLRAENKSAV EMRKALTDFI
QEEFQRLKVQ AEQLHGHLQP RR
//
