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Database: UniProt
Entry: A0A077RXJ6_WHEAT
LinkDB: A0A077RXJ6_WHEAT
Original site: A0A077RXJ6_WHEAT 
ID   A0A077RXJ6_WHEAT        Unreviewed;       502 AA.
AC   A0A077RXJ6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Phospholipid/glycerol acyltransferase domain-containing protein {ECO:0000259|SMART:SM00563};
GN   ORFNames=TRAES_3BF111600230CFD_c1 {ECO:0000313|EMBL:CDM81858.1};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EMBL:CDM81858.1};
RN   [1] {ECO:0000313|EMBL:CDM81858.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25035497; DOI=10.1126/science.1249721;
RA   Choulet F., Alberti A., Theil S., Glover N., Barbe V., Daron J.,
RA   Pingault L., Sourdille P., Couloux A., Paux E., Leroy P., Mangenot S.,
RA   Guilhot N., Le Gouis J., Balfourier F., Alaux M., Jamilloux V., Poulain J.,
RA   Durand C., Bellec A., Gaspin C., Safar J., Dolezel J., Rogers J.,
RA   Vandepoele K., Aury J.M., Mayer K., Berges H., Quesneville H., Wincker P.,
RA   Feuillet C.;
RT   "Structural and functional partitioning of bread wheat chromosome 3B.";
RL   Science 345:1249721-1249721(2014).
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   -!- 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}.
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DR   EMBL; HG670306; CDM81858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077RXJ6; -.
DR   HOGENOM; CLU_031593_0_0_1; -.
DR   ExpressionAtlas; A0A077RXJ6; baseline and differential.
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:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0006644; P:phospholipid metabolic process; IEA:InterPro.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00022787}.
FT   DOMAIN          156..283
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
FT   REGION          415..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          334..361
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   502 AA;  55572 MW;  87B6DD001FB08DE0 CRC64;
     MANPSMAAGG GVPWAEGARA VGAQIRNRLR VAPVDRRWLW RRPEGRAASE AVRQWSDRLR
     AILQRDKQNQ GPGSPDASAA AAAKPSSSAF KFYRKKVGKE VNGVEDSVIF RSLQALAVPL
     IGNACHVFMH GLNSVQIYGA EKLQQALQER PKDKPLLTVS NHVAAMDDPF VIASLLPPSV
     MLEAQKLRWT LCATDRCFTN PVLSTFFRSV KVLPVNRGEG IYQKGMDMAL SKLNNGGWVH
     IFPEGSRSRD GGKTIAPAKR GVGRLIMDAD SLPVVVPFVH TGMQDIMPVG KRIPRTGKRV
     IVVVGDPINF DDLMAENSND SQHISRGDLY DKVTERIGQR LQQLKVEVDR LAAEQKAELQ
     NRHVANDTVN DGYKVWQQVD WESFGIGNML SSAEHSSAQE PPPKQIQHEV LLAEQSASPA
     KQAEPEPRLE EEQSVFSPIS RVPHWFSRRT DASELMGFAA RGLVGNGRSM QEGYRQFQEP
     SVFSAWWEAQ TSSAMMPRWS TA
//
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