LPAAT_ORYSJ
ID LPAAT_ORYSJ Reviewed; 414 AA.
AC Q0J0A4; Q650U5;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 3.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Probable 1-acylglycerol-3-phosphate O-acyltransferase;
DE EC=2.3.1.51;
DE AltName: Full=Lipid droplet-binding protein CGI-58 homolog;
GN OrderedLocusNames=Os09g0520200, LOC_Os09g34860; ORFNames=P0669G04.7;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=18089549; DOI=10.1093/nar/gkm978;
RG The rice annotation project (RAP);
RT "The rice annotation project database (RAP-DB): 2008 update.";
RL Nucleic Acids Res. 36:D1028-D1033(2008).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
CC -!- FUNCTION: Lysophosphatidic acid acyltransferase which functions in
CC phosphatidic acid biosynthesis. May regulate neutral lipid accumulation
CC and participate in the regulation of lipid turnover in vegetative
CC cells. May possess additional triacylglycerol lipase and phospholipase
CC A2 activities in vitro (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-diacyl-
CC sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:19709,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57970, ChEBI:CHEBI:58342,
CC ChEBI:CHEBI:58608; EC=2.3.1.51;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity and
CC may constitute the binding site for the phosphate moiety of the
CC glycerol-3-phosphate. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. ABHD4/ABHD5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD46672.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAF25611.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AP006175; BAD46672.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP008215; BAF25611.2; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015651253.1; XM_015795767.1.
DR AlphaFoldDB; Q0J0A4; -.
DR SMR; Q0J0A4; -.
DR STRING; 4530.OS09T0520200-00; -.
DR ESTHER; orysa-Q0J0A4; CGI-58_ABHD5_ABHD4.
DR PaxDb; Q0J0A4; -.
DR PRIDE; Q0J0A4; -.
DR GeneID; 4347605; -.
DR KEGG; osa:4347605; -.
DR eggNOG; KOG4409; Eukaryota.
DR InParanoid; Q0J0A4; -.
DR OrthoDB; 1555935at2759; -.
DR Proteomes; UP000000763; Chromosome 9.
DR Proteomes; UP000059680; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IBA:GO_Central.
DR GO; GO:0042171; F:lysophosphatidic acid acyltransferase activity; IBA:GO_Central.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Cytoplasm; Lipid biosynthesis; Lipid metabolism;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transferase.
FT CHAIN 1..414
FT /note="Probable 1-acylglycerol-3-phosphate O-
FT acyltransferase"
FT /id="PRO_0000430170"
FT DOMAIN 117..382
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT MOTIF 193..197
FT /note="GXSXG"
FT MOTIF 375..380
FT /note="HXXXXD motif"
SQ SEQUENCE 414 AA; 45728 MW; 25DC41C01A97FB2C CRC64;
MRRAAAAAVT VTTTTRMAAE GMSTAAAAAE ATATAAPAAG SRWGRAWPSA LRWIPTSTDR
IIAAEKRLLS IVKTGYVQEQ VNIGSSPPGS KVRWFRSSSD EPRFINTVTF DSEENAPTLV
MVHGYGASQG FFFRNFDALA SRFRVIAIDQ LGWGGSSRPD FTCKSTEETE AWFIDSFEEW
RKAKNLSNFI LLGHSFGGYV AAKYALQHPE HVQHLILVGP AGFSSETEHS SEWLTKFRAT
WKGMLVNHLW ESNFTPQRIV RGLGPWGPGL VQRYTSARFG SHSTGELLTE QESTLLTDYI
YHTLAAKASG ELCLKHIFSF GAFVRKPLLQ SASDWKVPTT FIYGQQDWMN YQGAQQARKE
MKVPCEIIRV PQGGHFVFID NPSGFHSAVF HACRKFLSGD GEEGLSLPEG LTSA