PCAT_DROME
ID PCAT_DROME Reviewed; 533 AA.
AC Q0KHU5; Q86NX4; Q95SE4; Q9W331;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lysophosphatidylcholine acyltransferase {ECO:0000312|FlyBase:FBgn0052699};
DE AltName: Full=1-acylglycerophosphocholine O-acyltransferase;
DE EC=2.3.1.23 {ECO:0000250|UniProtKB:Q3TFD2};
DE AltName: Full=Acyltransferase-like 2;
GN Name=LPCAT {ECO:0000312|FlyBase:FBgn0052699};
GN ORFNames=CG32699 {ECO:0000312|FlyBase:FBgn0052699};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:ABI30972.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABI30972.1};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:ABI30972.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAO39597.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND RNA EDITING OF POSITION 175.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39597.1}; TISSUE=Head;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAL28380.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-450.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28380.1};
RC TISSUE=Ovary {ECO:0000269|PubMed:12537569};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000305}
RP RNA EDITING OF POSITION 175.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25491198; DOI=10.1186/s12860-014-0043-3;
RA Moessinger C., Klizaite K., Steinhagen A., Philippou-Massier J.,
RA Shevchenko A., Hoch M., Ejsing C.S., Thiele C.;
RT "Two different pathways of phosphatidylcholine synthesis, the Kennedy
RT Pathway and the Lands Cycle, differentially regulate cellular
RT triacylglycerol storage.";
RL BMC Cell Biol. 15:43-43(2014).
CC -!- FUNCTION: Acetyltransferase which mediates the conversion of 1-acyl-sn-
CC glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC) (By
CC similarity). Has a calcium-independent activity (By similarity).
CC Displays a clear preference for saturated fatty acyl-CoAs, and 1-
CC myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively
CC (By similarity). Involved in the regulation of lipid droplet number and
CC size (PubMed:25491198). {ECO:0000250|UniProtKB:Q3TFD2,
CC ECO:0000269|PubMed:25491198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-
CC diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168,
CC ChEBI:CHEBI:58342; EC=2.3.1.23;
CC Evidence={ECO:0000250|UniProtKB:Q3TFD2};
CC -!- PATHWAY: Lipid metabolism; phospholipid metabolism.
CC {ECO:0000250|UniProtKB:Q8NF37}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q8NF37}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q8NF37}. Lipid droplet
CC {ECO:0000269|PubMed:25491198}.
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-phosphocholine. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- RNA EDITING: Modified_positions=175 {ECO:0000269|PubMed:17018572,
CC ECO:0000269|Ref.3}; Note=Partially edited. Target of Adar.
CC {ECO:0000269|PubMed:17018572};
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in larvae increases lipid
CC droplet size and reduces lipid droplet number in fat bodies.
CC {ECO:0000269|PubMed:25491198}.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000250|UniProtKB:Q3TFD2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28380.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR EMBL; AE014298; ABI30972.1; -; Genomic_DNA.
DR EMBL; BT003594; AAO39597.1; -; mRNA.
DR EMBL; AY060832; AAL28380.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001036265.1; NM_001042800.3.
DR AlphaFoldDB; Q0KHU5; -.
DR SMR; Q0KHU5; -.
DR STRING; 7227.FBpp0110147; -.
DR PaxDb; Q0KHU5; -.
DR PRIDE; Q0KHU5; -.
DR EnsemblMetazoa; FBtr0110850; FBpp0110147; FBgn0052699.
DR GeneID; 31899; -.
DR KEGG; dme:Dmel_CG32699; -.
DR CTD; 31899; -.
DR FlyBase; FBgn0052699; LPCAT.
DR VEuPathDB; VectorBase:FBgn0052699; -.
DR eggNOG; KOG4666; Eukaryota.
DR GeneTree; ENSGT01030000234574; -.
DR HOGENOM; CLU_025017_0_1_1; -.
DR InParanoid; Q0KHU5; -.
DR OMA; VQQTRMG; -.
DR OrthoDB; 1266853at2759; -.
DR PhylomeDB; Q0KHU5; -.
DR Reactome; R-DME-1482788; Acyl chain remodelling of PC.
DR Reactome; R-DME-1482801; Acyl chain remodelling of PS.
DR Reactome; R-DME-1482839; Acyl chain remodelling of PE.
DR Reactome; R-DME-1482925; Acyl chain remodelling of PG.
DR Reactome; R-DME-1483166; Synthesis of PA.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR UniPathway; UPA00085; -.
DR BioGRID-ORCS; 31899; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31899; -.
DR PRO; PR:Q0KHU5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0052699; Expressed in oocyte and 23 other tissues.
DR Genevisible; Q0KHU5; DM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:FlyBase.
DR GO; GO:0047184; F:1-acylglycerophosphocholine O-acyltransferase activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0071617; F:lysophospholipid acyltransferase activity; IMP:FlyBase.
DR GO; GO:0030258; P:lipid modification; IMP:FlyBase.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:UniProtKB.
DR CDD; cd07991; LPLAT_LPCAT1-like; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR045252; LPCAT1-like.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00563; PlsC; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 2: Evidence at transcript level;
KW Acyltransferase; Calcium; Endoplasmic reticulum; Golgi apparatus;
KW Lipid biosynthesis; Lipid droplet; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; RNA editing; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..533
FT /note="Lysophosphatidylcholine acyltransferase"
FT /id="PRO_0000291477"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..533
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 402..437
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 439..474
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 475..510
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 158..163
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q3TFD2"
FT VARIANT 175
FT /note="I -> M (in RNA edited version)"
FT /evidence="ECO:0000269|PubMed:17018572"
SQ SEQUENCE 533 AA; 60038 MW; 16B9BE7C366BE255 CRC64;
MTTSTIKPTG GDEVPPAGVV GNVADVGVAA SLTKRDSEED TWASKGYNYI NPFVHRIEID
SHIEVAKIYV LTVLLLPIRV VGCVLSLISA WMFACIGLYG MTLDDLKAKP LTGWRKQMQY
MTACGMRMVY TFGSFHYVTM KGRAATAKEA PILVVAPHSS YVDSILVVAS GPPSIVAKRE
TADIPLLGKI INYAQPIYVQ REDPNSRQNT IRDIVDRARS TDDWPQVVIF AEGTCTNRTA
LIKFKPGAFY PGVPVQPVLL KYPNKYDTFT WTWDGPGVLR LLWLTMTQFY NRCEIEYLPV
YTPSEDEVAD ANLYANNVRE VMAKALGVPT SDYSFEDVIV MSRARDMKIP FPGDIVEIER
TIEKLGLNES QRDAELCKGF LRLSNTDRLD IITFGELLQV DLKNTDLHKL FALLDHRRSG
TVSLKSFLLC SLFCKLKNSD LLTFLRALIH LYSESSQQID RESFVRLMRH AGGKLNEQKA
QALFYALDTD NLGYVSFDSF VELTEKQKSS YKFLYHKSEH IRRPKAVVTT AEN
