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Database: UniProt
Entry: Q9VYJ4_DROME
LinkDB: Q9VYJ4_DROME
Original site: Q9VYJ4_DROME 
ID   Q9VYJ4_DROME            Unreviewed;       343 AA.
AC   Q9VYJ4;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase {ECO:0000256|RuleBase:RU361267};
DE            EC=2.3.1.51 {ECO:0000256|RuleBase:RU361267};
GN   Name=Agpat1 {ECO:0000313|EMBL:AAF48201.1,
GN   ECO:0000313|FlyBase:FBgn0030421};
GN   Synonyms=AGPAT {ECO:0000313|EMBL:AAF48201.1}, AGPAT1
GN   {ECO:0000313|EMBL:AAF48201.1}, AGPAT2 {ECO:0000313|EMBL:AAF48201.1},
GN   dAGPAT1 {ECO:0000313|EMBL:AAF48201.1}, Dmel\CG3812
GN   {ECO:0000313|EMBL:AAF48201.1};
GN   ORFNames=CG3812 {ECO:0000313|EMBL:AAF48201.1,
GN   ECO:0000313|FlyBase:FBgn0030421}, Dmel_CG3812
GN   {ECO:0000313|EMBL:AAF48201.1};
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 {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803};
RN   [1] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J., 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., Scheeler F., Shen H.,
RA   Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., Spier E.,
RA   Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C.,
RA   Turner R., Venter E., Wang A.H., Wang X., Wang Z.Y., Wassarman D.A.,
RA   Weinstock G.M., Weissenbach J., Williams S.M., WoodageT, Worley K.C.,
RA   Wu D., Yang S., Yao Q.A., Ye J., Yeh R.F., Zaveri J.S., Zhan M., Zhang G.,
RA   Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.,
RA   Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [2] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537568;
RA   Celniker S.E., Wheeler D.A., Kronmiller B., Carlson J.W., Halpern A.,
RA   Patel S., Adams M., Champe M., Dugan S.P., Frise E., Hodgson A.,
RA   George R.A., Hoskins R.A., Laverty T., Muzny D.M., Nelson C.R.,
RA   Pacleb J.M., Park S., Pfeiffer B.D., Richards S., Sodergren E.J.,
RA   Svirskas R., Tabor P.E., Wan K., Stapleton M., Sutton G.G., Venter C.,
RA   Weinstock G., Scherer S.E., Myers E.W., Gibbs R.A., Rubin G.M.;
RT   "Finishing a whole-genome shotgun: release 3 of the Drosophila melanogaster
RT   euchromatic genome sequence.";
RL   Genome Biol. 3:RESEARCH0079-RESEARCH0079(2002).
RN   [3] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
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   [4] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537573;
RA   Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R.,
RA   Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M.,
RA   Celniker S.E.;
RT   "The transposable elements of the Drosophila melanogaster euchromatin: a
RT   genomics perspective.";
RL   Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002).
RN   [5] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=12537574;
RA   Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A.,
RA   Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G.,
RA   Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M.,
RA   Karpen G.H.;
RT   "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly.";
RL   Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002).
RN   [6] {ECO:0000313|EMBL:AAM49957.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Berkeley {ECO:0000313|EMBL:AAM49957.1};
RA   Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J., Champe M.,
RA   Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.,
RA   Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G., Miranda A.,
RA   Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S., Patel S.,
RA   Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M., Celniker S.;
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=16110336; DOI=10.1371/journal.pcbi.0010022;
RA   Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D.,
RA   Ashburner M., Anxolabehere D.;
RT   "Combined evidence annotation of transposable elements in genome
RT   sequences.";
RL   PLoS Comput. Biol. 1:166-175(2005).
RN   [8] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S.,
RA   Svirskas R., Rubin G.;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN   [9] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569856; DOI=10.1126/science.1139815;
RA   Smith C.D., Shu S., Mungall C.J., Karpen G.H.;
RT   "The Release 5.1 annotation of Drosophila melanogaster heterochromatin.";
RL   Science 316:1586-1591(2007).
RN   [10] {ECO:0000313|EMBL:AAF48201.1, ECO:0000313|Proteomes:UP000000803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000313|Proteomes:UP000000803};
RX   PubMed=17569867; DOI=10.1126/science.1139816;
RA   Hoskins R.A., Carlson J.W., Kennedy C., Acevedo D., Evans-Holm M.,
RA   Frise E., Wan K.H., Park S., Mendez-Lago M., Rossi F., Villasante A.,
RA   Dimitri P., Karpen G.H., Celniker S.E.;
RT   "Sequence finishing and mapping of Drosophila melanogaster
RT   heterochromatin.";
RL   Science 316:1625-1628(2007).
RN   [11] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109357; DOI=.1534/g3.115.018929;
RG   FlyBase Consortium;
RA   Matthews B.B., Dos Santos G., Crosby M.A., Emmert D.B., St Pierre S.E.,
RA   Gramates L.S., Zhou P., Schroeder A.J., Falls K., Strelets V., Russo S.M.,
RA   Gelbart W.M., null;
RT   "Gene Model Annotations for Drosophila melanogaster: Impact of High-
RT   Throughput Data.";
RL   G3 (Bethesda) 5:1721-1736(2015).
RN   [12] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=26109356; DOI=.1534/g3.115.018937;
RG   FlyBase Consortium;
RA   Crosby M.A., Gramates L.S., Dos Santos G., Matthews B.B., St Pierre S.E.,
RA   Zhou P., Schroeder A.J., Falls K., Emmert D.B., Russo S.M., Gelbart W.M.,
RA   null;
RT   "Gene Model Annotations for Drosophila melanogaster: The Rule-Benders.";
RL   G3 (Bethesda) 5:1737-1749(2015).
RN   [13] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25589440;
RA   Hoskins R.A., Carlson J.W., Wan K.H., Park S., Mendez I., Galle S.E.,
RA   Booth B.W., Pfeiffer B.D., George R.A., Svirskas R., Krzywinski M.,
RA   Schein J., Accardo M.C., Damia E., Messina G., Mendez-Lago M.,
RA   de Pablos B., Demakova O.V., Andreyeva E.N., Boldyreva L.V., Marra M.,
RA   Carvalho A.B., Dimitri P., Villasante A., Zhimulev I.F., Rubin G.M.,
RA   Karpen G.H., Celniker S.E.;
RT   "The Release 6 reference sequence of the Drosophila melanogaster genome.";
RL   Genome Res. 25:445-458(2015).
RN   [14] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Berkeley Drosophila Genome Project;
RA   Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R.,
RA   Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C.,
RA   Rubin G.;
RT   "Drosophila melanogaster release 4 sequence.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
RN   [15] {ECO:0000313|EMBL:AAF48201.1}
RP   NUCLEOTIDE SEQUENCE.
RG   FlyBase;
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|RuleBase:RU361267};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC       {ECO:0000256|ARBA:ARBA00004728}.
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:0000256|RuleBase:RU361267}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000256|ARBA:ARBA00008655,
CC       ECO:0000256|RuleBase:RU361267}.
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DR   EMBL; AE014298; AAF48201.1; -; Genomic_DNA.
DR   EMBL; AY118588; AAM49957.1; -; mRNA.
DR   EMBL; AE014298; AAN09316.1; -; Genomic_DNA.
DR   EMBL; AE014298; AGB95336.1; -; Genomic_DNA.
DR   RefSeq; NP_001259494.1; NM_001272565.1.
DR   RefSeq; NP_572828.1; NM_132600.2.
DR   RefSeq; NP_727641.1; NM_167337.2.
DR   AlphaFoldDB; Q9VYJ4; -.
DR   SMR; Q9VYJ4; -.
DR   IntAct; Q9VYJ4; 1.
DR   STRING; 7227.FBpp0073522; -.
DR   PaxDb; 7227-FBpp0073522; -.
DR   DNASU; 32230; -.
DR   EnsemblMetazoa; FBtr0073688; FBpp0073521; FBgn0030421.
DR   EnsemblMetazoa; FBtr0073689; FBpp0073522; FBgn0030421.
DR   EnsemblMetazoa; FBtr0333176; FBpp0305378; FBgn0030421.
DR   GeneID; 32230; -.
DR   KEGG; dme:Dmel_CG3812; -.
DR   UCSC; CG3812-RA; d. melanogaster.
DR   AGR; FB:FBgn0030421; -.
DR   CTD; 10554; -.
DR   FlyBase; FBgn0030421; Agpat1.
DR   VEuPathDB; VectorBase:FBgn0030421; -.
DR   eggNOG; KOG2848; Eukaryota.
DR   GeneTree; ENSGT00390000008726; -.
DR   HOGENOM; CLU_027938_10_1_1; -.
DR   InParanoid; Q9VYJ4; -.
DR   OMA; KKSLVWI; -.
DR   OrthoDB; 209232at2759; -.
DR   Reactome; R-DME-1483166; Synthesis of PA.
DR   Reactome; R-DME-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-DME-6798695; Neutrophil degranulation.
DR   BioGRID-ORCS; 32230; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 32230; -.
DR   Proteomes; UP000000803; Chromosome X.
DR   Bgee; FBgn0030421; Expressed in saliva-secreting gland and 18 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central.
DR   CDD; cd07989; LPLAT_AGPAT-like; 1.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   NCBIfam; TIGR00530; AGP_acyltrn; 1.
DR   PANTHER; PTHR10434; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR10434:SF11; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267,
KW   ECO:0000313|EMBL:AAF48201.1};
KW   Lipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Lipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|RuleBase:RU361267};
KW   Phospholipid metabolism {ECO:0000256|RuleBase:RU361267};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000803};
KW   Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:AAF48201.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        35..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..212
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   343 AA;  38235 MW;  FB48477231A51F5D CRC64;
     MITMTSFIEL LGLFLLLMLP FLYETNHIFR YYFKFLMYYG IVSFNSIILI PAFLTRPCDV
     RNLLWASTWC HRVSTLIGLR WELRGKEHLA KDQACIIVAN HQSSLDVLGM FNIWHVMNKC
     TVVAKRELFY AWPFGLAAWL AGLIFIDRVR GEKARETLND VNRRIKKQRI KLWVFPEGTR
     RNTGALHPFK KGAFHMAIDQ QIPILPVVFS SYCTFLNDKK KILNSGRIVI TTLPPVSTEG
     LTKDDIDVLM ERVRSQMIET FKVTSAEALH RYKPIKKVGI PAASSASTSS TTTTTLASPG
     TAVTPVADAA VAAAAAVASS SSAYGQPPGY EAGAAKASLL KTL
//
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