ID   PLCA_HUMAN              Reviewed;         283 AA.
AC   Q99943; A2BFI5; Q5BL03;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 2.
DT   27-MAR-2024, entry version 196.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase alpha;
DE            EC=2.3.1.51 {ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 1;
DE            Short=1-AGP acyltransferase 1;
DE            Short=1-AGPAT 1;
DE   AltName: Full=Lysophosphatidic acid acyltransferase alpha {ECO:0000303|PubMed:9461603};
DE            Short=LPAAT-alpha;
DE   AltName: Full=Protein G15;
DE   Flags: Precursor;
GN   Name=AGPAT1; Synonyms=G15;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9212163; DOI=10.1089/dna.1997.16.691;
RA   West J., Tompkins C.K., Balantac N., Nudelman E., Meengs B., White T.,
RA   Bursten S., Coleman J., Kumar A., Singer J.W., Leung D.W.;
RT   "Cloning and expression of two human lysophosphatidic acid acyltransferase
RT   cDNAs that enhance cytokine-induced signaling responses in cells.";
RL   DNA Cell Biol. 16:691-701(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9291118; DOI=10.1042/bj3260455;
RA   Stamps A.C., Elmore M.A., Hill M.E., Kelly K., Makda A.A., Finnen M.J.;
RT   "A human cDNA sequence with homology to non-mammalian lysophosphatidic acid
RT   acyltransferases.";
RL   Biochem. J. 326:455-461(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, AND TOPOLOGY.
RX   PubMed=9461603; DOI=10.1074/jbc.273.7.4096;
RA   Aguado B., Campbell R.D.;
RT   "Characterization of a human lysophosphatidic acid acyltransferase that is
RT   encoded by a gene located in the class III region of the human major
RT   histocompatibility complex.";
RL   J. Biol. Chem. 273:4096-4105(1998).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, Lung, and Skin;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND MOTIF EGTR.
RX   PubMed=21873652; DOI=10.1074/jbc.m111.250449;
RA   Agarwal A.K., Sukumaran S., Cortes V.A., Tunison K., Mizrachi D.,
RA   Sankella S., Gerard R.D., Horton J.D., Garg A.;
RT   "Human 1-acylglycerol-3-phosphate O-acyltransferase isoforms 1 and 2:
RT   biochemical characterization and inability to rescue hepatic steatosis in
RT   Agpat2(-/-) gene lipodystrophic mice.";
RL   J. Biol. Chem. 286:37676-37691(2011).
CC   -!- FUNCTION: Converts 1-acyl-sn-glycerol-3-phosphate (lysophosphatidic
CC       acid or LPA) into 1,2-diacyl-sn-glycerol-3-phosphate (phosphatidic acid
CC       or PA) by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone. {ECO:0000269|PubMed:21873652,
CC       ECO:0000269|PubMed:9461603}.
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:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37131, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74546;
CC         Evidence={ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + hexadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37143, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74551;
CC         Evidence={ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + heptadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-heptadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37155, ChEBI:CHEBI:57287, ChEBI:CHEBI:74307,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74558;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + octadecanoyl-CoA
CC         = 1-(9Z-octadecenoyl)-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37147, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74552;
CC         Evidence={ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37148;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z,12Z)-octadecadienoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-
CC         3-phosphate = 1-(9Z)-octadecenoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC         glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37159, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57383, ChEBI:CHEBI:74544, ChEBI:CHEBI:74563;
CC         Evidence={ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + tetradecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37171, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74579;
CC         Evidence={ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC         Evidence={ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + pentadecanoyl-CoA
CC         = 1-(9Z)-octadecenoyl-2-pentadecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37175, ChEBI:CHEBI:57287, ChEBI:CHEBI:74309,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:74578;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-hexadecanoyl-sn-glycero-3-phosphate
CC         = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:33187, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:57518, ChEBI:CHEBI:64839;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(9Z,12Z,15Z)-octadecatrienoyl-sn-
CC         glycero-3-phosphate = 1-(9Z,12Z,15Z)-octadecatrienoyl-2-(9Z)-
CC         octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37139,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74549,
CC         ChEBI:CHEBI:74550; Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-(6Z,9Z,12Z-octadecatrienoyl)-sn-
CC         glycero-3-phosphate = (6Z,9Z,12Z)-octadecatrienoyl-2-(9Z)-
CC         octadecenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37179,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:74581,
CC         ChEBI:CHEBI:74582; Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-eicosanoyl-sn-glycero-3-phosphate =
CC         1-eicosanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37183, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387,
CC         ChEBI:CHEBI:74583, ChEBI:CHEBI:74584;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-octadecenoyl-CoA + 1-tetradecanoyl-sn-glycerol 3-
CC         phosphate = 1-tetradecanoyl-2-(9Z)-octadecenoyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:37187, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57387, ChEBI:CHEBI:72683, ChEBI:CHEBI:74586;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-(9Z-octadecenoyl)-sn-
CC         glycero-3-phosphate = 1-(9Z)-octadecenoyl-2-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoyl-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:37443,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:74544,
CC         ChEBI:CHEBI:74928; Evidence={ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37444;
CC         Evidence={ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + dodecanoyl-CoA =
CC         1-(9Z)-octadecenoyl-2-dodecanoyl-sn-glycero-3-phosphate + CoA;
CC         Xref=Rhea:RHEA:37591, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:75076;
CC         Evidence={ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37592;
CC         Evidence={ECO:0000305|PubMed:9461603};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1-(9Z)-octadecenoyl-2-(6Z)-octadecenoyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:37607, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:75123, ChEBI:CHEBI:75124;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37608;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(11Z)-octadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1-(9Z)-octadecenoyl-2-(11Z)-octadecenoyl-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:37603, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:74544, ChEBI:CHEBI:75121, ChEBI:CHEBI:75122;
CC         Evidence={ECO:0000269|PubMed:21873652};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604;
CC         Evidence={ECO:0000305|PubMed:21873652};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9Z)-hexadecenoyl-CoA + 1-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphate = 1-(9Z-octadecenoyl)-2-(9Z-hexadecenoyl)-sn-glycero-3-
CC         phosphate + CoA; Xref=Rhea:RHEA:40195, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:61540, ChEBI:CHEBI:74544, ChEBI:CHEBI:74697;
CC         Evidence={ECO:0000269|PubMed:9461603};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40196;
CC         Evidence={ECO:0000305|PubMed:9461603};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=137.97 uM for C14:0-CoA {ECO:0000269|PubMed:21873652};
CC         KM=3.04 uM for C15:0-CoA {ECO:0000269|PubMed:21873652};
CC         KM=116.73 uM for C18:0-CoA {ECO:0000269|PubMed:21873652};
CC         KM=39.37 uM for C18:1-CoA {ECO:0000269|PubMed:21873652};
CC         KM=6 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21873652};
CC         Vmax=96.21 nmol/min/mg enzyme for C14:0-CoA
CC         {ECO:0000269|PubMed:21873652};
CC         Vmax=86.09 nmol/min/mg enzyme for C15:0-CoA
CC         {ECO:0000269|PubMed:21873652};
CC         Vmax=91.94 nmol/min/mg enzyme for C18:0-CoA
CC         {ECO:0000269|PubMed:21873652};
CC         Vmax=77.57 nmol/min/mg enzyme for C18:1-CoA
CC         {ECO:0000269|PubMed:21873652};
CC         Vmax=92 nmol/min/mg enzyme for LPA sn-1 C18:1
CC         {ECO:0000269|PubMed:21873652};
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-
CC       diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- INTERACTION:
CC       Q99943; P50222: MEOX2; NbExp=3; IntAct=EBI-3893468, EBI-748397;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9461603}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in adipose tissue and
CC       at high levels in testis and pancreas. Expressed at lower levels in
CC       tissues such as heart, brain, placenta, kidney, lung, spleen, thymus,
CC       prostate, ovary, intestine, colon, leukocyte and liver.
CC       {ECO:0000269|PubMed:21873652}.
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|UniProtKB:Q9D517}.
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB47493.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U56417; AAB58775.1; -; mRNA.
DR   EMBL; U75971; AAB96378.1; -; mRNA.
DR   EMBL; Y09565; CAA70758.1; -; mRNA.
DR   EMBL; U89336; AAB47493.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL662884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL845464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX284686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX927239; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR933878; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR812478; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03600.1; -; Genomic_DNA.
DR   EMBL; BC002402; AAH02402.1; -; mRNA.
DR   EMBL; BC003007; AAH03007.1; -; mRNA.
DR   EMBL; BC004310; AAH04310.1; -; mRNA.
DR   EMBL; BC090849; AAH90849.1; -; mRNA.
DR   CCDS; CCDS4744.1; -.
DR   RefSeq; NP_006402.1; NM_006411.3.
DR   RefSeq; NP_116130.2; NM_032741.4.
DR   RefSeq; XP_005248863.1; XM_005248806.2.
DR   RefSeq; XP_011512536.1; XM_011514234.1.
DR   AlphaFoldDB; Q99943; -.
DR   SMR; Q99943; -.
DR   BioGRID; 115805; 305.
DR   IntAct; Q99943; 12.
DR   MINT; Q99943; -.
DR   STRING; 9606.ENSP00000378877; -.
DR   ChEMBL; CHEMBL3583; -.
DR   SwissLipids; SLP:000000095; -.
DR   iPTMnet; Q99943; -.
DR   PhosphoSitePlus; Q99943; -.
DR   SwissPalm; Q99943; -.
DR   BioMuta; AGPAT1; -.
DR   DMDM; 3914372; -.
DR   EPD; Q99943; -.
DR   jPOST; Q99943; -.
DR   MassIVE; Q99943; -.
DR   MaxQB; Q99943; -.
DR   PaxDb; 9606-ENSP00000378877; -.
DR   PeptideAtlas; Q99943; -.
DR   ProteomicsDB; 78534; -.
DR   Pumba; Q99943; -.
DR   Antibodypedia; 28453; 165 antibodies from 21 providers.
DR   DNASU; 10554; -.
DR   Ensembl; ENST00000336984.6; ENSP00000337463.6; ENSG00000204310.13.
DR   Ensembl; ENST00000375104.6; ENSP00000364245.2; ENSG00000204310.13.
DR   Ensembl; ENST00000375107.8; ENSP00000364248.3; ENSG00000204310.13.
DR   Ensembl; ENST00000383294.4; ENSP00000372782.4; ENSG00000206324.11.
DR   Ensembl; ENST00000395496.5; ENSP00000378874.1; ENSG00000204310.13.
DR   Ensembl; ENST00000395497.5; ENSP00000378875.1; ENSG00000204310.13.
DR   Ensembl; ENST00000395499.5; ENSP00000378877.1; ENSG00000204310.13.
DR   Ensembl; ENST00000399825.5; ENSP00000382721.1; ENSG00000206324.11.
DR   Ensembl; ENST00000399827.5; ENSP00000382723.1; ENSG00000206324.11.
DR   Ensembl; ENST00000399829.5; ENSP00000382725.1; ENSG00000206324.11.
DR   Ensembl; ENST00000399830.5; ENSP00000382726.1; ENSG00000206324.11.
DR   Ensembl; ENST00000399833.7; ENSP00000382728.3; ENSG00000206324.11.
DR   Ensembl; ENST00000414520.5; ENSP00000406615.1; ENSG00000227642.9.
DR   Ensembl; ENST00000414933.6; ENSP00000388870.2; ENSG00000227642.9.
DR   Ensembl; ENST00000415173.5; ENSP00000412805.1; ENSG00000228892.9.
DR   Ensembl; ENST00000416363.6; ENSP00000407189.2; ENSG00000236873.9.
DR   Ensembl; ENST00000417388.2; ENSP00000415015.2; ENSG00000228892.9.
DR   Ensembl; ENST00000424030.5; ENSP00000397765.1; ENSG00000236873.9.
DR   Ensembl; ENST00000425204.2; ENSP00000388253.2; ENSG00000226467.9.
DR   Ensembl; ENST00000425572.5; ENSP00000394919.1; ENSG00000235758.9.
DR   Ensembl; ENST00000427763.5; ENSP00000401410.1; ENSG00000226467.9.
DR   Ensembl; ENST00000430226.5; ENSP00000412304.1; ENSG00000235758.9.
DR   Ensembl; ENST00000430777.2; ENSP00000392820.2; ENSG00000236873.9.
DR   Ensembl; ENST00000433376.6; ENSP00000387810.2; ENSG00000228892.9.
DR   Ensembl; ENST00000433896.5; ENSP00000408842.1; ENSG00000236873.9.
DR   Ensembl; ENST00000434614.5; ENSP00000401287.1; ENSG00000235758.9.
DR   Ensembl; ENST00000436149.5; ENSP00000388090.1; ENSG00000235758.9.
DR   Ensembl; ENST00000439774.5; ENSP00000398016.1; ENSG00000236873.9.
DR   Ensembl; ENST00000440840.5; ENSP00000395863.1; ENSG00000236873.9.
DR   Ensembl; ENST00000444369.5; ENSP00000408032.1; ENSG00000227642.9.
DR   Ensembl; ENST00000446323.5; ENSP00000392083.1; ENSG00000226467.9.
DR   Ensembl; ENST00000446463.6; ENSP00000405864.2; ENSG00000226467.9.
DR   Ensembl; ENST00000448196.2; ENSP00000404106.2; ENSG00000235758.9.
DR   Ensembl; ENST00000449776.5; ENSP00000410831.1; ENSG00000226467.9.
DR   Ensembl; ENST00000451833.5; ENSP00000406582.1; ENSG00000228892.9.
DR   Ensembl; ENST00000452393.5; ENSP00000406614.1; ENSG00000228892.9.
DR   Ensembl; ENST00000452427.6; ENSP00000387738.2; ENSG00000235758.9.
DR   Ensembl; ENST00000454929.5; ENSP00000390988.1; ENSG00000227642.9.
DR   Ensembl; ENST00000455898.5; ENSP00000395613.1; ENSG00000228892.9.
DR   Ensembl; ENST00000456421.5; ENSP00000389516.1; ENSG00000227642.9.
DR   Ensembl; ENST00000456679.2; ENSP00000388815.2; ENSG00000227642.9.
DR   Ensembl; ENST00000457923.5; ENSP00000405565.1; ENSG00000226467.9.
DR   GeneID; 10554; -.
DR   KEGG; hsa:10554; -.
DR   MANE-Select; ENST00000375107.8; ENSP00000364248.3; NM_006411.4; NP_006402.1.
DR   UCSC; uc003oae.4; human.
DR   AGR; HGNC:324; -.
DR   CTD; 10554; -.
DR   DisGeNET; 10554; -.
DR   GeneCards; AGPAT1; -.
DR   HGNC; HGNC:324; AGPAT1.
DR   HPA; ENSG00000204310; Low tissue specificity.
DR   MIM; 603099; gene.
DR   neXtProt; NX_Q99943; -.
DR   OpenTargets; ENSG00000204310; -.
DR   PharmGKB; PA24621; -.
DR   VEuPathDB; HostDB:ENSG00000204310; -.
DR   eggNOG; KOG2848; Eukaryota.
DR   GeneTree; ENSGT00390000008726; -.
DR   HOGENOM; CLU_027938_10_1_1; -.
DR   InParanoid; Q99943; -.
DR   OMA; KKSLVWI; -.
DR   OrthoDB; 209232at2759; -.
DR   PhylomeDB; Q99943; -.
DR   TreeFam; TF314867; -.
DR   BioCyc; MetaCyc:HS09762-MONOMER; -.
DR   BRENDA; 2.3.1.51; 2681.
DR   PathwayCommons; Q99943; -.
DR   Reactome; R-HSA-1483166; Synthesis of PA.
DR   Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR   SignaLink; Q99943; -.
DR   UniPathway; UPA00557; UER00613.
DR   BioGRID-ORCS; 10554; 41 hits in 1164 CRISPR screens.
DR   ChiTaRS; AGPAT1; human.
DR   GeneWiki; AGPAT1; -.
DR   GenomeRNAi; 10554; -.
DR   Pharos; Q99943; Tbio.
DR   PRO; PR:Q99943; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q99943; Protein.
DR   Bgee; ENSG00000204310; Expressed in right frontal lobe and 97 other cell types or tissues.
DR   ExpressionAtlas; Q99943; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IGI:BHF-UCL.
DR   GO; GO:0006644; P:phospholipid metabolic process; TAS:ProtInc.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IMP:BHF-UCL.
DR   GO; GO:0001961; P:positive regulation of cytokine-mediated signaling pathway; IC:BHF-UCL.
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:SF66; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE ALPHA; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR   Genevisible; Q99943; HS.
PE   1: Evidence at protein level;
KW   Acyltransferase; Endoplasmic reticulum; Lipid biosynthesis;
KW   Lipid metabolism; Membrane; Phospholipid biosynthesis;
KW   Phospholipid metabolism; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..283
FT                   /note="1-acyl-sn-glycerol-3-phosphate acyltransferase
FT                   alpha"
FT                   /id="PRO_0000208190"
FT   TOPO_DOM        27..37
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:9461603"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..127
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:9461603"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        149..283
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305|PubMed:9461603"
FT   MOTIF           104..109
FT                   /note="HXXXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9D517"
FT   MOTIF           178..181
FT                   /note="EGTR motif"
FT                   /evidence="ECO:0000305|PubMed:21873652"
FT   VARIANT         30
FT                   /note="P -> S (in dbSNP:rs11964847)"
FT                   /id="VAR_050593"
SQ   SEQUENCE   283 AA;  31717 MW;  71F3207259747C68 CRC64;
     MDLWPGAWML LLLLFLLLLF LLPTLWFCSP SAKYFFKMAF YNGWILFLAV LAIPVCAVRG
     RNVENMKILR LMLLHIKYLY GIRVEVRGAH HFPPSQPYVV VSNHQSSLDL LGMMEVLPGR
     CVPIAKRELL WAGSAGLACW LAGVIFIDRK RTGDAISVMS EVAQTLLTQD VRVWVFPEGT
     RNHNGSMLPF KRGAFHLAVQ AQVPIVPIVM SSYQDFYCKK ERRFTSGQCQ VRVLPPVPTE
     GLTPDDVPAL ADRVRHSMLT VFREISTDGR GGGDYLKKPG GGG
//