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   29-APR-2015, entry version 137.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase alpha;
DE            EC=2.3.1.51;
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;
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9212163;
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
RT   acyltransferase cDNAs that enhance cytokine-induced signaling
RT   responses in cells.";
RL   DNA Cell Biol. 16:691-701(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9291118;
RA   Stamps A.C., Elmore M.A., Hill M.E., Kelly K., Makda A.A.,
RA   Finnen M.J.;
RT   "A human cDNA sequence with homology to non-mammalian lysophosphatidic
RT   acid acyltransferases.";
RL   Biochem. J. 326:455-461(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9461603; DOI=10.1074/jbc.273.7.4096;
RA   Aguado B., Campbell R.D.;
RT   "Characterization of a human lysophosphatidic acid acyltransferase
RT   that is encoded by a gene located in the class III region of the human
RT   major 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.,
RA   Campbell R.D., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
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
RT   in Agpat2(-/-) gene lipodystrophic mice.";
RL   J. Biol. Chem. 286:37676-37691(2011).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone. {ECO:0000269|PubMed:21873652}.
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC       {ECO:0000269|PubMed:21873652}.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- INTERACTION:
CC       A4D127:MEOX2; NbExp=3; IntAct=EBI-3893468, EBI-10172134;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:21873652}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:21873652}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed in adipose tissue
CC       and at high levels in testis and pancreas. Expressed at lower
CC       levels in tissues such as heart, brain, placenta, kidney, lung,
CC       spleen, thymus, prostate, ovary, intestine, colon, leukocyte and
CC       liver. {ECO:0000269|PubMed:21873652}.
CC   -!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
CC       and may constitute the binding site for the phosphate moiety of
CC       the glycerol-3-phosphate. {ECO:0000250}.
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=Translation N-terminally extended.; 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; CAI18347.1; -; Genomic_DNA.
DR   EMBL; AL662828; CAI17430.1; -; Genomic_DNA.
DR   EMBL; AL845464; CAI41807.1; -; Genomic_DNA.
DR   EMBL; BX284686; CAM26221.1; -; Genomic_DNA.
DR   EMBL; BX927239; CAQ06593.1; -; Genomic_DNA.
DR   EMBL; CR933878; CAQ09622.1; -; Genomic_DNA.
DR   EMBL; CR812478; CAQ10697.1; -; 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_005248806.1.
DR   RefSeq; XP_005272819.1; XM_005272762.1.
DR   RefSeq; XP_005274887.1; XM_005274830.1.
DR   RefSeq; XP_005275131.1; XM_005275074.1.
DR   RefSeq; XP_005275261.1; XM_005275204.1.
DR   RefSeq; XP_005275395.1; XM_005275338.1.
DR   RefSeq; XP_005275562.1; XM_005275505.1.
DR   UniGene; Hs.409230; -.
DR   ProteinModelPortal; Q99943; -.
DR   BioGrid; 115805; 11.
DR   IntAct; Q99943; 3.
DR   STRING; 9606.ENSP00000401287; -.
DR   ChEMBL; CHEMBL3583; -.
DR   PhosphoSite; Q99943; -.
DR   BioMuta; AGPAT1; -.
DR   DMDM; 3914372; -.
DR   MaxQB; Q99943; -.
DR   PaxDb; Q99943; -.
DR   PRIDE; Q99943; -.
DR   Ensembl; ENST00000336984; ENSP00000337463; ENSG00000204310.
DR   Ensembl; ENST00000375104; ENSP00000364245; ENSG00000204310.
DR   Ensembl; ENST00000375107; ENSP00000364248; ENSG00000204310.
DR   Ensembl; ENST00000383294; ENSP00000372782; ENSG00000206324.
DR   Ensembl; ENST00000395496; ENSP00000378874; ENSG00000204310.
DR   Ensembl; ENST00000395497; ENSP00000378875; ENSG00000204310.
DR   Ensembl; ENST00000395499; ENSP00000378877; ENSG00000204310.
DR   Ensembl; ENST00000399825; ENSP00000382721; ENSG00000206324.
DR   Ensembl; ENST00000399827; ENSP00000382723; ENSG00000206324.
DR   Ensembl; ENST00000399829; ENSP00000382725; ENSG00000206324.
DR   Ensembl; ENST00000399830; ENSP00000382726; ENSG00000206324.
DR   Ensembl; ENST00000399833; ENSP00000382728; ENSG00000206324.
DR   Ensembl; ENST00000414520; ENSP00000406615; ENSG00000227642.
DR   Ensembl; ENST00000414933; ENSP00000388870; ENSG00000227642.
DR   Ensembl; ENST00000415173; ENSP00000412805; ENSG00000228892.
DR   Ensembl; ENST00000416363; ENSP00000407189; ENSG00000236873.
DR   Ensembl; ENST00000417388; ENSP00000415015; ENSG00000228892.
DR   Ensembl; ENST00000424030; ENSP00000397765; ENSG00000236873.
DR   Ensembl; ENST00000425204; ENSP00000388253; ENSG00000226467.
DR   Ensembl; ENST00000425572; ENSP00000394919; ENSG00000235758.
DR   Ensembl; ENST00000427763; ENSP00000401410; ENSG00000226467.
DR   Ensembl; ENST00000430226; ENSP00000412304; ENSG00000235758.
DR   Ensembl; ENST00000430777; ENSP00000392820; ENSG00000236873.
DR   Ensembl; ENST00000433376; ENSP00000387810; ENSG00000228892.
DR   Ensembl; ENST00000433896; ENSP00000408842; ENSG00000236873.
DR   Ensembl; ENST00000434614; ENSP00000401287; ENSG00000235758.
DR   Ensembl; ENST00000436149; ENSP00000388090; ENSG00000235758.
DR   Ensembl; ENST00000439774; ENSP00000398016; ENSG00000236873.
DR   Ensembl; ENST00000440840; ENSP00000395863; ENSG00000236873.
DR   Ensembl; ENST00000444369; ENSP00000408032; ENSG00000227642.
DR   Ensembl; ENST00000446323; ENSP00000392083; ENSG00000226467.
DR   Ensembl; ENST00000446463; ENSP00000405864; ENSG00000226467.
DR   Ensembl; ENST00000448196; ENSP00000404106; ENSG00000235758.
DR   Ensembl; ENST00000449776; ENSP00000410831; ENSG00000226467.
DR   Ensembl; ENST00000451833; ENSP00000406582; ENSG00000228892.
DR   Ensembl; ENST00000452393; ENSP00000406614; ENSG00000228892.
DR   Ensembl; ENST00000452427; ENSP00000387738; ENSG00000235758.
DR   Ensembl; ENST00000454929; ENSP00000390988; ENSG00000227642.
DR   Ensembl; ENST00000455898; ENSP00000395613; ENSG00000228892.
DR   Ensembl; ENST00000456421; ENSP00000389516; ENSG00000227642.
DR   Ensembl; ENST00000456679; ENSP00000388815; ENSG00000227642.
DR   Ensembl; ENST00000457923; ENSP00000405565; ENSG00000226467.
DR   GeneID; 10554; -.
DR   KEGG; hsa:10554; -.
DR   UCSC; uc003oae.3; human.
DR   CTD; 10554; -.
DR   GeneCards; GC06M032135; -.
DR   GeneCards; GC06Mi32147; -.
DR   GeneCards; GC06Mj32084; -.
DR   GeneCards; GC06Ml32175; -.
DR   GeneCards; GC06Mm32212; -.
DR   GeneCards; GC06Mn32093; -.
DR   GeneCards; GC06Mo32142; -.
DR   HGNC; HGNC:324; AGPAT1.
DR   MIM; 603099; gene.
DR   neXtProt; NX_Q99943; -.
DR   PharmGKB; PA24621; -.
DR   eggNOG; COG0204; -.
DR   GeneTree; ENSGT00390000008726; -.
DR   HOGENOM; HOG000026375; -.
DR   HOVERGEN; HBG000676; -.
DR   InParanoid; Q99943; -.
DR   KO; K13509; -.
DR   OMA; MLTIFRE; -.
DR   PhylomeDB; Q99943; -.
DR   TreeFam; TF314867; -.
DR   BioCyc; MetaCyc:HS09762-MONOMER; -.
DR   BRENDA; 2.3.1.51; 2681.
DR   Reactome; REACT_1190; Triglyceride Biosynthesis.
DR   Reactome; REACT_120906; Synthesis of PA.
DR   Reactome; REACT_2122; ChREBP activates metabolic gene expression.
DR   UniPathway; UPA00557; UER00613.
DR   GeneWiki; AGPAT1; -.
DR   GenomeRNAi; 10554; -.
DR   NextBio; 40041; -.
DR   PRO; PR:Q99943; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Proteomes; UP000005640; Unplaced.
DR   Bgee; Q99943; -.
DR   CleanEx; HS_AGPAT1; -.
DR   ExpressionAtlas; Q99943; baseline and differential.
DR   Genevestigator; Q99943; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IGI:BHF-UCL.
DR   GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
DR   GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR   GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IGI:BHF-UCL.
DR   GO; GO:0006644; P:phospholipid metabolic process; TAS:Reactome.
DR   GO; GO:0031325; P:positive regulation of cellular metabolic process; TAS:Reactome.
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   GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Complete proteome; Endoplasmic reticulum;
KW   Lipid biosynthesis; Lipid metabolism; Membrane;
KW   Phospholipid biosynthesis; Phospholipid metabolism; Polymorphism;
KW   Reference proteome; Signal; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     26       {ECO:0000255}.
FT   CHAIN        27    283       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase alpha.
FT                                /FTId=PRO_0000208190.
FT   TRANSMEM     38     58       Helical. {ECO:0000255}.
FT   TRANSMEM    128    148       Helical. {ECO:0000255}.
FT   TRANSMEM    193    213       Helical. {ECO:0000255}.
FT   MOTIF       104    109       HXXXXD motif.
FT   MOTIF       178    181       EGTR motif.
FT   VARIANT      30     30       P -> S (in dbSNP:rs11964847).
FT                                /FTId=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
//