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 02-MAR-2010, entry version 90. 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; 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 MEDLINE=97355682; 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 MEDLINE=97419100; 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 MEDLINE=98129822; 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 MEDLINE=22935763; 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). 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. CC -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CC CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3. CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein CC (Potential). 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 (By similarity). CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 IPI; IPI00019141; -. DR RefSeq; NP_006402.1; -. DR RefSeq; NP_116130.2; -. DR UniGene; Hs.409230; -. DR STRING; Q99943; -. DR PhosphoSite; Q99943; -. DR PRIDE; Q99943; -. DR Ensembl; ENST00000336984; ENSP00000337463; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000375104; ENSP00000364245; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000375107; ENSP00000364248; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000383294; ENSP00000372782; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000395496; ENSP00000378874; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000395497; ENSP00000378875; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000395499; ENSP00000378877; ENSG00000204310; Homo sapiens. DR Ensembl; ENST00000399825; ENSP00000382721; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000399827; ENSP00000382723; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000399829; ENSP00000382725; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000399830; ENSP00000382726; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000399833; ENSP00000382728; ENSG00000206324; Homo sapiens. DR Ensembl; ENST00000414520; ENSP00000406615; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000414933; ENSP00000388870; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000415173; ENSP00000412805; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000416363; ENSP00000407189; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000417388; ENSP00000415015; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000424030; ENSP00000397765; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000425204; ENSP00000388253; ENSG00000226467; Homo sapiens. DR Ensembl; ENST00000425572; ENSP00000394919; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000427763; ENSP00000401410; ENSG00000226467; Homo sapiens. DR Ensembl; ENST00000430226; ENSP00000412304; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000430777; ENSP00000392820; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000433376; ENSP00000387810; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000433896; ENSP00000408842; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000434614; ENSP00000401287; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000436149; ENSP00000388090; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000439774; ENSP00000398016; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000440840; ENSP00000395863; ENSG00000236873; Homo sapiens. DR Ensembl; ENST00000444369; ENSP00000408032; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000446323; ENSP00000392083; ENSG00000226467; Homo sapiens. DR Ensembl; ENST00000446463; ENSP00000405864; ENSG00000226467; Homo sapiens. DR Ensembl; ENST00000448196; ENSP00000404106; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000449776; ENSP00000410831; ENSG00000226467; Homo sapiens. DR Ensembl; ENST00000451833; ENSP00000406582; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000452393; ENSP00000406614; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000452427; ENSP00000387738; ENSG00000235758; Homo sapiens. DR Ensembl; ENST00000454929; ENSP00000390988; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000455898; ENSP00000395613; ENSG00000228892; Homo sapiens. DR Ensembl; ENST00000456421; ENSP00000389516; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000456679; ENSP00000388815; ENSG00000227642; Homo sapiens. DR Ensembl; ENST00000457923; ENSP00000405565; ENSG00000226467; Homo sapiens. DR GeneID; 10554; -. DR KEGG; hsa:10554; -. DR UCSC; uc003oae.1; human. DR CTD; 10554; -. DR GeneCards; GC06M032243; -. DR H-InvDB; HIX0005747; -. DR H-InvDB; HIX0057918; -. DR H-InvDB; HIX0058092; -. DR HGNC; HGNC:324; AGPAT1. DR MIM; 603099; gene. DR PharmGKB; PA24621; -. DR HOGENOM; HBG736534; -. DR HOVERGEN; HBG000676; -. DR InParanoid; Q99943; -. DR OMA; KSLVWIP; -. DR OrthoDB; EOG99GP2H; -. DR PhylomeDB; Q99943; -. DR BioCyc; MetaCyc:ENSG00000168448-MONOMER; -. DR BRENDA; 2.3.1.51; 247. DR Reactome; REACT_1505; Integration of energy metabolism. DR Reactome; REACT_602; Metabolism of lipids and lipoproteins. DR NextBio; 40041; -. DR CleanEx; HS_AGPAT1; -. DR Genevestigator; Q99943; -. DR GermOnline; ENSG00000204310; Homo sapiens. DR GO; GO:0005829; C:cytosol; EXP:Reactome. DR GO; GO:0005783; C:endoplasmic reticulum; TAS:ProtInc. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IGI:UniProtKB. DR GO; GO:0046027; F:phospholipid:diacylglycerol acyltransferase...; EXP:Reactome. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IGI:UniProtKB. DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB. DR GO; GO:0001961; P:positive regulation of cytokine-mediated si...; IC:UniProtKB. DR InterPro; IPR002123; Acyltransferase. DR InterPro; IPR004552; AGP_acyltrans. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR TIGRFAMs; TIGR00530; AGP_acyltrn; 1. PE 2: Evidence at transcript level; KW Acyltransferase; Complete proteome; Membrane; KW Phospholipid biosynthesis; Polymorphism; Transferase; Transmembrane. FT CHAIN 1 283 1-acyl-sn-glycerol-3-phosphate FT acyltransferase alpha. FT /FTId=PRO_0000208190. FT TRANSMEM 7 27 Potential. FT TRANSMEM 38 58 Potential. FT TRANSMEM 128 148 Potential. FT MOTIF 104 109 HXXXXD 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 //