PLCB_HUMAN
ID PLCB_HUMAN Reviewed; 278 AA.
AC O15120; O00516; O15106; Q5VUD3; Q5VUD4; Q9BSV7; Q9BWR7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase beta;
DE EC=2.3.1.51 {ECO:0000269|PubMed:15629135, ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711};
DE AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 2;
DE Short=1-AGP acyltransferase 2;
DE Short=1-AGPAT 2;
DE AltName: Full=Lysophosphatidic acid acyltransferase beta {ECO:0000303|PubMed:9242711};
DE Short=LPAAT-beta;
DE Flags: Precursor;
GN Name=AGPAT2;
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] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=9242711; DOI=10.1074/jbc.272.32.20299;
RA Eberhardt C., Gray P.W., Tjoelker L.W.;
RT "Human lysophosphatidic acid acyltransferase. cDNA cloning, expression, and
RT localization to chromosome 9q34.3.";
RL J. Biol. Chem. 272:20299-20305(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] (ISOFORM 1).
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 [4]
RP SEQUENCE REVISION TO 51.
RA Leung D.W., Tompkin C.K., West J.;
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, 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 REVIEW.
RX PubMed=15028826; DOI=10.1056/nejmra025261;
RA Garg A.;
RT "Acquired and inherited lipodystrophies.";
RL N. Engl. J. Med. 350:1220-1234(2004).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION OF VARIANTS CGL1
RP ARG-136; PHE-140 DEL; PRO-228 AND VAL-239.
RX PubMed=15629135; DOI=10.1016/j.bbrc.2004.12.024;
RA Haque W., Garg A., Agarwal A.K.;
RT "Enzymatic activity of naturally occurring 1-acylglycerol-3-phosphate-O-
RT acyltransferase 2 mutants associated with congenital generalized
RT lipodystrophy.";
RL Biochem. Biophys. Res. Commun. 327:446-453(2005).
RN [10]
RP CATALYTIC ACTIVITY.
RX PubMed=19075029; DOI=10.1194/jlr.m800567-jlr200;
RA Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.;
RT "The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin
RT acyltransferase is an acyltransferase of multiple anionic
RT lysophospholipids.";
RL J. Lipid Res. 50:945-956(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
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).
RN [13]
RP VARIANTS CGL1 ARG-136; PHE-140 DEL; PRO-228 AND VAL-239.
RX PubMed=11967537; DOI=10.1038/ng880;
RA Agarwal A.K., Arioglu E., de Almeida S., Akkoc N., Taylor S.I.,
RA Bowcock A.M., Barnes R.I., Garg A.;
RT "AGPAT2 is mutated in congenital generalized lipodystrophy linked to
RT chromosome 9q34.";
RL Nat. Genet. 31:21-23(2002).
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:15629135,
CC ECO:0000269|PubMed:19075029, ECO:0000269|PubMed:21873652,
CC ECO:0000269|PubMed:9242711}.
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:15629135, ECO:0000269|PubMed:19075029,
CC ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC Evidence={ECO:0000305|PubMed:15629135, ECO:0000305|PubMed:19075029,
CC ECO:0000305|PubMed:21873652, ECO:0000305|PubMed:9242711};
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:15629135, ECO:0000269|PubMed:21873652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC Evidence={ECO:0000305|PubMed:15629135, ECO:0000305|PubMed:21873652};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC Evidence={ECO:0000305|PubMed:21873652};
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=(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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC Evidence={ECO:0000305|PubMed:21873652};
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};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC Evidence={ECO:0000305|PubMed:21873652};
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-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=(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=1-hexadecanoyl-sn-glycero-3-phosphate + octadecanoyl-CoA = 1-
CC hexadecanoyl-2-octadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35907, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72857;
CC Evidence={ECO:0000269|PubMed:9242711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35908;
CC Evidence={ECO:0000305|PubMed:9242711};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + 1-hexadecanoyl-sn-
CC glycero-3-phosphate = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycero-3-phosphate + CoA; Xref=Rhea:RHEA:35915,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:57518,
CC ChEBI:CHEBI:72864; Evidence={ECO:0000269|PubMed:9242711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35916;
CC Evidence={ECO:0000305|PubMed:9242711};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + hexadecanoyl-CoA =
CC 1,2-dihexadecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35903, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72859;
CC Evidence={ECO:0000269|PubMed:9242711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35904;
CC Evidence={ECO:0000305|PubMed:9242711};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + tetradecanoyl-CoA = 1-
CC hexadecanoyl-2-tetradecanoyl-sn-glycero-3-phosphate + CoA;
CC Xref=Rhea:RHEA:35899, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:72858;
CC Evidence={ECO:0000269|PubMed:9242711};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35900;
CC Evidence={ECO:0000305|PubMed:9242711};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.05 uM for C15:0-CoA {ECO:0000269|PubMed:21873652};
CC KM=523.97 uM for C18:0-CoA {ECO:0000269|PubMed:21873652};
CC KM=30.21 uM for C18:1-CoA {ECO:0000269|PubMed:21873652};
CC KM=8.29 uM for LPA sn-1 C18:1 {ECO:0000269|PubMed:21873652};
CC Vmax=51.61 nmol/min/mg enzyme for C15:0-CoA
CC {ECO:0000269|PubMed:21873652};
CC Vmax=95.55 nmol/min/mg enzyme for C18:0-CoA
CC {ECO:0000269|PubMed:21873652};
CC Vmax=73.81 nmol/min/mg enzyme for C18:1-CoA
CC {ECO:0000269|PubMed:21873652};
CC Vmax=86.05 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 -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21873652}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15120-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15120-2; Sequence=VSP_005071;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in adipose tissue, pancreas
CC and liver. {ECO:0000269|PubMed:21873652, ECO:0000269|PubMed:9242711}.
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 -!- DISEASE: Congenital generalized lipodystrophy 1 (CGL1) [MIM:608594]: An
CC autosomal recessive disorder characterized by a near complete absence
CC of adipose tissue, extreme insulin resistance, hypertriglyceridemia,
CC hepatic steatosis and early onset of diabetes.
CC {ECO:0000269|PubMed:11967537, ECO:0000269|PubMed:15629135}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC acyltransferase family. {ECO:0000305}.
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DR EMBL; AF000237; AAC51649.1; -; mRNA.
DR EMBL; AF011374; AAB64299.1; -; mRNA.
DR EMBL; U56418; AAB58776.2; -; mRNA.
DR EMBL; AL590226; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88249.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88251.1; -; Genomic_DNA.
DR EMBL; BC000026; AAH00026.1; -; mRNA.
DR EMBL; BC004529; AAH04529.1; -; mRNA.
DR CCDS; CCDS35181.1; -. [O15120-2]
DR CCDS; CCDS7003.1; -. [O15120-1]
DR RefSeq; NP_001012745.1; NM_001012727.1. [O15120-2]
DR RefSeq; NP_006403.2; NM_006412.3. [O15120-1]
DR AlphaFoldDB; O15120; -.
DR SMR; O15120; -.
DR BioGRID; 115806; 96.
DR CORUM; O15120; -.
DR IntAct; O15120; 19.
DR STRING; 9606.ENSP00000360761; -.
DR BindingDB; O15120; -.
DR ChEMBL; CHEMBL4772; -.
DR SwissLipids; SLP:000000096; -.
DR iPTMnet; O15120; -.
DR PhosphoSitePlus; O15120; -.
DR BioMuta; AGPAT2; -.
DR EPD; O15120; -.
DR jPOST; O15120; -.
DR MassIVE; O15120; -.
DR MaxQB; O15120; -.
DR PaxDb; O15120; -.
DR PeptideAtlas; O15120; -.
DR PRIDE; O15120; -.
DR ProteomicsDB; 48457; -. [O15120-1]
DR ProteomicsDB; 48458; -. [O15120-2]
DR Antibodypedia; 18762; 175 antibodies from 27 providers.
DR DNASU; 10555; -.
DR Ensembl; ENST00000371694.7; ENSP00000360759.3; ENSG00000169692.13. [O15120-2]
DR Ensembl; ENST00000371696.7; ENSP00000360761.2; ENSG00000169692.13. [O15120-1]
DR Ensembl; ENST00000538402.1; ENSP00000438919.1; ENSG00000169692.13. [O15120-1]
DR GeneID; 10555; -.
DR KEGG; hsa:10555; -.
DR MANE-Select; ENST00000371696.7; ENSP00000360761.2; NM_006412.4; NP_006403.2.
DR UCSC; uc004cii.2; human. [O15120-1]
DR CTD; 10555; -.
DR DisGeNET; 10555; -.
DR GeneCards; AGPAT2; -.
DR GeneReviews; AGPAT2; -.
DR HGNC; HGNC:325; AGPAT2.
DR HPA; ENSG00000169692; Tissue enhanced (adipose tissue, breast, liver).
DR MalaCards; AGPAT2; -.
DR MIM; 603100; gene.
DR MIM; 608594; phenotype.
DR neXtProt; NX_O15120; -.
DR OpenTargets; ENSG00000169692; -.
DR Orphanet; 528; Congenital generalized lipodystrophy.
DR PharmGKB; PA24622; -.
DR VEuPathDB; HostDB:ENSG00000169692; -.
DR eggNOG; KOG2848; Eukaryota.
DR GeneTree; ENSGT00390000008726; -.
DR HOGENOM; CLU_027938_10_1_1; -.
DR InParanoid; O15120; -.
DR OMA; WVMRYTT; -.
DR PhylomeDB; O15120; -.
DR TreeFam; TF314867; -.
DR BioCyc; MetaCyc:HS09990-MON; -.
DR BRENDA; 2.3.1.51; 2681.
DR PathwayCommons; O15120; -.
DR Reactome; R-HSA-1483166; Synthesis of PA.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; O15120; -.
DR SignaLink; O15120; -.
DR UniPathway; UPA00557; UER00613.
DR BioGRID-ORCS; 10555; 35 hits in 1073 CRISPR screens.
DR GeneWiki; AGPAT2; -.
DR GenomeRNAi; 10555; -.
DR Pharos; O15120; Tchem.
DR PRO; PR:O15120; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O15120; protein.
DR Bgee; ENSG00000169692; Expressed in mucosa of transverse colon and 177 other tissues.
DR ExpressionAtlas; O15120; baseline and differential.
DR Genevisible; O15120; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
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:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IGI:BHF-UCL.
DR GO; GO:0006644; P:phospholipid metabolic process; NAS:UniProtKB.
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:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; Alternative splicing;
KW Congenital generalized lipodystrophy; Diabetes mellitus; Disease variant;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Signal; Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..278
FT /note="1-acyl-sn-glycerol-3-phosphate acyltransferase beta"
FT /id="PRO_0000208192"
FT TOPO_DOM 24..29
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..278
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT MOTIF 98..103
FT /note="HXXXXD motif"
FT /evidence="ECO:0000250|UniProtKB:Q9D517"
FT MOTIF 172..175
FT /note="EGTR motif"
FT /evidence="ECO:0000305|PubMed:21873652"
FT VAR_SEQ 165..196
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_005071"
FT VARIANT 136
FT /note="G -> R (in CGL1; reduced 1-acyl-sn-glycerol-3-
FT phosphate acyltransferase activity; dbSNP:rs797045222)"
FT /evidence="ECO:0000269|PubMed:11967537,
FT ECO:0000269|PubMed:15629135"
FT /id="VAR_017328"
FT VARIANT 140
FT /note="Missing (in CGL1; reduced 1-acyl-sn-glycerol-3-
FT phosphate acyltransferase activity)"
FT /evidence="ECO:0000269|PubMed:11967537,
FT ECO:0000269|PubMed:15629135"
FT /id="VAR_017326"
FT VARIANT 228
FT /note="L -> P (in CGL1; reduced 1-acyl-sn-glycerol-3-
FT phosphate acyltransferase activity; dbSNP:rs104894100)"
FT /evidence="ECO:0000269|PubMed:11967537,
FT ECO:0000269|PubMed:15629135"
FT /id="VAR_017327"
FT VARIANT 239
FT /note="A -> V (in CGL1; 90% of wild-type 1-acyl-sn-
FT glycerol-3-phosphate acyltransferase activity;
FT dbSNP:rs145975461)"
FT /evidence="ECO:0000269|PubMed:11967537,
FT ECO:0000269|PubMed:15629135"
FT /id="VAR_017325"
FT CONFLICT 126
FT /note="L -> V (in Ref. 2; AAB64299)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="V -> F (in Ref. 7; AAH00026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 278 AA; 30914 MW; 1E58F537F703BE9F CRC64;
MELWPCLAAA LLLLLLLVQL SRAAEFYAKV ALYCALCFTV SAVASLVCLL RHGGRTVENM
SIIGWFVRSF KYFYGLRFEV RDPRRLQEAR PCVIVSNHQS ILDMMGLMEV LPERCVQIAK
RELLFLGPVG LIMYLGGVFF INRQRSSTAM TVMADLGERM VRENLKVWIY PEGTRNDNGD
LLPFKKGAFY LAVQAQVPIV PVVYSSFSSF YNTKKKFFTS GTVTVQVLEA IPTSGLTAAD
VPALVDTCHR AMRTTFLHIS KTPQENGATA GSGVQPAQ
