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Database: UniProt
Entry: A0A0R4J263_MOUSE
LinkDB: A0A0R4J263_MOUSE
Original site: A0A0R4J263_MOUSE 
ID   A0A0R4J263_MOUSE        Unreviewed;       285 AA.
AC   A0A0R4J263;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 47.
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|Ensembl:ENSMUSP00000134358.2,
GN   ECO:0000313|MGI:MGI:1932075};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000134358.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0000313|Ensembl:ENSMUSP00000134358.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000134358.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000134358.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000134358.2};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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:0000256|ARBA:ARBA00004086}.
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:0000256|ARBA:ARBA00000091};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37604;
CC         Evidence={ECO:0000256|ARBA:ARBA00000091};
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:0000256|ARBA:ARBA00000191};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37180;
CC         Evidence={ECO:0000256|ARBA:ARBA00000191};
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:0000256|ARBA:ARBA00001322};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37140;
CC         Evidence={ECO:0000256|ARBA:ARBA00001322};
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:0000256|ARBA:ARBA00000045};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37132;
CC         Evidence={ECO:0000256|ARBA:ARBA00000045};
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:0000256|ARBA:ARBA00000892};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37184;
CC         Evidence={ECO:0000256|ARBA:ARBA00000892};
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:0000256|ARBA:ARBA00001203};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001203};
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:0000256|ARBA:ARBA00001392};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37188;
CC         Evidence={ECO:0000256|ARBA:ARBA00001392};
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:0000256|ARBA:ARBA00001109};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37160;
CC         Evidence={ECO:0000256|ARBA:ARBA00001109};
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:0000256|ARBA:ARBA00001467};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37156;
CC         Evidence={ECO:0000256|ARBA:ARBA00001467};
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:0000256|ARBA:ARBA00000816};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37144;
CC         Evidence={ECO:0000256|ARBA:ARBA00000816};
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:0000256|ARBA:ARBA00001880};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37176;
CC         Evidence={ECO:0000256|ARBA:ARBA00001880};
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:0000256|ARBA:ARBA00001783};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:37172;
CC         Evidence={ECO:0000256|ARBA:ARBA00001783};
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|ARBA:ARBA00000300};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19710;
CC         Evidence={ECO:0000256|ARBA:ARBA00000300};
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   RefSeq; NP_001156851.1; NM_001163379.1.
DR   RefSeq; NP_061350.3; NM_018862.3.
DR   RefSeq; XP_006524710.1; XM_006524647.2.
DR   RefSeq; XP_006524711.1; XM_006524648.1.
DR   SMR; A0A0R4J263; -.
DR   ProteomicsDB; 330675; -.
DR   Antibodypedia; 28453; 165 antibodies from 21 providers.
DR   DNASU; 55979; -.
DR   Ensembl; ENSMUST00000037489.15; ENSMUSP00000048573.9; ENSMUSG00000034254.18.
DR   Ensembl; ENSMUST00000114140.10; ENSMUSP00000109776.4; ENSMUSG00000034254.18.
DR   Ensembl; ENSMUST00000174595.2; ENSMUSP00000134358.2; ENSMUSG00000034254.18.
DR   GeneID; 55979; -.
DR   KEGG; mmu:55979; -.
DR   AGR; MGI:1932075; -.
DR   CTD; 10554; -.
DR   MGI; MGI:1932075; Agpat1.
DR   VEuPathDB; HostDB:ENSMUSG00000034254; -.
DR   GeneTree; ENSGT00390000008726; -.
DR   OMA; KKSLVWI; -.
DR   OrthoDB; 209232at2759; -.
DR   BioGRID-ORCS; 55979; 2 hits in 81 CRISPR screens.
DR   ChiTaRS; Agpat1; mouse.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000034254; Expressed in spermatid and 227 other cell types or tissues.
DR   ExpressionAtlas; A0A0R4J263; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IEA:Ensembl.
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 ALPHA; 1.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267};
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   Proteomics identification {ECO:0007829|EPD:A0A0R4J263,
KW   ECO:0007829|MaxQB:A0A0R4J263};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|RuleBase:RU361267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          95..210
FT                   /note="Phospholipid/glycerol acyltransferase"
FT                   /evidence="ECO:0000259|SMART:SM00563"
SQ   SEQUENCE   285 AA;  31737 MW;  035E4AA2DF298741 CRC64;
     MELWPGAWTA LLLLLLLLLS TLWFCSSSAK YFFKMAFYNG WILFLAILAI PVCAVRGRNV
     ENMKILRLLL LHVKYLYGIR VEVRGAHHFP PTQPYVVVSN HQSSLDLLGM MEVLPDRCVP
     IAKRELLWAG SAGLACWLAG IIFIDRKRTG DAISVMSEVA QTLLTQDVRV WVFPEGTRNH
     NGSMLPFKRG AFHLAVQAQV PIIPIVMSSY QDFYSKKERR FTSPGRCQVR VLPPVSTEGL
     TPDDVPALAD SVRHSMLTIF REISTDGLGG GDCLKKPGGA GEARL
//
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