ID A0JMM2_DANRE Unreviewed; 271 AA. AC A0JMM2; A0A8M1NAL6; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 13-SEP-2023, entry version 106. 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=zgc:153984 {ECO:0000313|RefSeq:NP_001071200.1}; GN OrderedLocusNames=agpat2 {ECO:0000313|Ensembl:ENSDARP00000131892, GN ECO:0000313|RefSeq:NP_001071200.1, GN ECO:0000313|ZFIN:ZDB-GENE-061103-541}; OS Danio rerio (Zebrafish) (Brachydanio rerio). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; OC Danionidae; Danioninae; Danio. OX NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI25930.1}; RN [1] {ECO:0000313|EMBL:AAI25930.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Whole {ECO:0000313|EMBL:AAI25930.1}; RG NIH - Zebrafish Gene Collection (ZGC) project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|RefSeq:NP_001071200.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21148433; RA Zou J., Li W.Q., Li Q., Li X.Q., Zhang J.T., Liu G.Q., Chen J., Qiu X.X., RA Tian F.J., Wang Z.Z., Zhu N., Qin Y.W., Shen B., Liu T.X., Jing Q.; RT "Two functional microRNA-126s repress a novel target gene p21-activated RT kinase 1 to regulate vascular integrity in zebrafish."; RL Circ. Res. 108:201-209(2011). RN [3] {ECO:0000313|RefSeq:NP_001071200.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23416188; RA Her G.M., Pai W.Y., Lai C.Y., Hsieh Y.W., Pang H.W.; RT "Ubiquitous transcription factor YY1 promotes zebrafish liver steatosis and RT lipotoxicity by inhibiting CHOP-10 expression."; RL Biochim. Biophys. Acta 1831:1037-1051(2013). RN [4] {ECO:0000313|Ensembl:ENSDARP00000131892, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131892}; RX PubMed=23594743; DOI=10.1038/nature12111; RG Genome Reference Consortium Zebrafish; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M., RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I., RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J., RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y., RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B., RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S., RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M., RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J., RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D., RA Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B., RA Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M., RA Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M., RA Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J., RA Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D., RA Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K., RA Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R., RA Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., RA Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M., RA Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M., RA Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D., RA Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J., RA Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I., RA Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M., RA Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M., RA Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B., RA Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P., RA Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R., RA Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I., RA Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., RA Rogers J., Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the human RT genome."; RL Nature 496:498-503(2013). RN [5] {ECO:0000313|Ensembl:ENSDARP00000131892} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131892}; RG Ensembl; RL Submitted (NOV-2015) to UniProtKB. RN [6] {ECO:0000313|RefSeq:NP_001071200.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28252024; RA Bayes A., Collins M.O., Reig-Viader R., Gou G., Goulding D., Izquierdo A., RA Choudhary J.S., Emes R.D., Grant S.G.; RT "Evolution of complexity in the zebrafish synapse proteome."; RL Nat. Commun. 8:14613-14613(2017). RN [7] {ECO:0000313|RefSeq:NP_001071200.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28217809; RA Fei F., Sun S.Y., Yao Y.X., Wang X.; RT "[Generation and phenotype analysis of zebrafish mutations of obesity- RT related genes lepr and mc4r]."; RL Sheng Li Xue Bao 69:61-69(2017). RN [8] {ECO:0000313|RefSeq:NP_001071200.1} RP IDENTIFICATION. RG RefSeq; RL Submitted (MAR-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}. 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; CU655841; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU855788; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CU929160; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC125929; AAI25930.1; -; mRNA. DR RefSeq; NP_001071200.1; NM_001077732.1. DR STRING; 7955.ENSDARP00000089754; -. DR Ensembl; ENSDART00000172174.3; ENSDARP00000131892.1; ENSDARG00000101139.3. DR GeneID; 777624; -. DR KEGG; dre:777624; -. DR CTD; 10555; -. DR ZFIN; ZDB-GENE-061103-541; agpat2. DR eggNOG; KOG2848; Eukaryota. DR HOGENOM; CLU_027938_10_1_1; -. DR OMA; AWMMFLA; -. DR OrthoDB; 209232at2759; -. DR TreeFam; TF314867; -. DR Reactome; R-DRE-1483166; Synthesis of PA. DR Reactome; R-DRE-6798695; Neutrophil degranulation. DR Proteomes; UP000000437; Chromosome 21. DR Bgee; ENSDARG00000101139; Expressed in intestine and 24 other tissues. DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IBA:GO_Central. DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IBA:GO_Central. 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:SF2; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE BETA; 1. DR Pfam; PF01553; Acyltransferase; 1. DR SMART; SM00563; PlsC; 1. DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1. PE 2: Evidence at transcript level; KW Acyltransferase {ECO:0000256|RuleBase:RU361267, KW ECO:0000313|EMBL:AAI25930.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000000437}; KW Transferase {ECO:0000256|RuleBase:RU361267, ECO:0000313|EMBL:AAI25930.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32..49 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 122..140 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 187..206 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 91..206 FT /note="Phospholipid/glycerol acyltransferase" FT /evidence="ECO:0000259|SMART:SM00563" SQ SEQUENCE 271 AA; 30510 MW; 8C88AABE2C5F1602 CRC64; MDAVWMLPVL LVLPLLLWTS STFVFYFKKC FYVAYMMLLA VIAIPICILK SGGRDIENMR VIRFLVRHVK YFLGLRYQVS GWEHLQTEGP YVIISNHQSS LDVLGMVEIL PDRCTMIAKK ELIWAGTVGM ICWLGGIVFI NRKKTSDAKN VMSDAAKTML TDKIRLWVFP EGTRNQNGGL LPFKKGAFHL AIQAQVPIIP IVFSSYSKFY LRKEKEFKSG TITLKVLPKI ETKGLTADDV TTLSDQAFGV MRSAFMEISG QSAQSNGPST H //