ID A0JMM2_DANRE Unreviewed; 271 AA. AC A0JMM2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 03-AUG-2022, entry version 100. 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 OrderedLocusNames=agpat2 {ECO:0000313|EMBL:AAI25930.1, GN ECO:0000313|Ensembl:ENSDARP00000131892, GN ECO:0000313|ZFIN:ZDB-GENE-061103-541}; GN ORFNames=SO:0001217 {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|Ensembl:ENSDARP00000131892} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131892}; RX PubMed=23594743; DOI=10.1038/nature12111; 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., Threadgold G., RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P., RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N., RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J., RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J., RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D., RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S., RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E., RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A., RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J., RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E., RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C., RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C., RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M., RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F., RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M., RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M., RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C., RA Hubbard T.J., Roest Crollius H., 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 [3] {ECO:0000313|Ensembl:ENSDARP00000131892} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131892}; RG Ensembl; RL Submitted (NOV-2015) 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 -!- 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 ZFIN; ZDB-GENE-061103-541; SO:0001217. DR eggNOG; KOG2848; Eukaryota. DR GeneTree; ENSGT00390000008726; -. DR HOGENOM; CLU_027938_10_1_1; -. DR OMA; MPRPLCY; -. DR OrthoDB; 1623097at2759; -. DR TreeFam; TF314867; -. DR Reactome; R-DRE-1483166; Synthesis of PA. DR Reactome; R-DRE-163765; ChREBP activates metabolic gene expression. DR Proteomes; UP000814640; 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:0016021; C:integral component of 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 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 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 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="PlsC" 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 //