ID A0JMM2_DANRE Unreviewed; 271 AA. AC A0JMM2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 12-SEP-2018, entry version 84. 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=agpat2 {ECO:0000313|EMBL:AAI25930.1, GN ECO:0000313|Ensembl:ENSDARP00000131892, 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 Cyprinidae; 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, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000131892, RC ECO:0000313|Proteomes:UP000000437}; RX PubMed=23594743; DOI=10.1038/nature12111; RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., RA Muffato M., Collins J.E., Humphray S., McLaren K., Matthews L., RA McLaren S., Sealy I., Caccamo M., Churcher C., Scott C., Barrett J.C., RA Koch R., Rauch G.J., White S., Chow W., Kilian B., Quintais L.T., RA Guerra-Assuncao J.A., Zhou Y., Gu Y., Yen J., Vogel J.H., Eyre T., RA Redmond S., Banerjee R., Chi J., Fu B., Langley E., Maguire S.F., RA Laird G.K., Lloyd D., Kenyon E., Donaldson S., Sehra H., RA 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., RA Clark S., Pelan S., Griffiths G., Smith M., Glithero R., Howden P., RA Barker N., Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., RA Lovell J., Beasley H., Henderson C., Gordon D., Auger K., Wright D., RA Collins J., Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., RA Leongamornlert D., McGuire S., Gilderthorp R., Griffiths C., RA Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M., Brown J., RA Murnane C., Gray E., Humphries M., Sycamore N., Barker D., RA Saunders D., Wallis J., Babbage A., Hammond S., RA Mashreghi-Mohammadi M., Barr L., Martin S., Wray P., Ellington A., RA 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., RA Bird C., Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., RA Eser C., Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., RA Konantz M., Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., RA Raddatz G., Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., RA Yang F., Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., RA Searle S.M., Enright A., Geisler R., Plasterk R.H., Lee C., RA Westerfield M., de Jong P.J., Zon L.I., Postlethwait J.H., RA Nusslein-Volhard C., Hubbard T.J., Roest Crollius H., Rogers J., RA Stemple D.L.; RT "The zebrafish reference genome sequence and its relationship to the RT human 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 -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CC CoA + 1,2-diacyl-sn-glycerol 3-phosphate. CC {ECO:0000256|RuleBase:RU361267}. 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. {ECO:0000256|RuleBase:RU361267}. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {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 UniGene; Dr.30677; -. DR STRING; 7955.ENSDARP00000089754; -. DR Ensembl; ENSDART00000172174; ENSDARP00000131892; ENSDARG00000101139. DR GeneID; 777624; -. DR KEGG; dre:777624; -. DR CTD; 10555; -. DR ZFIN; ZDB-GENE-061103-541; agpat2. DR eggNOG; KOG2848; Eukaryota. DR eggNOG; COG0204; LUCA. DR GeneTree; ENSGT00390000008726; -. DR HOGENOM; HOG000026375; -. DR HOVERGEN; HBG000676; -. DR KO; K13509; -. DR OMA; MPRPLCY; -. DR OrthoDB; EOG091G0ICC; -. 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 26 organ(s), highest expression level in intestine. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; IBA:GO_Central. DR GO; GO:0046474; P:glycerophospholipid 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 Complete proteome {ECO:0000313|Proteomes:UP000000437}; 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, KW ECO:0000313|EMBL:AAI25930.1}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 32 49 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 122 140 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 187 206 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 91 206 PlsC. {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 //