ID A0JMM2_DANRE Unreviewed; 271 AA. AC A0JMM2; DT 12-DEC-2006, integrated into UniProtKB/TrEMBL. DT 12-DEC-2006, sequence version 1. DT 29-APR-2015, entry version 58. 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:ENSDARP00000089754, 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, ECO:0000313|Proteomes:UP000000437}; 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:ENSDARP00000089754} RP IDENTIFICATION. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000089754}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. RN [3] {ECO:0000313|Ensembl:ENSDARP00000089754, ECO:0000313|Proteomes:UP000000437} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000089754, 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., Eliott D., Threadgold G., RA Harden G., Ware D., Mortimer B., Kerry G., Heath P., Phillimore B., RA Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S., Pelan S., RA Griffiths G., Smith M., Glithero R., Howden P., Barker N., Stevens C., RA Harley J., Holt K., Panagiotidis G., Lovell J., Beasley H., RA Henderson C., Gordon D., Auger K., Wright D., Collins J., Raisen C., RA 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., RA Babbage A., Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., RA Wray P., Ellington A., Matthews N., Ellwood M., Woodmansey R., RA Clark G., Cooper J., Tromans A., Grafham D., Skuce C., Pandian R., RA Andrews R., Harrison E., Kimberley A., Garnett J., Fosker N., Hall R., RA Garner P., Kelly D., Bird C., Palmer S., Gehring I., Berger A., RA 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., Osoegawa K., Zhu B., Rapp A., Widaa S., RA Langford C., Yang F., 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). 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; ENSDART00000098983; ENSDARP00000089754; ENSDARG00000068437. DR GeneID; 777624; -. DR KEGG; dre:777624; -. DR CTD; 10555; -. DR ZFIN; ZDB-GENE-061103-541; agpat2. DR eggNOG; COG0204; -. DR GeneTree; ENSGT00390000008726; -. DR HOGENOM; HOG000026375; -. DR HOVERGEN; HBG000676; -. DR KO; K13509; -. DR OMA; CWLGGIV; -. DR OrthoDB; EOG780RNF; -. DR TreeFam; TF314867; -. DR Reactome; REACT_317406; Triglyceride Biosynthesis. DR Reactome; REACT_338865; Synthesis of PA. DR NextBio; 20924239; -. DR PRO; PR:A0JMM2; -. DR Proteomes; UP000000437; Chromosome 11. DR GO; GO:0016020; C:membrane; IEA:InterPro. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. 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 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}. 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 //