ID F8WGD9_MOUSE Unreviewed; 291 AA. AC F8WGD9; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-MAR-2024, entry version 70. DE SubName: Full=1-acylglycerol-3-phosphate O-acyltransferase 5 (lysophosphatidic acid acyltransferase, epsilon) {ECO:0000313|Ensembl:ENSMUSP00000033847.5}; GN Name=Agpat5 {ECO:0000313|Ensembl:ENSMUSP00000033847.5, GN ECO:0000313|MGI:MGI:1196345}; 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:ENSMUSP00000033847.5, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000033847.5, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000033847.5, 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:0000313|Ensembl:ENSMUSP00000033847.5} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000033847.5}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate CC acyltransferase family. {ECO:0000256|ARBA:ARBA00008655}. 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 AlphaFoldDB; F8WGD9; -. DR MaxQB; F8WGD9; -. DR PeptideAtlas; F8WGD9; -. DR ProteomicsDB; 303903; -. DR Antibodypedia; 2138; 360 antibodies from 27 providers. DR Ensembl; ENSMUST00000033847.5; ENSMUSP00000033847.5; ENSMUSG00000031467.11. DR AGR; MGI:1196345; -. DR MGI; MGI:1196345; Agpat5. DR VEuPathDB; HostDB:ENSMUSG00000031467; -. DR GeneTree; ENSGT00950000182836; -. DR HOGENOM; CLU_041844_2_0_1; -. DR OMA; CPRIHIH; -. DR ChiTaRS; Agpat5; mouse. DR Proteomes; UP000000589; Chromosome 8. DR Bgee; ENSMUSG00000031467; Expressed in triceps brachii and 270 other cell types or tissues. DR ExpressionAtlas; F8WGD9; baseline and differential. DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW. DR CDD; cd07990; LPLAT_LCLAT1-like; 1. DR InterPro; IPR032098; Acyltransf_C. DR InterPro; IPR002123; Plipid/glycerol_acylTrfase. DR PANTHER; PTHR10983:SF76; 1-ACYL-SN-GLYCEROL-3-PHOSPHATE ACYLTRANSFERASE EPSILON; 1. DR PANTHER; PTHR10983; 1-ACYLGLYCEROL-3-PHOSPHATE ACYLTRANSFERASE-RELATED; 1. DR Pfam; PF16076; Acyltransf_C; 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|ARBA:ARBA00023315}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264}; KW Proteomics identification {ECO:0007829|EPD:F8WGD9, KW ECO:0007829|MaxQB:F8WGD9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 87..212 FT /note="Phospholipid/glycerol acyltransferase" FT /evidence="ECO:0000259|SMART:SM00563" SQ SEQUENCE 291 AA; 33845 MW; E221CD0742495A8D CRC64; MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV DDRLYCVYQN MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI VADMLAARQD ALGHVRYVLK DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT YTKLLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG KYSNPPSMTE FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD R //