ID Q66J26_XENLA Unreviewed; 273 AA. AC Q66J26; DT 11-OCT-2004, integrated into UniProtKB/TrEMBL. DT 11-OCT-2004, sequence version 1. DT 11-DEC-2019, entry version 60. 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=agpat1 {ECO:0000313|Xenbase:XB-GENE-865749}; GN Synonyms=MGC82195 {ECO:0000313|EMBL:AAH81085.1}; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH81085.1}; RN [1] {ECO:0000313|EMBL:AAH81085.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo {ECO:0000313|EMBL:AAH81085.1}; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. 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|RuleBase:RU361267}; 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|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; BC081085; AAH81085.1; -; mRNA. DR RefSeq; NP_001087689.1; NM_001094220.1. DR GeneID; 447513; -. DR KEGG; xla:447513; -. DR CTD; 447513; -. DR Xenbase; XB-GENE-865749; agpat1. DR KO; K13509; -. DR OrthoDB; 1623097at2759; -. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferase activity; ISS:UniProtKB. 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 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}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 34..53 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 124..142 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 93..208 FT /note="PlsC" FT /evidence="ECO:0000259|SMART:SM00563" SQ SEQUENCE 273 AA; 30846 MW; 18932F439412F030 CRC64; MELSVAQWLL VVCLVAFPLL YEWSVSFKYF CKMAFYNGWI LTLAILAIPI CAVRGRNVEN MKVLQFMLLH IKYLYGIKIE VRGWENFNIK EPYVVVSNHQ SSLDLLGMME ILPSRCVPIA KRELMYAGTA GLACWLAGVI FINRKKTDDA ISVMTEAADT MLKEDVRVWV FPEGTRNHSG SLLPFKRGAF HLAVQAQVPV IPVVMSSYKD FYCKKEKKFT TGKCTVRILP GVHTKGLSSD DVPELADRVR DMMIEAFTQI SSERPGKGPG VMH //