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Database: UniProt
Entry: A0A1L8F126_XENLA
LinkDB: A0A1L8F126_XENLA
Original site: A0A1L8F126_XENLA 
ID   A0A1L8F126_XENLA        Unreviewed;       276 AA.
AC   A0A1L8F126;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   16-JAN-2019, entry version 10.
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|Xenbase:XB-GENE-17337489};
GN   ORFNames=XELAEV_18041540mg {ECO:0000313|EMBL:OCT65301.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:OCT65301.1, ECO:0000313|Proteomes:UP000186698};
RN   [1] {ECO:0000313|Proteomes:UP000186698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J {ECO:0000313|Proteomes:UP000186698};
RX   PubMed=27762356; DOI=10.1038/nature19840;
RA   Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA   Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J.,
RA   Quigley I., Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B.,
RA   Simakov O., Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T.,
RA   Watanabe M., Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S.,
RA   van Kruijsbergen I., Shu S., Carlson J., Kinoshita T., Ohta Y.,
RA   Mawaribuchi S., Jenkins J., Grimwood J., Schmutz J., Mitros T.,
RA   Mozaffari S.V., Suzuki Y., Haramoto Y., Yamamoto T.S., Takagi C.,
RA   Heald R., Miller K., Haudenschild C., Kitzman J., Nakayama T.,
RA   Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V., Karimi K.,
RA   Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W., Shendure J.,
RA   DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA   Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y.,
RA   Veenstra G.J., Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT   "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL   Nature 538:336-343(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1-acyl-sn-glycero-3-phosphate + an acyl-CoA = a 1,2-
CC         diacyl-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
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}.
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DR   EMBL; CM004481; OCT65301.1; -; Genomic_DNA.
DR   RefSeq; XP_018088072.1; XM_018232583.1.
DR   GeneID; 108699908; -.
DR   KEGG; xla:108699908; -.
DR   CTD; 108699908; -.
DR   Xenbase; XB-GENE-17337489; agpat2.
DR   KO; K13509; -.
DR   OrthoDB; 1623097at2759; -.
DR   Proteomes; UP000186698; Chromosome 8s.
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: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   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361267};
KW   Complete proteome {ECO:0000313|Proteomes:UP000186698};
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:UP000186698};
KW   Transferase {ECO:0000256|RuleBase:RU361267};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM      5     26       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     32     52       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    125    143       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN       94    209       PlsC. {ECO:0000259|SMART:SM00563}.
SQ   SEQUENCE   276 AA;  31231 MW;  5A95E42E7122F783 CRC64;
     MDLGWLLWTF LLLLLPFIIM EISSTFKFHF KITSYCALCL LLSALAAPMC LLRNGGRTVE
     NMRIISRVVR TLKYFFGIRF EVRGLENFQI DGPCVIISNH QSILDMMGLM EILPDRCVQI
     AKKELMYAGS VGLITYLGGV IYINRNRTSD AKSIMAAVAE AMISDNLKVW VYPEGTRNNS
     GDLLPFKKGA FHLALQAQVP IIPVVYSSFT SFYNQKKNLF TGGTIKVEIL PKIDTSDLSE
     KDIADLTERC HQTMRQVFFR LSNKPYEANE QSNCGQ
//
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