ID   GPAT3_CHICK             Reviewed;         446 AA.
AC   Q5ZLL8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   16-JUN-2009, entry version 33.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 3;
DE            Short=GPAT3;
DE            EC=2.3.1.15;
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 9;
DE            Short=1-AGP acyltransferase 9;
DE            Short=1-AGPAT 9;
DE   AltName: Full=Lysophosphatidic acid acyltransferase theta;
DE            Short=LPAAT-theta;
GN   Name=AGPAT9; Synonyms=GPAT3; ORFNames=RCJMB04_5j9;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
RA   Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
RA   Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:RESEARCH006.1-RESEARCH006.9(2005).
CC   -!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position
CC       of glycerol-3-phosphate, an essential step in glycerolipid
CC       biosynthesis (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC       acyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein (By similarity).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
CC       acyltransferase family.
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DR   EMBL; AJ719716; CAG31375.1; -; mRNA.
DR   IPI; IPI00587916; -.
DR   RefSeq; NP_001026316.1; -.
DR   UniGene; Gga.16404; -.
DR   Ensembl; ENSGALG00000011221; Gallus gallus.
DR   GeneID; 422610; -.
DR   KEGG; gga:422610; -.
DR   HOGENOM; Q5ZLL8; -.
DR   HOVERGEN; Q5ZLL8; -.
DR   BRENDA; 2.3.1.51; 4.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase acti...; ISS:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Endoplasmic reticulum; Membrane;
KW   Phospholipid biosynthesis; Transferase; Transmembrane.
FT   CHAIN         1    446       Glycerol-3-phosphate acyltransferase 3.
FT                                /FTId=PRO_0000291573.
FT   TRANSMEM     25     45       Potential.
FT   TRANSMEM    142    162       Potential.
FT   TRANSMEM    164    184       Potential.
FT   TRANSMEM    352    372       Potential.
FT   MOTIF       232    237       HXXXXD motif.
SQ   SEQUENCE   446 AA;  50112 MW;  EE0DCF6D77C3DB6B CRC64;
     MEELGSLAVW LGAAWLSLVF ALIVLPSALG VSLGISEAYM WVLVKTLEWA TIRIEKGVKK
     PQPQMLKIPA ANGIIERDET PMEKEIAGLH RMEFRFSDIF YFCRKGFEAI VEDEVTQRFS
     SEELVSWNLL TRTNVNFHYV SLRLTVVWVI GVIVRYCFLL PLRFTLAAIG ITSMIVGTTV
     VGQLPNGSLK NYLSEVVHLT CSRILVRALS GTIHYHNKEN KPQKGGICVA NHTSPIDAII
     LTNDGCYAMV GQVHGGLMGV IQRATVKACP HVWFERSEIK DRHLVTKRLR EHVADKNKLP
     ILIFPEGTCI NNTSVMMFKK GSFEIGGTIY PVAIKYDPQF GDAFWNSSKY NIVSYLLRIM
     TSWAIVCHVW YMPPMVRKEG EDAVQFANRV RSAIARQGGL TELPWDGGLK RAKVKDSFKE
     EQQKNYSKML VRNGSQGNLP AGTESD
//