ID   PLCD_MOUSE              Reviewed;         378 AA.
AC   Q8K4X7; Q3TKN0; Q9DB84;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase delta;
DE            EC=2.3.1.51;
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 4;
DE            Short=1-AGP acyltransferase 4;
DE            Short=1-AGPAT 4;
DE   AltName: Full=Lysophosphatidic acid acyltransferase delta;
DE            Short=LPAAT-delta;
GN   Name=Agpat4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RA   Brathwaite M.E., Waeltz P., Qian Y., Dudekula D., Schlessinger D.,
RA   Nagaraja R.;
RT   "Genomic sequence analysis in the mouse T-complex region.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic
CC       acid by incorporating an acyl moiety at the sn-2 position of the
CC       glycerol backbone (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate =
CC       CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
CC   -!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CC       CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein
CC       (Potential).
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; AK005139; BAB23837.2; -; mRNA.
DR   EMBL; AK166917; BAE39115.1; -; mRNA.
DR   EMBL; AF485269; AAM33375.1; -; Genomic_DNA.
DR   EMBL; BC047281; AAH47281.1; -; mRNA.
DR   IPI; IPI00173168; -.
DR   RefSeq; NP_080920.2; -.
DR   UniGene; Mm.258300; -.
DR   IntAct; Q8K4X7; 1.
DR   PRIDE; Q8K4X7; -.
DR   Ensembl; ENSMUSG00000023827; Mus musculus.
DR   GeneID; 68262; -.
DR   KEGG; mmu:68262; -.
DR   MGI; MGI:1915512; Agpat4.
DR   HOGENOM; Q8K4X7; -.
DR   HOVERGEN; Q8K4X7; -.
DR   OMA; Q8K4X7; LVNWLFW.
DR   BRENDA; 2.3.1.51; 244.
DR   NextBio; 326850; -.
DR   ArrayExpress; Q8K4X7; -.
DR   Bgee; Q8K4X7; -.
DR   GermOnline; ENSMUSG00000023827; Mus musculus.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IEA:EC.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002123; Acyltransferase.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
PE   2: Evidence at transcript level;
KW   Acyltransferase; Membrane; Phospholipid biosynthesis; Transferase;
KW   Transmembrane.
FT   CHAIN         1    378       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase delta.
FT                                /FTId=PRO_0000208198.
FT   TRANSMEM     11     31       Potential.
FT   TRANSMEM    125    145       Potential.
FT   TRANSMEM    311    331       Potential.
FT   TRANSMEM    338    358       Potential.
FT   MOTIF        96    101       HXXXXD motif.
SQ   SEQUENCE   378 AA;  43810 MW;  3D9EF15B6A5E49BC CRC64;
     MDLIGLLKSQ FLCHLVFCYV FIASGLIVNA IQLCTLVIWP INKQLFRKIN ARLCYCVSSQ
     LVMLLEWWSG TECTIYTDPK ACPHYGKENA IVVLNHKFEI DFLCGWSLAE RLGILGNSKV
     LAKKELAYVP IIGWMWYFVE MIFCTRKWEQ DRQTVAKSLL HLRDYPEKYL FLIHCEGTRF
     TEKKHQISMQ VAQAKGLPSL KHHLLPRTKG FAITVKCLRD VVPAVYDCTL NFRNNENPTL
     LGVLNGKKYH ADCYVRRIPM EDIPEDEDKC SAWLHKLYQE KDAFQEEYYR TGVFPETPWV
     PPRRPWSLVN WLFWASLLLY PFFQFLVSMV SSGSSVTLAS LVLIFCMASM GVRWMIGVTE
     IDKGSAYGNI DNKRKQTD
//