ID   PLCB_MOUSE              Reviewed;         278 AA.
AC   Q8K3K7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 46.
DE   RecName: Full=1-acyl-sn-glycerol-3-phosphate acyltransferase beta;
DE            EC=2.3.1.51;
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 2;
DE            Short=1-AGP acyltransferase 2;
DE            Short=1-AGPAT 2;
DE   AltName: Full=Lysophosphatidic acid acyltransferase beta;
DE            Short=LPAAT-beta;
GN   Name=Agpat2;
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 [MRNA].
RC   STRAIN=BALB/c; TISSUE=Liver;
RX   MEDLINE=21980204; PubMed=11967537; DOI=10.1038/ng880;
RA   Agarwal A.K., Arioglu E., de Almeida S., Akkoc N., Taylor S.I.,
RA   Bowcock A.M., Barnes R.I., Garg A.;
RT   "AGPAT2 is mutated in congenital generalized lipodystrophy linked to
RT   chromosome 9q34.";
RL   Nat. Genet. 31:21-23(2002).
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-260, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=17203969; DOI=10.1021/pr0604155;
RA   Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
RT   "Protein phosphorylation and expression profiling by Yin-yang
RT   multidimensional liquid chromatography (Yin-yang MDLC) mass
RT   spectrometry.";
RL   J. Proteome Res. 6:250-262(2007).
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.
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; AY072769; AAL62337.1; -; mRNA.
DR   IPI; IPI00170100; -.
DR   RefSeq; NP_080488.1; -.
DR   UniGene; Mm.24244; -.
DR   PhosphoSite; Q8K3K7; -.
DR   Ensembl; ENSMUSG00000026922; Mus musculus.
DR   GeneID; 67512; -.
DR   KEGG; mmu:67512; -.
DR   MGI; MGI:1914762; Agpat2.
DR   HOGENOM; Q8K3K7; -.
DR   HOVERGEN; Q8K3K7; -.
DR   OMA; Q8K3K7; EGTRNDN.
DR   BRENDA; 2.3.1.51; 244.
DR   NextBio; 324790; -.
DR   Bgee; Q8K3K7; -.
DR   GermOnline; ENSMUSG00000026922; Mus musculus.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003841; F:1-acylglycerol-3-phosphate O-acyltransferas...; IDA:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; NAS:UniProtKB.
DR   InterPro; IPR002123; Acyltransferase.
DR   InterPro; IPR004552; AGP_acyltrans.
DR   Pfam; PF01553; Acyltransferase; 1.
DR   SMART; SM00563; PlsC; 1.
DR   TIGRFAMs; TIGR00530; AGP_acyltrn; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Membrane; Phospholipid biosynthesis; Phosphoprotein;
KW   Transferase; Transmembrane.
FT   CHAIN         1    278       1-acyl-sn-glycerol-3-phosphate
FT                                acyltransferase beta.
FT                                /FTId=PRO_0000208193.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     30     50       Potential.
FT   TRANSMEM    122    142       Potential.
FT   MOTIF        98    103       HXXXXD motif.
FT   MOD_RES     255    255       Phosphothreonine.
FT   MOD_RES     260    260       Phosphoserine.
SQ   SEQUENCE   278 AA;  31011 MW;  57A54BFB1A0EFF56 CRC64;
     MDPWPWLTAA LLLLLLLVQL SRTARFYAKV GLYCVLCLSF SAAASIVCLL RHGGRTVDNM
     SIISWFVRSF KYVYGLRFEV SGQKKLEVDG PCVIISNHQS ILDMMGLMEI LPKRCVQIAK
     RELMFTGPVG LIMYLGGVYF INRQQARTAM SVMADLGDLM VKENLKVWIY PEGTRNDNGD
     LLPFKKGAFY LAIQAQVPII PVVYSSFSSF YNVKTKLFTS GTIKVQVLDA VPTNGLTDAD
     VTKLVDTCYQ SMRATFLQIS QIPQENSAIK EPGVLPAQ
//