ID   GPAT4_MOUSE             Reviewed;         456 AA.
AC   Q8K2C8; Q3TF78;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   16-JUN-2009, entry version 57.
DE   RecName: Full=Glycerol-3-phosphate acyltransferase 4;
DE            Short=GPAT4;
DE            EC=2.3.1.15;
DE   AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 4;
DE   AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 6;
DE            Short=1-AGP acyltransferase 6;
DE            Short=1-AGPAT 6;
DE   AltName: Full=Lysophosphatidic acid acyltransferase zeta;
DE            Short=LPAAT-zeta;
DE   Flags: Precursor;
GN   Name=Agpat6; Synonyms=Gpat4;
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=Czech II;
RA   Guo J.H., Dai F.Y., Yu L.;
RT   "A novel gene encodes a product of putative lysophosphatidic acid
RT   acyltransferase.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
RN   [4]
RP   FUNCTION.
RX   PubMed=18238778; DOI=10.1074/jbc.M708151200;
RA   Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
RA   Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
RA   Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
RT   "AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
RL   J. Biol. Chem. 283:10048-10057(2008).
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. Active against both saturated and unsaturated long-
CC       chain fatty acyl-CoAs (By similarity).
CC   -!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
CC       acyl-sn-glycerol 3-phosphate.
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; AF406611; AAP97283.1; -; mRNA.
DR   EMBL; AK045235; BAC32273.1; -; mRNA.
DR   EMBL; AK077561; BAC36864.1; -; mRNA.
DR   EMBL; AK083589; BAC38962.1; -; mRNA.
DR   EMBL; AK161270; BAE36282.1; -; mRNA.
DR   EMBL; AK169257; BAE41020.1; -; mRNA.
DR   EMBL; BC031767; AAH31767.1; -; mRNA.
DR   IPI; IPI00322144; -.
DR   RefSeq; NP_061213.2; -.
DR   UniGene; Mm.200898; -.
DR   PRIDE; Q8K2C8; -.
DR   Ensembl; ENSMUSG00000031545; Mus musculus.
DR   GeneID; 102247; -.
DR   KEGG; mmu:102247; -.
DR   MGI; MGI:2142716; Agpat6.
DR   HOGENOM; Q8K2C8; -.
DR   HOVERGEN; Q8K2C8; -.
DR   OMA; Q8K2C8; YRICVRA.
DR   BRENDA; 2.3.1.51; 244.
DR   NextBio; 355374; -.
DR   ArrayExpress; Q8K2C8; -.
DR   Bgee; Q8K2C8; -.
DR   GermOnline; ENSMUSG00000031545; Mus musculus.
DR   GO; GO:0030176; C:integral to endoplasmic reticulum membrane; NAS:UniProtKB.
DR   GO; GO:0008780; F:acyl-[acyl-carrier-protein]-UDP-N-acetylglu...; NAS:UniProtKB.
DR   GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase acti...; IMP:UniProtKB.
DR   GO; GO:0046339; P:diacylglycerol metabolic process; IMP:MGI.
DR   GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
DR   GO; GO:0002071; P:glandular epithelial cell maturation; IMP:MGI.
DR   GO; GO:0007595; P:lactation; IMP:UniProtKB.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
DR   GO; GO:0019432; P:triglyceride biosynthetic process; IMP: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; Glycoprotein; Membrane;
KW   Phospholipid biosynthesis; Phosphoprotein; Signal; Transferase;
KW   Transmembrane.
FT   SIGNAL        1     37       Potential.
FT   CHAIN        38    456       Glycerol-3-phosphate acyltransferase 4.
FT                                /FTId=PRO_0000024704.
FT   TRANSMEM    156    176       Potential.
FT   TRANSMEM    180    200       Potential.
FT   MOTIF       248    253       HXXXXD motif (By similarity).
FT   MOD_RES     218    218       Phosphotyrosine (By similarity).
FT   CARBOHYD    247    247       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    327    327       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    328    328       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    362    362       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   456 AA;  52181 MW;  2C3E1C37044C14FA CRC64;
     MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKTL LKIFAWATLR
     MERGAKERNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDKTPEF ELSDIFYFCR
     KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TILWGLGVLI RYCFLLPLRI
     ALAFTGIGLL VVGTTMVGYL PNGRFKEFLS KHVHLMCYRI CVRALTAIIT YHNRKNRPRN
     GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL
     VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF
     WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREKDEDAV QFANRVKSAI ARQGGLVDLL
     WDGGLKREKV KDTFKEEQQK LYSKMIVGNH EDRSRS
//