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Glycerol-3-phosphate acyltransferase 4 (GPAT4) (EC 2.3.1.15) (1-acylglycerol-3-phosphate O-acyltransferase 6) (1-AGP acyltransferase 6) (1-AGPAT 6) (Acyl-CoA:glycerol-3-phosphate acyltransferase 4) (Lysophosphatidic acid acyltransferase zeta) (LPAAT-zeta)

 GPAT4_MOUSE             Reviewed;         456 AA.
Q8K2C8; Q3TF78; Q5QHR4;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
10-OCT-2018, entry version 129.
RecName: Full=Glycerol-3-phosphate acyltransferase 4 {ECO:0000312|MGI:MGI:2142716};
Short=GPAT4;
EC=2.3.1.15;
AltName: Full=1-acylglycerol-3-phosphate O-acyltransferase 6;
Short=1-AGP acyltransferase 6;
Short=1-AGPAT 6;
AltName: Full=Acyl-CoA:glycerol-3-phosphate acyltransferase 4;
AltName: Full=Lysophosphatidic acid acyltransferase zeta;
Short=LPAAT-zeta;
AltName: Full=Testis spermatogenesis apoptosis-related protein 7 {ECO:0000303|PubMed:15944755};
Flags: Precursor;
Name=Gpat4 {ECO:0000312|MGI:MGI:2142716};
Synonyms=Agpat6, Tsarg7 {ECO:0000303|PubMed:15944755};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
Guo J.H., Dai F.Y., Yu L.;
"A novel gene encodes a product of putative lysophosphatidic acid
acyltransferase.";
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Heart, and Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-402, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ;
PubMed=15944755; DOI=10.1111/j.1745-7270.2005.00057.x;
Tan X.J., Xing X.W., Li L.Y., Wu Z.D., Zhong C.G., Nie D.S., Fu J.J.,
Xiang Y., Deng Y., Lu G.X.;
"Molecular cloning of a novel mouse testis-specific spermatogenic cell
apoptosis inhibitor gene mTSARG7 as a candidate oncogene.";
Acta Biochim. Biophys. Sin. 37:396-405(2005).
[5]
FUNCTION.
PubMed=18238778; DOI=10.1074/jbc.M708151200;
Chen Y.Q., Kuo M.-S., Li S., Bui H.H., Peake D.A., Sanders P.E.,
Thibodeaux S.J., Chu S., Qian Y.-W., Zhao Y., Bredt D.S., Moller D.E.,
Konrad R.J., Beigneux A.P., Young S.G., Cao G.;
"AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase.";
J. Biol. Chem. 283:10048-10057(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Esterifies acyl-group from acyl-ACP to the sn-1 position
of glycerol-3-phosphate, an essential step in glycerolipid
biosynthesis. Active against both saturated and unsaturated long-
chain fatty acyl-CoAs. {ECO:0000250|UniProtKB:Q86UL3,
ECO:0000269|PubMed:18238778}.
-!- CATALYTIC ACTIVITY: Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-
acyl-sn-glycerol 3-phosphate.
-!- PATHWAY: Phospholipid metabolism; CDP-diacylglycerol biosynthesis;
CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:Q86UL3}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:Q86UL3}.
-!- TISSUE SPECIFICITY: Highly expressed in testis.
{ECO:0000269|PubMed:15944755}.
-!- DOMAIN: The HXXXXD motif is essential for acyltransferase activity
and may constitute the binding site for the phosphate moiety of
the glycerol-3-phosphate. {ECO:0000250}.
-!- SIMILARITY: Belongs to the 1-acyl-sn-glycerol-3-phosphate
acyltransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AY489184; AAS75838.1; -; mRNA.
EMBL; AF406611; AAP97283.1; -; mRNA.
EMBL; AK045235; BAC32273.1; -; mRNA.
EMBL; AK077561; BAC36864.1; -; mRNA.
EMBL; AK083589; BAC38962.1; -; mRNA.
EMBL; AK161270; BAE36282.1; -; mRNA.
EMBL; AK169257; BAE41020.1; -; mRNA.
EMBL; BC031767; AAH31767.1; -; mRNA.
CCDS; CCDS22189.1; -.
RefSeq; NP_061213.2; NM_018743.4.
UniGene; Mm.200898; -.
UniGene; Mm.241152; -.
ProteinModelPortal; Q8K2C8; -.
STRING; 10090.ENSMUSP00000127325; -.
SwissLipids; SLP:000000104; -.
iPTMnet; Q8K2C8; -.
PhosphoSitePlus; Q8K2C8; -.
SwissPalm; Q8K2C8; -.
EPD; Q8K2C8; -.
MaxQB; Q8K2C8; -.
PaxDb; Q8K2C8; -.
PRIDE; Q8K2C8; -.
Ensembl; ENSMUST00000167004; ENSMUSP00000127325; ENSMUSG00000031545.
GeneID; 102247; -.
KEGG; mmu:102247; -.
UCSC; uc009leo.2; mouse.
CTD; 137964; -.
MGI; MGI:2142716; Gpat4.
eggNOG; KOG2898; Eukaryota.
eggNOG; COG0204; LUCA.
GeneTree; ENSGT00390000000536; -.
HOGENOM; HOG000265725; -.
HOVERGEN; HBG052874; -.
InParanoid; Q8K2C8; -.
KO; K13506; -.
OMA; KMLVGTQ; -.
OrthoDB; EOG091G04E8; -.
PhylomeDB; Q8K2C8; -.
TreeFam; TF315039; -.
BRENDA; 2.3.1.15; 3474.
Reactome; R-MMU-1483166; Synthesis of PA.
UniPathway; UPA00557; UER00612.
ChiTaRS; Gpat4; mouse.
PRO; PR:Q8K2C8; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031545; Expressed in 271 organ(s), highest expression level in testis.
ExpressionAtlas; Q8K2C8; baseline and differential.
Genevisible; Q8K2C8; MM.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; NAS:UniProtKB.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0004366; F:glycerol-3-phosphate O-acyltransferase activity; IMP:UniProtKB.
GO; GO:0102420; F:sn-1-glycerol-3-phosphate C16:0-DCA-CoA acyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0006637; P:acyl-CoA metabolic process; ISO:MGI.
GO; GO:0016024; P:CDP-diacylglycerol biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0046339; P:diacylglycerol metabolic process; IMP:MGI.
GO; GO:0006631; P:fatty acid metabolic process; IMP:MGI.
GO; GO:0002071; P:glandular epithelial cell maturation; IMP:MGI.
GO; GO:0007595; P:lactation; IMP:UniProtKB.
GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
GO; GO:0030879; P:mammary gland development; IMP:MGI.
GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISO:MGI.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:MGI.
GO; GO:0019432; P:triglyceride biosynthetic process; IMP:UniProtKB.
GO; GO:0006641; P:triglyceride metabolic process; IMP:MGI.
InterPro; IPR002123; Plipid/glycerol_acylTrfase.
Pfam; PF01553; Acyltransferase; 1.
SMART; SM00563; PlsC; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Endoplasmic reticulum;
Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane;
Phospholipid biosynthesis; Phospholipid metabolism;
Reference proteome; Signal; Transferase; Transmembrane;
Transmembrane helix.
SIGNAL 1 37 {ECO:0000255}.
CHAIN 38 456 Glycerol-3-phosphate acyltransferase 4.
/FTId=PRO_0000024704.
TRANSMEM 156 176 Helical. {ECO:0000255}.
TRANSMEM 180 200 Helical. {ECO:0000255}.
MOTIF 248 253 HXXXXD motif.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 327 327 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 362 362 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 119 119 C -> G (in Ref. 4; AAS75838).
{ECO:0000305}.
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


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