Reviewed, UniProtKB/Swiss-Prot Q8K2C8 (GPAT4_MOUSE)

Names and origin

Protein names

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

Gene names

Name:	Agpat6
Synonyms:	Gpat4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

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 By similarity. Ref.4
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; Multi-pass membrane protein By similarity.
Domain	The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity.
Sequence similarities	Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Signal Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	diacylglycerol metabolic process Inferred from mutant phenotype. Source: MGI glandular epithelial cell maturation Inferred from mutant phenotype. Source: MGI lactation Inferred from mutant phenotype. Source: UniProtKB regulation of multicellular organism growth Inferred from mutant phenotype. Source: MGI triglyceride biosynthetic process Inferred from mutant phenotype. Source: UniProtKB
Cellular component	integral to endoplasmic reticulum membrane Non-traceable author statement. Source: UniProtKB
Molecular function	acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity Non-traceable author statement. Source: UniProtKB glycerol-3-phosphate O-acyltransferase activity Ref.4 Inferred from mutant phenotype. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Potential
	Chain	38 – 456	419	Glycerol-3-phosphate acyltransferase 4		PRO_0000024704
Regions
	Transmembrane	156 – 176	21	Potential
	Transmembrane	180 – 200	21	Potential
	Motif	248 – 253	6	HXXXXD motif
Amino acid modifications
	Modified residue	218	1	Phosphotyrosine By similarity
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
	Glycosylation	328	1	N-linked (GlcNAc...) Potential
	Glycosylation	362	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8K2C8-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 2C3E1C37044C14FA	FASTA	456	52,181
	10 20 30 40 50 60 MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKTL LKIFAWATLR 70 80 90 100 110 120 MERGAKERNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDKTPEF ELSDIFYFCR 130 140 150 160 170 180 KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TILWGLGVLI RYCFLLPLRI 190 200 210 220 230 240 ALAFTGIGLL VVGTTMVGYL PNGRFKEFLS KHVHLMCYRI CVRALTAIIT YHNRKNRPRN 250 260 270 280 290 300 GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL 310 320 330 340 350 360 VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF 370 380 390 400 410 420 WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREKDEDAV QFANRVKSAI ARQGGLVDLL 430 440 450 WDGGLKREKV KDTFKEEQQK LYSKMIVGNH EDRSRS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel gene encodes a product of putative lysophosphatidic acid acyltransferase." Guo J.H., Dai F.Y., Yu L. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II.
[2]	"The transcriptional landscape of the mammalian genome." 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. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart and Testis.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
[4]	"AGPAT6 is a novel microsomal glycerol-3-phosphate acyltransferase." 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. J. Biol. Chem. 283:10048-10057(2008) [PubMed: 18238778] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF406611 mRNA. Translation: AAP97283.1. AK045235 mRNA. Translation: BAC32273.1. AK077561 mRNA. Translation: BAC36864.1. AK083589 mRNA. Translation: BAC38962.1. AK161270 mRNA. Translation: BAE36282.1. AK169257 mRNA. Translation: BAE41020.1. BC031767 mRNA. Translation: AAH31767.1.
IPI	IPI00322144.
RefSeq	NP_061213.2.
UniGene	Mm.200898
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8K2C8.
Proteomic databases
PRIDE	Q8K2C8.
Genome annotation databases
Ensembl	ENSMUST00000033949; ENSMUSP00000033949; ENSMUSG00000031545; Mus musculus. [Genome view]
GeneID	102247.
KEGG	mmu:102247.
UCSC	uc009leo.1. mouse.
Organism-specific databases
CTD	102247.
MGI	MGI:2142716. Agpat6.
Phylogenomic databases
HOGENOM	HBG408354.
HOVERGEN	Q8K2C8.
InParanoid	Q8K2C8.
OMA	FLSKHVH.
OrthoDB	EOG9PK4V7.
PhylomeDB	Q8K2C8.
Enzyme and pathway databases
BRENDA	2.3.1.51. 244.
Gene expression databases
ArrayExpress	Q8K2C8.
Bgee	Q8K2C8.
Genevestigator	Q8K2C8.
GermOnline	ENSMUSG00000031545. Mus musculus.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	355374.
SOURCE	Search...

Entry information

Entry name

GPAT4_MOUSE

Accession

Primary (citable) accession number: Q8K2C8
Secondary accession number(s): Q3TF78

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	October 1, 2002
Last modified:	January 19, 2010
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)