Q9D1E8 (PLCE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon
EC=2.3.1.51

Alternative name(s):
1-acylglycerol-3-phosphate O-acyltransferase 5
Short name=1-AGP acyltransferase 5
Short name=1-AGPAT 5
Lysophosphatidic acid acyltransferase epsilon
Short name=LPAAT-epsilon

Gene names

Name:	Agpat5
Synonyms:	D8Ertd319e

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Acts on LPA containing saturated or unsaturated fatty acids C15:0-C20:4 at the sn-1 position using C18:1-CoA as the acyl donor. Also acts on lysophosphatidylethanolamine using oleoyl-CoA, but not arachidonoyl-CoA, and lysophosphatidylinositol using arachidonoyl-CoA, but not oleoyl-CoA. Activity toward lysophosphatidylglycerol not detectable. Ref.4
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Nucleus envelope By similarity. Mitochondrion By similarity.
Tissue specificity	Widely expressed. Ref.4
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.
Caution	It is uncertain whether Met-1 or Met-12 is the initiator.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Nucleus
Domain	Transmembrane Transmembrane helix
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	CDP-diacylglycerol biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway acylglycerol metabolic process Inferred from direct assay Ref.4. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI nuclear envelope Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from direct assay Ref.4. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 365	365	1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon		PRO_0000208201
Regions
	Transmembrane	15 – 35	21	Helical; Potential
	Transmembrane	345 – 365	21	Helical; Potential
	Motif	93 – 98	6	HXXXXD motif
Experimental info
	Sequence conflict	80	1	L → W in AAN75571. Ref.1
	Sequence conflict	128	1	L → M in AAN75571. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9D1E8 [UniParc]. Last modified May 16, 2003. Version 2. Checksum: C13E14759610E19B	FASTA	365	42,202
	10 20 30 40 50 60 MLLSLVLHTY SMRYLLPSVL LLGSAPTYLL AWTLWRVLSA LMPARLYQRV DDRLYCVYQN 70 80 90 100 110 120 MVLFFFENYT GVQILLYGDL PKNKENVIYL ANHQSTVDWI VADMLAARQD ALGHVRYVLK 130 140 150 160 170 180 DKLKWLPLYG FYFAQHGGIY VKRSAKFNDK EMRSKLQSYV NAGTPMYLVI FPEGTRYNAT 190 200 210 220 230 240 YTKLLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDSMKS HLDAIYDVTV VYEGNEKGSG 250 260 270 280 290 300 KYSNPPSMTE FLCKQCPKLH IHFDRIDRNE VPEEQEHMKK WLHERFEIKD RLLIEFYDSP 310 320 330 340 350 360 DPERRNKFPG KSVHSRLSVK KTLPSVLILG SLTAVMLMTE SGRKLYMGTW LYGTLLGCLW FVIKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and characterization of 1-acylglycerolphosphate acyltransferase-epsilon." Lu B., Jiang Y.J., Chan M., Choy P.C. Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NMRI.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Bone marrow, Cerebellum, Dendritic cell, Embryo and Spleen.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary gland.
[4]	"Cloning and characterization of murine 1-acyl-sn-glycerol 3-phosphate acyltransferases and their regulation by PPARalpha in murine heart." Lu B., Jiang Y.J., Zhou Y., Xu F.Y., Hatch G.M., Choy P.C. Biochem. J. 385:469-477(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6J.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY161042 mRNA. Translation: AAN75571.1. AK003649 mRNA. Translation: BAB22915.2. AK082137 mRNA. Translation: BAC38421.1. AK089885 mRNA. Translation: BAC40983.1. AK152709 mRNA. Translation: BAE31436.1. AK152889 mRNA. Translation: BAE31572.1. AK155378 mRNA. Translation: BAE33229.1. BC031987 mRNA. Translation: AAH31987.2.
IPI	IPI00221486.
RefSeq	NP_081068.1. NM_026792.3.
UniGene	Mm.24117.
3D structure databases
ProteinModelPortal	Q9D1E8.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D1E8. 1 interaction.
STRING	10090.ENSMUSP00000117025.
PTM databases
PhosphoSite	Q9D1E8.
Proteomic databases
PaxDb	Q9D1E8.
PRIDE	Q9D1E8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000149565; ENSMUSP00000117025; ENSMUSG00000031467.
GeneID	52123.
KEGG	mmu:52123.
UCSC	uc009kzv.1. mouse.
Organism-specific databases
CTD	55326.
MGI	MGI:1196345. Agpat5.
Phylogenomic databases
eggNOG	COG0204.
GeneTree	ENSGT00530000062943.
HOGENOM	HOG000007801.
HOVERGEN	HBG039632.
InParanoid	Q9D1E8.
OMA	ADMLAIR.
OrthoDB	EOG4F7NK8.
Enzyme and pathway databases
UniPathway	UPA00557; UER00613.
Gene expression databases
ArrayExpress	Q9D1E8.
Bgee	Q9D1E8.
Genevestigator	Q9D1E8.
GermOnline	ENSMUSG00000031467. Mus musculus.
Family and domain databases
InterPro	IPR002123. Plipid/glycerol_acylTrfase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	308524.
SOURCE	Search...

Entry information

Entry name

PLCE_MOUSE

Accession

Primary (citable) accession number: Q9D1E8
Secondary accession number(s): Q3U702, Q8BG61, Q8CGN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 16, 2003
Last modified:	May 1, 2013
This is version 83 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program