Reviewed, UniProtKB/Swiss-Prot Q9NUQ2 (PLCE_HUMAN)

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

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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 By similarity.
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	Membrane; Multi-pass membrane protein Potential.
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	Phospholipid biosynthesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: LIFEdb
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Non-traceable author statement. Source: UniProtKB phospholipid:diacylglycerol acyltransferase activity Inferred from Experiment. Source: Reactome
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 364	364	1-acyl-sn-glycerol-3-phosphate acyltransferase epsilon		PRO_0000208200
Regions
	Transmembrane	15 – 35	21	Potential
	Transmembrane	61 – 81	21	Potential
	Transmembrane	344 – 364	21	Potential
	Motif	93 – 98	6	HXXXXD motif
Natural variations
	Natural variant	77	1	Y → C: dbSNP rs17077958.		VAR_022696
Experimental info
	Sequence conflict	156	1	L → V in BAA92069. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NUQ2-1 [UniParc]. Last modified May 16, 2003. Version 3. Checksum: 90A0F87FC7C78081	FASTA	364	42,072
	10 20 30 40 50 60 MLLSLVLHTY SMRYLLPSVV LLGTAPTYVL AWGVWRLLSA FLPARFYQAL DDRLYCVYQS 70 80 90 100 110 120 MVLFFFENYT GVQILLYGDL PKNKENIIYL ANHQSTVDWI VADILAIRQN ALGHVRYVLK 130 140 150 160 170 180 EGLKWLPLYG CYFAQHGGIY VKRSAKFNEK EMRNKLQSYV DAGTPMYLVI FPEGTRYNPE 190 200 210 220 230 240 QTKVLSASQA FAAQRGLAVL KHVLTPRIKA THVAFDCMKN YLDAIYDVTV VYEGKDDGGQ 250 260 270 280 290 300 RRESPTMTEF LCKECPKIHI HIDRIDKKDV PEEQEHMRRW LHERFEIKDK MLIEFYESPD 310 320 330 340 350 360 PERRKRFPGK SVNSKLSIKK TLPSMLILSG LTAGMLMTDA GRKLYVNTWI YGTLLGCLWV TIKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of LPAAT-epsilon." Leung D.W. Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[4]	"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]. Tissue: Brain and Lung.
[5]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF375789 mRNA. Translation: AAK54809.1. AL136587 mRNA. Translation: CAB66522.1. AK002072 mRNA. Translation: BAA92069.1. Different initiation. BC023550 mRNA. Translation: AAH23550.1. BC080537 mRNA. Translation: AAH80537.1.
IPI	IPI00028491.
RefSeq	NP_060831.2.
UniGene	Hs.624002
3D structure databases
ModBase	Search...
Proteomic databases
PeptideAtlas	Q9NUQ2.
PRIDE	Q9NUQ2.
Genome annotation databases
Ensembl	ENSG00000155189. Homo sapiens. [Contig view]
GeneID	55326.
KEGG	hsa:55326.
UCSC	uc003wqo.1. human.
Organism-specific databases
GeneCards	GC08P006554.
HGNC	HGNC:20886. AGPAT5.
HPA	HPA010644. HPA010950.
PharmGKB	PA134952751.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9NUQ2.
HOVERGEN	Q9NUQ2.
OMA	Q9NUQ2. VLTPRVK.
Enzyme and pathway databases
BRENDA	2.3.1.51. 247.
Reactome	REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	Q9NUQ2.
Bgee	Q9NUQ2.
CleanEx	HS_AGPAT5.
GermOnline	ENSG00000155189. Homo sapiens.
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	59600.

Entry information

Entry name

PLCE_HUMAN

Accession

Primary (citable) accession number: Q9NUQ2
Secondary accession number(s): Q8IZ47, Q9BQG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	May 16, 2003
Last modified:	July 7, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)