Q9NUQ2 (PLCE_HUMAN) 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	364 AA.
Sequence status	Complete.
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. 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.7
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. Nucleus envelope. Mitochondrion Ref.7.
Tissue specificity	Widely expressed. Ref.5 Ref.7
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.
Biophysicochemical properties	Kinetic parameters: KM=5.52 µM for LPA sn-1 C18:1 KM=16.30 µM for C18:1-CoA Vmax=2.42 nmol/min/mg enzyme toward LPA sn-1 C18:1 Vmax=1.22 nmol/min/mg enzyme toward C18:1-CoA
Sequence caution	The sequence BAA92069.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism Phospholipid biosynthesis Phospholipid metabolism
Cellular component	Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Polymorphism
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 phosphatidic acid biosynthetic process Traceable author statement. Source: Reactome small molecule metabolic process Traceable author statement. Source: Reactome triglyceride biosynthetic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Traceable author statement. Source: Reactome nuclear envelope Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	1-acylglycerol-3-phosphate O-acyltransferase activity Non-traceable author statement PubMed 15367102. Source: UniProtKB
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	Helical; Potential
	Transmembrane	61 – 81	21	Helical; Potential
	Transmembrane	344 – 364	21	Helical; Potential
	Motif	93 – 98	6	HXXXXD motif
Natural variations
	Natural variant	77	1	Y → C. Corresponds to variant rs17077958 [ dbSNP | Ensembl ].		VAR_022696
Experimental info
	Sequence conflict	156	1	L → V in BAA92069. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NUQ2 [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[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]. Tissue: Brain and Lung.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-364. Tissue: Placenta.
[5]	"Functional characterization of human 1-acylglycerol-3-phosphate acyltransferase isoform 8: cloning, tissue distribution, gene structure, and enzymatic activity." Agarwal A.K., Barnes R.I., Garg A. Arch. Biochem. Biophys. 449:64-76(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"Enzymatic activities of the human AGPAT isoform 3 and isoform 5: localization of AGPAT5 to mitochondria." Prasad S.S., Garg A., Agarwal A.K. J. Lipid Res. 52:451-462(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF375789 mRNA. Translation: AAK54809.1. AL136587 mRNA. Translation: CAB66522.1. BC023550 mRNA. Translation: AAH23550.1. BC080537 mRNA. Translation: AAH80537.1. AK002072 mRNA. Translation: BAA92069.1. Different initiation.
IPI	IPI00028491.
RefSeq	NP_060831.2. NM_018361.3.
UniGene	Hs.624002.
3D structure databases
ProteinModelPortal	Q9NUQ2.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000285518.
PTM databases
PhosphoSite	Q9NUQ2.
Polymorphism databases
DMDM	30923427.
Proteomic databases
PaxDb	Q9NUQ2.
PeptideAtlas	Q9NUQ2.
PRIDE	Q9NUQ2.
Protocols and materials databases
DNASU	55326.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000285518; ENSP00000285518; ENSG00000155189.
GeneID	55326.
KEGG	hsa:55326.
UCSC	uc003wqo.3. human.
Organism-specific databases
CTD	55326.
GeneCards	GC08P006554.
HGNC	HGNC:20886. AGPAT5.
HPA	HPA010644. HPA010950.
MIM	614796. gene.
neXtProt	NX_Q9NUQ2.
PharmGKB	PA134952751.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0204.
HOGENOM	HOG000007801.
HOVERGEN	HBG039632.
InParanoid	Q9NUQ2.
OMA	ADMLAIR.
OrthoDB	EOG4F7NK8.
PhylomeDB	Q9NUQ2.
Enzyme and pathway databases
BioCyc	MetaCyc:HS08034-MONOMER.
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00557; UER00613.
Gene expression databases
ArrayExpress	Q9NUQ2.
Bgee	Q9NUQ2.
CleanEx	HS_AGPAT5.
Genevestigator	Q9NUQ2.
GermOnline	ENSG00000155189. Homo sapiens.
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
GenomeRNAi	55326.
NextBio	59600.
SOURCE	Search...

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:	May 1, 2013
This is version 100 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.