Reviewed, UniProtKB/Swiss-Prot Q53EU6 (PLCH_HUMAN)

Names and origin

Protein names

Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase theta
    EC=2.3.1.51
Alternative name(s):
    1-AGP acyltransferase 9
      Short name=1-AGPAT 9
    Lysophosphatidic acid acyltransferase theta
      Short name=LPAAT-theta
    Acyl-CoA:glycerol-3-phosphate acyltransferase 3
      Short name=hGPAT3
    Lung cancer metastasis-associated protein 1
    MAG-1

Gene names

Name:	AGPAT9
Synonyms:	GPAT3, MAG1
ORF Names:	HMFN0839, UNQ2753/PRO6492

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Endoplasmic reticulum acyl-CoA:glycerol-3-phosphate acyltransferase, which catalyzes the first step during de novo synthesis of triacylglycerol. Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone. Overexpression activates the mTOR pathway.
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.
Enzyme regulation	Inhibited by N-ethylmaleimide (NEM).
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein.
Tissue specificity	Widely expressed. Expressed in liver, kidney, testis, brain, heart, skeletal muscle, thyroid, prostate, thymus and placenta. Also expressed lung and adipose tissue.
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	Transmembrane
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 434	434	1-acyl-sn-glycerol-3-phosphate acyltransferase theta
Regions
	Transmembrane	14 – 34	21	Potential
	Transmembrane	137 – 157	21	Potential
	Transmembrane	161 – 181	21	Potential
	Motif	229 – 234	6	HXXXXD motif
Experimental info
	Sequence conflict	156	1	L → I in BAD97263. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q53EU6-1 [UniParc]. Last modified June 26, 2007. Version 2. Checksum: 80DD5423E5E7847A	FASTA	434	48,705
	10 20 30 40 50 60 MEGAELAGKI LSTWLTLVLG FILLPSVFGV SLGISEIYMK ILVKTLEWAT IRIEKGTPKE 70 80 90 100 110 120 SILKNSASVG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE 130 140 150 160 170 180 LVSWNLLTRT NVNFQYISLR LTMVWVLGVI VRYCVLLPLR VTLAFIGISL LVIGTTLVGQ 190 200 210 220 230 240 LPDSSLKNWL SELVHLTCCR ICVRALSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILTT 250 260 270 280 290 300 DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEMKDRH LVTKRLKEHI ADKKKLPILI 310 320 330 340 350 360 FPEGTCINNT SVMMFKKGSF EIGGTIHPVA IKYNPQFGDA FWNSSKYNMV SYLLRMMTSW 370 380 390 400 410 420 AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAIQGGLTEL PWDGGLKRAK VKDIFKEEQQ 430 KNYSKMIVGN GSLS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of metastasis associated genes MAG-1 and MAG-2." Zhang J., Meng Y., Du Z., Chen Z., Ling X., Xu Y., Lu Y. Zhongguo Fei Ai Za Zhi 6:460-463(2003) Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification of a novel human lysophosphatidic acid acyltransferase, LPAAT-theta, which activates mTOR pathway." Tang W., Yuan J., Chen X., Gu X., Luo K., Li J., Wan B., Wang Y., Yu L. J. Biochem. Mol. Biol. 39:626-635(2006) [PubMed: 17002884] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[3]	"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment." Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M. Genome Res. 13:2265-2270(2003) [PubMed: 12975309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[5]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
[6]	"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: PNS and Testis.
[7]	"Expression profiling and differential screening between hepatoblastomas and the corresponding normal livers: identification of high expression of the PLK1 oncogene as a poor-prognostic indicator of hepatoblastomas." Yamada S., Ohira M., Horie H., Ando K., Takayasu H., Suzuki Y., Sugano S., Hirata T., Goto T., Matsunaga T., Hiyama E., Hayashi Y., Ando H., Suita S., Kaneko M., Sasaki F., Hashizume K., Ohnuma N., Nakagawara A. Oncogene 23:5901-5911(2004) [PubMed: 15221005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 167-434.
[8]	"Molecular identification of microsomal acyl-CoA:glycerol-3-phosphate acyltransferase, a key enzyme in de novo triacylglycerol synthesis." Cao J., Li J.-L., Li D., Tobin J.F., Gimeno R.E. Proc. Natl. Acad. Sci. U.S.A. 103:19695-19700(2006) [PubMed: 17170135] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ324782 mRNA. Translation: ABC55674.1. DQ345298 mRNA. Translation: ABC70186.1. AY358100 mRNA. Translation: AAQ88467.1. AK055749 mRNA. Translation: BAB71002.1. AK223543 mRNA. Translation: BAD97263.1. BC073136 mRNA. Translation: AAH73136.1. BC090956 mRNA. Translation: AAH90956.1. AB075872 mRNA. Translation: BAD38654.1.
RefSeq	NP_116106.2.
UniGene	Hs.99196
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q53EU6.
Genome annotation databases
Ensembl	ENSG00000138678. Homo sapiens. [Contig view]
GeneID	84803.
KEGG	hsa:84803.
Organism-specific databases
HGNC	HGNC:28157. AGPAT9.
MIM	610958. gene.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q53EU6.
HOVERGEN	Q53EU6.
Gene expression databases
ArrayExpress	Q53EU6.
CleanEx	HS_AGPAT9.
Family and domain databases
InterPro	IPR002123. Acyltransferase. [Graphical view]
Pfam	PF01553. Acyltransferase. 1 hit. [Graphical view]
SMART	SM00563. PlsC. 1 hit. [Graphical view]
ProDom	Q53EU6. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

PLCH_HUMAN

Accession

Primary (citable) accession number: Q53EU6
Secondary accession number(s): Q68CJ4, Q6GPI6, Q96NA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	June 26, 2007
Last modified:	September 2, 2008
This is version 24 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)