Reviewed, UniProtKB/Swiss-Prot Q9D517 (PLCC_MOUSE)

Names and origin

Protein names

Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
    EC=2.3.1.51
Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 3
      Short name=1-AGP acyltransferase 3
      Short name=1-AGPAT 3
    Lysophosphatidic acid acyltransferase gamma
      Short name=LPAAT-gamma

Gene names

Name:

Agpat3

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	376 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. Ref.1
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.
Tissue specificity	Widely expressed. Ref.1
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	Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 376	376	1-acyl-sn-glycerol-3-phosphate acyltransferase gamma		PRO_0000208195
Regions
	Transmembrane	11 – 31	21	Potential
	Transmembrane	125 – 145	21	Potential
	Transmembrane	308 – 330	23	Potential
	Transmembrane	335 – 357	23	Potential
	Motif	96 – 101	6	HXXXXD motif
Experimental info
	Sequence conflict	21	1	F → V in AAH52382. Ref.3
	Sequence conflict	21	1	F → V in AAH58519. Ref.3
	Sequence conflict	249	1	Y → N in BAC27043. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9D517-1 [UniParc]. Last modified March 1, 2003. Version 2. Checksum: 6F8C8970404B2EC1	FASTA	376	43,296
	10 20 30 40 50 60 MGLLAYLKTQ FVVHLLIGFV FVVSGLIINF TQLCTLALWP ISKHLYRRIN CRLAYSLWSQ 70 80 90 100 110 120 LVMLLEWWSC TECTLFTDQA TVDHFGKEHV VVILNHNFEI DFLCGWTMCE RFGVLGSSKV 130 140 150 160 170 180 LAKRELLCVP LIGWTWYFLE IVFCKRKWEE DRDTVIEGLR RLADYPEYMW FLLYCEGTRF 190 200 210 220 230 240 TETKHRISME VAASKGLPPL KYHLLPRTKG FTTAVQCLRG TVAAIYDVTL NFRGNKNPSL 250 260 270 280 290 300 LGILYGKKYE ADMCVRRFPL EDIPADETSA AQWLHKLYQE KDALQEMYKQ KGVFPGEQFK 310 320 330 340 350 360 PARRPWTLLN FLCWATILLS PLFSFVLGVF ASGSPLLILT FLGFVGAASF GVRRLIGVTE 370 IEKGSSYGNQ ELKKKE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 15367102] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: C57BL/6J.
[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: Head, Liver, Pituitary 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: C57BL/6. Tissue: Embryonic brain.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 237-248, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY167588 mRNA. Translation: AAN75574.1. AK015906 mRNA. Translation: BAB30025.2. AK030607 mRNA. Translation: BAC27043.1. Different initiation. AK075715 mRNA. Translation: BAC35905.1. AK076414 mRNA. Translation: BAC36329.1. BC052382 mRNA. Translation: AAH52382.1. BC058519 mRNA. Translation: AAH58519.1.
IPI	IPI00469338.
RefSeq	NP_443747.2.
UniGene	Mm.141230
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q9D517.
Proteomic databases
PRIDE	Q9D517.
Genome annotation databases
Ensembl	ENSMUST00000001240; ENSMUSP00000001240; ENSMUSG00000001211; Mus musculus. [Genome view] ENSMUST00000105387; ENSMUSP00000101026; ENSMUSG00000001211; Mus musculus. [Genome view] ENSMUST00000105388; ENSMUSP00000101027; ENSMUSG00000001211; Mus musculus. [Genome view] ENSMUST00000105389; ENSMUSP00000101028; ENSMUSG00000001211; Mus musculus. [Genome view] ENSMUST00000105390; ENSMUSP00000101029; ENSMUSG00000001211; Mus musculus. [Genome view]
GeneID	28169.
KEGG	mmu:28169.
UCSC	uc007fxo.1. mouse.
Organism-specific databases
CTD	28169.
MGI	MGI:1336186. Agpat3.
Phylogenomic databases
HOGENOM	Q9D517.
HOVERGEN	Q9D517.
OMA	HFGKEHV.
Enzyme and pathway databases
BRENDA	2.3.1.51. 244.
Gene expression databases
ArrayExpress	Q9D517.
Bgee	Q9D517.
CleanEx	MM_AGPAT3.
Genevestigator	Q9D517.
GermOnline	ENSMUSG00000001211. 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	306746.
SOURCE	Search...

Entry information

Entry name

PLCC_MOUSE

Accession

Primary (citable) accession number: Q9D517
Secondary accession number(s): Q7TT39, Q8BST2

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)