Reviewed, UniProtKB/Swiss-Prot Q8LG50 (LPAT2_ARATH)

Names and origin

Protein names

Recommended name:
    1-acyl-sn-glycerol-3-phosphate acyltransferase 2
    EC=2.3.1.51
Alternative name(s):
    Lysophosphatidyl acyltransferase 2

Gene names

Name:	LPAT2
Synonyms:	LPAAT2
Ordered Locus Names:	At3g57650
ORF Names:	F15B8.160

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	389 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 acyl moiety at the 2 position. Has preference for C-18-CoA substrates compared to C-16-CoA substrates. Required for female but not male gametophyte development. Ref.4
Catalytic activity	Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate. Ref.4
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. Ref.4
Tissue specificity	Present in roots, leaves, stems, floral buds and siliques (at protein level). Widely expressed. In contrast to LPAT1, it is not expressed at higher level in leaves. Ref.4 Ref.3
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.
Sequence caution	The sequence CAB41190.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Developmental protein Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-acylglycerol-3-phosphate O-acyltransferase activity Ref.4 Inferred from direct assay. Source: TAIR
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 389	389	1-acyl-sn-glycerol-3-phosphate acyltransferase 2		PRO_0000208179
Regions
	Transmembrane	2 – 22	21	Potential
	Transmembrane	305 – 325	21	Potential
	Transmembrane	333 – 353	21	Potential
	Motif	91 – 96	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q8LG50-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: F34F73B2E2AC6837	FASTA	389	43,706
	10 20 30 40 50 60 MVIAAAVIVP LGLLFFISGL AVNLFQAVCY VLIRPLSKNT YRKINRVVAE TLWLELVWIV 70 80 90 100 110 120 DWWAGVKIQV FADNETFNRM GKEHALVVCN HRSDIDWLVG WILAQRSGCL GSALAVMKKS 130 140 150 160 170 180 SKFLPVIGWS MWFSEYLFLE RNWAKDESTL KSGLQRLSDF PRPFWLALFV EGTRFTEAKL 190 200 210 220 230 240 KAAQEYAASS ELPIPRNVLI PRTKSFVSAV SNMRSFVPAI YDMTVTIPKT SPPPTMLRLF 250 260 270 280 290 300 KGQPSVVHVH IKCHSMKDLP ESDDAIAQWC RDQFVAKDAL LDKHIAADTF PGQQEQNIGR 310 320 330 340 350 360 PIKSLAVVLS WACVLTLGAI KFLHWAQLFS SWKGITISAL GLGIITLCMQ ILIRSSQSER 370 380 STPAKVVPAK PKDNHHPESS SQTETEKEK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Plastid lysophosphatidyl acyltransferase is essential for embryo development in Arabidopsis." Kim H.U., Huang A.H.C. Plant Physiol. 134:1206-1216(2004) [PubMed: 14976237] [Abstract] Cited for: TISSUE SPECIFICITY.
[4]	"Ubiquitous and endoplasmic reticulum-located lysophosphatidyl acyltransferase, LPAT2, is essential for female but not male gametophyte development in Arabidopsis." Kim H.U., Li Y., Huang A.H.C. Plant Cell 17:1073-1089(2005) [PubMed: 15772283] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL049660 Genomic DNA. Translation: CAB41190.1. Sequence problems. AY084461 mRNA. Translation: AAM61033.1.
IPI	IPI00528234.
PIR	T06755.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q8LG50.
Genome annotation databases
GenomeReviews	Gene locus AT3G57650 in contig BA000014_GR.
Organism-specific databases
TAIR	At3g57650.
Enzyme and pathway databases
BRENDA	2.3.1.51. 302.
Gene expression databases
GermOnline	AT3G57650. Arabidopsis thaliana.
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...

Entry information

Entry name

LPAT2_ARATH

Accession

Primary (citable) accession number: Q8LG50
Secondary accession number(s): Q9SVX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 1, 2002
Last modified:	June 16, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)