Reviewed, UniProtKB/Swiss-Prot Q8L4Y2 (LPAT4_ARATH)

Names and origin

Protein names

Recommended name:
    Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4
    EC=2.3.1.51
Alternative name(s):
    Lysophosphatidyl acyltransferase 4

Gene names

Name:	LPAT4
Synonyms:	LPAAT4
Ordered Locus Names:	At1g75020
ORF Names:	F25A4.2

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

General annotation (Comments)

Function	May convert lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position By similarity. Has no activity when expressed in bacteria or yeast.
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 at low level. Ref.4
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 AAD55275.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAG51931.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
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-KW
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 – 378	378	Probable 1-acyl-sn-glycerol-3-phosphate acyltransferase 4		PRO_0000208183
Regions
	Transmembrane	26 – 46	21	Potential
	Transmembrane	62 – 82	21	Potential
	Transmembrane	317 – 337	21	Potential
	Motif	105 – 110	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q8L4Y2-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 36DB41D29E3B7ABC	FASTA	378	43,064
	10 20 30 40 50 60 MEVCGDLKSD NLKNRPLTPL RILRGLMILL VFLSTAFMFL LYFAPIAALG LRLLSVQQSR 70 80 90 100 110 120 KVVSLIFGLW LALWPYLFET VNGTTVVFSG DIIPVEKRVL LIANHRTEVD WMYLWNIALR 130 140 150 160 170 180 KGCLGYIKYV LKSSLMKLPI FGWGFHVLEF IPVERKREVD EPVLLQMLSS FKDPQEPLWL 190 200 210 220 230 240 ALFPEGTDFT EEKCKRSQKF AAEVGLPALS NVLLPKTRGF GVCLEVLHNS LDAVYDLTIA 250 260 270 280 290 300 YKPRCPSFMD NVFGTDPSEV HIHVRRVLLK EIPANEAESS AWLMDSFKLK DKLLSDFNAQ 310 320 330 340 350 360 GKFPNQRPEE ELSVLKCIAT FAGVISLTVV FIYLTLYSHS CFKVYACLSG TYLTFATYYK 370 FQPSPGCFRE DSCKVKNH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"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].
[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: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC008263 Genomic DNA. Translation: AAD55275.1. Sequence problems. AC013258 Genomic DNA. Translation: AAG51931.1. Sequence problems. AY099547 mRNA. Translation: AAM20399.1. BT001236 mRNA. Translation: AAN65123.1. AY084709 mRNA. Translation: AAM61283.1.
IPI	IPI00537505.
PIR	B96780.
RefSeq	NP_565098.1. NP_974144.1.
UniGene	At.43179
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	843840.
GenomeReviews	Gene locus AT1G75020 in contig CT485782_GR.
KEGG	ath:AT1G75020.
NMPDR	fig|3702.1.peg.7018.
Organism-specific databases
TAIR	At1g75020.
Phylogenomic databases
OMA	Q8L4Y2. ITIAYKH.
Enzyme and pathway databases
BRENDA	2.3.1.51. 302.
Gene expression databases
ArrayExpress	Q8L4Y2.
GermOnline	AT1G75020. 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

LPAT4_ARATH

Accession

Primary (citable) accession number: Q8L4Y2
Secondary accession number(s): Q9C9P8, Q9SSH0

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)