Reviewed, UniProtKB/Swiss-Prot Q9LMM0 (GPAT4_ARATH)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 4
      Short name=AtGPAT4
    EC=2.3.1.15

Gene names

Name:	GPAT4
Ordered Locus Names:	At1g01610
ORF Names:	F22L4.15

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 › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	503 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Esterifies acyl-group from acyl-ACP to the sn-1 position of glycerol-3-phosphate, an essential step in glycerolipid biosynthesis.
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. Ref.3
Pathway	Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Widely expressed at high level. Highly expressed in seedlings, developing seedlings and flower buds. 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 GPAT/DAPAT family.
Biophysicochemical properties	Kinetic parameters: Vmax=58.92 pmol/min/mg enzyme

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cutin biosynthetic process Inferred from mutant phenotype. Source: TAIR 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 Ref.3 Inferred from genetic interaction. Source: TAIR glycerol-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 – 503	503	Glycerol-3-phosphate acyltransferase 4		PRO_0000195252
Regions
	Transmembrane	42 – 62	21	Potential
	Transmembrane	64 – 84	21	Potential
	Transmembrane	244 – 264	21	Potential
	Motif	311 – 316	6	HXXXXD motif
Experimental info
	Sequence conflict	205	1	M → K in AAL32544. Ref.2
	Sequence conflict	205	1	M → K in AAM13293. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9LMM0-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 827EEB7EBE337766	FASTA	503	56,262
	10 20 30 40 50 60 MSPAKKSRSF PPISECKSRE YDSIAADLDG TLLLSRSSFP YFMLVAIEAG SLFRGLILLL 70 80 90 100 110 120 SLPIVIIAYL FVSESLGIQI LIFISFAGIK IKNIELVSRA VLTRFYAADV RKDSFEVFDK 130 140 150 160 170 180 CKKRKVVVTA NPIVMVEPFV KDYLGGDKVL GTEIEVNPKT MKATGFVKKP GVLVGDLKRL 190 200 210 220 230 240 AILKEFGDDS PDLGLGDRTS DHDFMSICKE GYMVHETKSA TTVPIESLKN RIIFHDGRLV 250 260 270 280 290 300 QRPTPLNALI IYLWLPFGFM LSVFRVYFNL PLPERFVRYT YEILGIHLTI RGHRPPPPSP 310 320 330 340 350 360 GKPGNLYVLN HRTALDPIII AIALGRKITC VTYSVSRLSL MLSPIPAVAL TRDRVADAAR 370 380 390 400 410 420 MRQLLEKGDL VICPEGTTCR EPYLLRFSAL FAELSDRIVP VAMNCKQGMF NGTTVRGVKF 430 440 450 460 470 480 WDPYFFFMNP RPSYEATFLD RLPEEMTVNG GGKTPFEVAN YVQKVIGGVL GFECTELTRK 490 500 DKYLLLGGND GKVESINKTK SME

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]	"Arabidopsis AtGPAT1, a member of the membrane-bound glycerol-3-phosphate acyltransferase gene family, is essential for tapetum differentiation and male fertility." Zheng Z., Xia Q., Dauk M., Shen W., Selvaraj G., Zou J. Plant Cell 15:1872-1887(2003) [PubMed: 12897259] [Abstract] Cited for: ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC061957 Genomic DNA. Translation: AAF81319.1. AY062466 mRNA. Translation: AAL32544.1. AY093294 mRNA. Translation: AAM13293.1.
IPI	IPI00538377.
PIR	H86146.
RefSeq	NP_171667.1.
UniGene	At.22475 Rra.14086
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	Q9LMM0.
Genome annotation databases
GeneID	839297.
GenomeReviews	Gene locus AT1G01610 in contig CT485782_GR.
KEGG	ath:AT1G01610.
NMPDR	fig|3702.1.peg.271.
Organism-specific databases
TAIR	At1g01610.
Phylogenomic databases
HOGENOM	HBG590278.
InParanoid	Q9LMM0.
Enzyme and pathway databases
BRENDA	2.3.1.15. 302.
Gene expression databases
Genevestigator	Q9LMM0.
GermOnline	AT1G01610. 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

GPAT4_ARATH

Accession

Primary (citable) accession number: Q9LMM0
Secondary accession number(s): Q8W4N0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)