Reviewed, UniProtKB/Swiss-Prot Q9LHS7 (GPAT7_ARATH)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 7
      Short name=AtGPAT7
    EC=2.3.1.15

Gene names

Name:	GPAT7
Ordered Locus Names:	At5g06090
ORF Names:	K16F4.5

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	500 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.2
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	Weakly or not expressed in roots, leaves, seedlings, developing siliques and flower buds. Ref.2
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=58.93 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	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.2 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 – 500	500	Glycerol-3-phosphate acyltransferase 7		PRO_0000195255
Regions
	Transmembrane	38 – 58	21	Potential
	Transmembrane	235 – 255	21	Potential
	Motif	298 – 303	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q9LHS7-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 717F16F9A1AB2289	FASTA	500	56,082
	10 20 30 40 50 60 MESSTTTSYS VVSELEGTLL KNPKPFAYFM LVAFEASGLI RFATLLFLWP IIALLDVLGY 70 80 90 100 110 120 RNGSLKLMIF VATAGLHESE IESVARAVLP KFFMDDISMD AWRAFGSCDK RVVVTRMPRV 130 140 150 160 170 180 MVERFAKDHL SADEVIGTEI VVNRFGYATG LIQETNVDQS VFNSVANLFV DRRPQLGLGR 190 200 210 220 230 240 HIISDSPTFL SLCEEQVHAP VPSNYNGHNQ RLHVQPLPVI FHDGRLVKLP TPATALIILL 250 260 270 280 290 300 WIPFGIILAM IRIFVGFLLP LWAIPYVSRI FNTRFIVKGK PPAQATTGNP GVLFVCTHRT 310 320 330 340 350 360 LMDPVVLSYV LGRSIPAVTY SISRLSEILS PIPTFRLTRI RDVDAEMIKK ELSNGDLVVY 370 380 390 400 410 420 PEGTTCREPF LLRFSALFAE LTDNIVPVAM NYRVGFFHAT TARGWKGLDP IFFFMNPRPV 430 440 450 460 470 480 YEVTFLNQLE VEATCSSGKS PYDVANYVQR ILAATLGFEC TNFTRKDKYR VLAGNDGTVS 490 500 YLSFLDQVKK VVTTFKPFLH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of Arabidopsis thaliana chromosome 5. XI." Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S. Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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
EMBLGenBankDDBJ	AP002030 Genomic DNA. Translation: BAA98198.1.
IPI	IPI00538134.
RefSeq	NP_196227.1.
UniGene	At.54743
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	830496.
GenomeReviews	Gene locus AT5G06090 in contig BA000015_GR.
KEGG	ath:AT5G06090.
NMPDR	fig|3702.1.peg.22726.
Organism-specific databases
TAIR	At5g06090.
Phylogenomic databases
OMA	PRIMAER.
Enzyme and pathway databases
BRENDA	2.3.1.15. 302.
Gene expression databases
Genevestigator	Q9LHS7.
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

GPAT7_ARATH

Accession

Primary (citable) accession number: Q9LHS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 42 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)