Reviewed, UniProtKB/Swiss-Prot Q9SHJ5 (GPAT1_ARATH)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 1
      Short name=AtGPAT1
    EC=2.3.1.15

Gene names

Name:	GPAT1
Ordered Locus Names:	At1g06520
ORF Names:	F12K11.15

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	585 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. Involved in pollen development, by being required for tapetum differentiation and male fertility. In addition to the sporophytic effect, it also exerts a gametophytic effect on pollen performance. Ref.3
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. Mitochondrion. Note: According to Ref.3 it is mitochondrial. However, no clear transit peptide is predicted by sequence analysis tools. Ref.3
Tissue specificity	Highly expressed in developing siliques and flower buds. Weakly or not expressed in roots, seedlings and leaves. 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.
Disruption phenotype	Plants display a massive pollen development arrest due to a perturbed degeneration of the tapetum, which is associated with altered endoplasmic reticulum profiles and reduced secretion. Defects correlate with several fatty acid composition changes in flower tissues and seeds. However, no significant change in seed oil content is observed. Ref.3
Sequence similarities	Belongs to the GPAT/DAPAT family.
Biophysicochemical properties	Kinetic parameters: Vmax=217.42 pmol/min/mg enzyme

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Membrane Mitochondrion
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 pollen sperm cell differentiation Ref.3 Inferred from mutant phenotype. Source: TAIR
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Ref.3 Inferred from direct assay. Source: TAIR
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 – 585	585	Glycerol-3-phosphate acyltransferase 1		PRO_0000195249
Regions
	Transmembrane	126 – 146	21	Potential
	Transmembrane	334 – 354	21	Potential
	Transmembrane	356 – 376	21	Potential
	Motif	403 – 408	6	HXXXXD motif
Experimental info
	Sequence conflict	21	1	K → N in AAM67097. Ref.2
	Sequence conflict	270	1	F → L in AAM67097. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9SHJ5-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 3F7FDCE161C28EAF	FASTA	585	66,514
	10 20 30 40 50 60 MVLPELLVIL AEWVLYRLLA KSCYRAARKL RGYGFQLKNL LSLSKTQSLH NNSQHHLHNH 70 80 90 100 110 120 HQQNHPNQTL QDSLDPLFPS LTKYQELLLD KNRACSVSSD HYRDTFFCDI DGVLLRQHSS 130 140 150 160 170 180 KHFHTFFPYF MLVAFEGGSI IRAILLLLSC SFLWTLQQET KLRVLSFITF SGLRVKDMDN 190 200 210 220 230 240 VSRSVLPKFF LENLNIQVYD IWARTEYSKV VFTSLPQVLV ERFLREHLNA DDVIGTKLQE 250 260 270 280 290 300 IKVMGRKFYT GLASGSGFVL KHKSAEDYFF DSKKKPALGI GSSSSPQDHI FISICKEAYF 310 320 330 340 350 360 WNEEESMSKN NALPRERYPK PLIFHDGRLA FLPTPLATLA MFIWLPIGFL LAVFRISVGV 370 380 390 400 410 420 FLPYHVANFL ASMSGVRITF KTHNLNNGRP EKGNSGVLYV CNHRTLLDPV FLTTSLGKPL 430 440 450 460 470 480 TAVTYSLSKF SEFIAPLKTV SLKRDRKKDG EAMQRLLSKG DLVVCPEGTT CREPYLLRFS 490 500 510 520 530 540 PLFAELTEDI VPVAVDARVS MFYGTTASGL KCLDPIFFLM NPRPVYCLEI LKKLPKEMTC 550 560 570 580 AGGKSSFEVA NFIQGELARV LGFECTNLTR RDKYLVLAGN EGIVR

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]	"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]	"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: FUNCTION, ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AC007592 Genomic DNA. Translation: AAF24816.1. AY088785 mRNA. Translation: AAM67097.1.
IPI	IPI00543964.
PIR	G86200.
RefSeq	NP_563768.1.
UniGene	At.27686
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	837163.
GenomeReviews	Gene locus AT1G06520 in contig CT485782_GR.
KEGG	ath:AT1G06520.
NMPDR	fig|3702.1.peg.828.
Organism-specific databases
TAIR	At1g06520.
Phylogenomic databases
OMA	AFEGGSI.
Enzyme and pathway databases
BRENDA	2.3.1.15. 302.
Gene expression databases
Genevestigator	Q9SHJ5.
GermOnline	AT1G06520. 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

GPAT1_ARATH

Accession

Primary (citable) accession number: Q9SHJ5
Secondary accession number(s): Q8L8V5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 1, 2000
Last modified:	November 3, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)