Reviewed, UniProtKB/Swiss-Prot Q4V8J4 (GPAT3_RAT)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 3
      Short name=GPAT3
    EC=2.3.1.15
Alternative name(s):
    1-acylglycerol-3-phosphate O-acyltransferase 9
      Short name=1-AGP acyltransferase 9
      Short name=1-AGPAT 9
    Lysophosphatidic acid acyltransferase theta
      Short name=LPAAT-theta

Gene names

Name:	Agpat9
Synonyms:	Gpat3

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	457 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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 By similarity.
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Pathway	Glycerolipid metabolism; triacylglycerol biosynthesis. Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3.
Subcellular location	Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity.
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.

Ontologies

Keywords
Biological process	Phospholipid biosynthesis
Cellular component	Endoplasmic reticulum Membrane
Domain	Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	phospholipid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW triglyceride biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	endoplasmic reticulum membrane Inferred from sequence or structural similarity. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	glycerol-3-phosphate O-acyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 457	457	Glycerol-3-phosphate acyltransferase 3		PRO_0000291572
Regions
	Transmembrane	14 – 34	21	Potential
	Transmembrane	137 – 157	21	Potential
	Transmembrane	161 – 181	21	Potential
	Motif	229 – 234	6	HXXXXD motif
Amino acid modifications
	Modified residue	68	1	Phosphoserine By similarity
	Modified residue	77	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4V8J4-1 [UniParc]. Last modified July 5, 2005. Version 1. Checksum: BC8A63BF240137A9	FASTA	457	51,012
	10 20 30 40 50 60 MEGTDLVVKL LSTWLTLVGS LILLPSAFGL SLGISEIYMK ILVKTLEWAT LRIEKGAPKE 70 80 90 100 110 120 SVLKSPASMG IIQRDESPME KGLSGLRGRD FELSDVFYFS KKGLEAIVED EVTQRFSSEE 130 140 150 160 170 180 LVSWNLLTRT NVNFHYISPK LTIVWVLGVL VRYCFLLPLR VTLAFIGISL LIIGTTLVGQ 190 200 210 220 230 240 LPDSSLKNWL SELVHLTCCR ICVRSLSGTI HYHNKQYRPQ KGGICVANHT SPIDVLILAT 250 260 270 280 290 300 DGCYAMVGQV HGGLMGIIQR AMVKACPHVW FERSEIKDRH LVTKRLKEHI ADKKKLPILI 310 320 330 340 350 360 FPEGTCINNT SVMMFKKGSF EIGGTIYPVA IKYNPQFGDA FWNSSKYNLV SYLLRIMTSW 370 380 390 400 410 420 AIVCDVWYMP PMTREEGEDA VQFANRVKSA IAVQGGLTEL PWDGGLKRAK VKDTFKEEQQ 430 440 450 KTYSKMIVGN GSPSLALDSS TVDNHGSPEP AFRSESL

References

[1]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BC097362 mRNA. Translation: AAH97362.1.
IPI	IPI00363908.
RefSeq	NP_001020841.1.
UniGene	Rn.214521
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q4V8J4.
Genome annotation databases
Ensembl	ENSRNOT00000002936; ENSRNOP00000002936; ENSRNOG00000002159; Rattus norvegicus. [Genome view]
GeneID	305166.
KEGG	rno:305166.
UCSC	NM_001025670. rat.
Organism-specific databases
CTD	305166.
RGD	1565703. Agpat9.
Phylogenomic databases
HOVERGEN	Q4V8J4.
OMA	WFERSEI.
Enzyme and pathway databases
BRENDA	2.3.1.51. 248.
Gene expression databases
Genevestigator	Q4V8J4.
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...
Other Resources
NextBio	654172.

Entry information

Entry name

GPAT3_RAT

Accession

Primary (citable) accession number: Q4V8J4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	July 5, 2005
Last modified:	November 3, 2009
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)