Reviewed, UniProtKB/Swiss-Prot Q6DG38 (GPAT3_DANRE)

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
ORF Names:	si:ch211-85e10.5, zgc:91857

Organism

Danio rerio (Zebrafish) (Brachydanio rerio)

Taxonomic identifier

7955 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Ostariophysi › Cypriniformes › Cyprinidae › Danio

Protein attributes

Sequence length	449 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
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 – 449	449	Glycerol-3-phosphate acyltransferase 3		PRO_0000291575
Regions
	Transmembrane	9 – 29	21	Potential
	Transmembrane	146 – 166	21	Potential
	Transmembrane	170 – 190	21	Potential
	Transmembrane	358 – 378	21	Potential
	Motif	238 – 243	6	HXXXXD motif

Sequences

	Sequence		Length	Mass (Da)
	Q6DG38-1 [UniParc]. Last modified August 16, 2004. Version 1. Checksum: 94FF3F8FB2A04B7C	FASTA	449	50,633
	10 20 30 40 50 60 MEGAWDVAFV LLHVWMSIVA GLIVLPAMFG VSLGFTDIYI KLLVKTLEWA TLRIQRGQKE 70 80 90 100 110 120 QPTLPLQLAN GIIEKDDGSM EEEIVELRRS HPKNLAEGNF TLCDAFYFCK KGIENIVEDQ 130 140 150 160 170 180 VTQRFSSEEL ASWNLLTRTN NNFRYISVRL TIIWGLGVFV RYCVLLPLRI TLAVIGLSWL 190 200 210 220 230 240 VIGTTLVGFL PNSKVKNWLS DLVHITCYRI CARGLSATIR YHNKENRPKK GGICVANHTS 250 260 270 280 290 300 PIDIVILAND GCYAMVGQVH GGLMGVIQRS MVRSCPHVWF ERSEMKDRHA VAKRLKDHIS 310 320 330 340 350 360 DKTKLPILIF PEGTCINNTS VMMFKKGSFE FGGTIYPVAI KYDPRFGDAF WNSAKYNMVS 370 380 390 400 410 420 YILRMMTSWA IVCNVWYLPP MTQQDGEDAV HFANRVKSAI AHQGGLVDLS WDGGLKRSKV 430 440 KESFKEEQQK MYSSMIVGLD SHEATVGPA

References

[1]	The Danio rerio sequencing project at the Sanger Institute Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tuebingen.
[2]	NIH - Zebrafish Gene Collection (ZGC) project Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX649525 Genomic DNA. Translation: CAK05016.1. Different initiation. BC076515 mRNA. Translation: AAH76515.1.
IPI	IPI00931309.
RefSeq	NP_001002685.1.
UniGene	Dr.106485
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	ENSDART00000008389; ENSDARP00000024703; ENSDARG00000016048; Danio rerio. [Genome view] ENSDART00000113997; ENSDARP00000097613; ENSDARG00000077689; Danio rerio. [Genome view]
GeneID	436958.
KEGG	dre:436958.
Organism-specific databases
CTD	436958.
ZFIN	ZDB-GENE-040718-436. agpat9.
Phylogenomic databases
HOVERGEN	Q6DG38.
OMA	VADVWYL.
Enzyme and pathway databases
BRENDA	2.3.1.51. 96826.
Gene expression databases
Bgee	Q6DG38.
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

GPAT3_DANRE

Accession

Primary (citable) accession number: Q6DG38
Secondary accession number(s): Q1LVP5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	August 16, 2004
Last modified:	November 3, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Zebrafish annotation project