Reviewed, UniProtKB/Swiss-Prot Q5R6J7 (GPAT4_PONAB)

Names and origin

Protein names

Recommended name:
    Glycerol-3-phosphate acyltransferase 4
      Short name=GPAT4
    EC=2.3.1.15
Alternative name(s):
    Acyl-CoA:glycerol-3-phosphate acyltransferase 4
    1-acylglycerol-3-phosphate O-acyltransferase 6
      Short name=1-AGP acyltransferase 6
      Short name=1-AGPAT 6
    Lysophosphatidic acid acyltransferase zeta
      Short name=LPAAT-zeta

Gene names

Name:	AGPAT6
Synonyms:	GPAT4

Organism

Pongo abelii (Sumatran orangutan)

Taxonomic identifier

9601 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length	456 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Active against both saturated and unsaturated long-chain fatty acyl-CoAs By similarity.
Catalytic activity	Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate.
Pathway	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	Signal Transmembrane
Molecular function	Acyltransferase Transferase
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	lactation Inferred from sequence or structural similarity. Source: UniProtKB 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 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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Potential
	Chain	38 – 456	419	Glycerol-3-phosphate acyltransferase 4		PRO_0000024705
Regions
	Transmembrane	156 – 176	21	Potential
	Transmembrane	180 – 200	21	Potential
	Motif	248 – 253	6	HXXXXD motif By similarity
Amino acid modifications
	Modified residue	218	1	Phosphotyrosine By similarity
	Glycosylation	247	1	N-linked (GlcNAc...) Potential
	Glycosylation	327	1	N-linked (GlcNAc...) Potential
	Glycosylation	328	1	N-linked (GlcNAc...) Potential
	Glycosylation	362	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q5R6J7-1 [UniParc]. Last modified June 21, 2005. Version 2. Checksum: D227B44AC447057B	FASTA	456	52,085
	10 20 30 40 50 60 MFLLLPFDSL IVNLLGISLT VLFTLLLVFI IVPAIFGVSF GIRKLYMKTL LKIFAWATLR 70 80 90 100 110 120 MERGAKEKNH QLYKPYTNGI IAKDPTSLEE EIKEIRRSGS SKALDNTPEF ELSDIFYFCR 130 140 150 160 170 180 KGMETIMDDE VTKRFSAEEL ESWNLLSRTN YNFQYISLRL TVLWGLGVLI RYCFLLPLRI 190 200 210 220 230 240 ALAFTGISLL VVGTTVVGYL PNGRFKEFMS KHVHLMCYRI CVRALTAIIT YHDRENRPRN 250 260 270 280 290 300 GGICVANHTS PIDVIILASD GYYAMVGQVH GGLMGVIQRA MVKACPHVWF ERSEVKDRHL 310 320 330 340 350 360 VAKRLTEHVQ DKSKLPILIF PEGTCINNTS VMMFKKGSFE IGATVYPVAI KYDPQFGDAF 370 380 390 400 410 420 WNSSKYGMVT YLLRMMTSWA IVCSVWYLPP MTREADEDAV QFANRVKSAI ARQGGLVDLL 430 440 450 WDGGLKREKV KDTFKEEQQK LYSKMIVGNH KDRSRS

References

[1]	The German cDNA consortium Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR860492 mRNA. Translation: CAH92613.1. Different initiation.
RefSeq	NP_001126531.1.
UniGene	Pab.8134
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	100173520.
Organism-specific databases
CTD	100173520.
Phylogenomic databases
HOVERGEN	Q5R6J7.
Enzyme and pathway databases
BRENDA	2.3.1.51. 269192.
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_PONAB

Accession

Primary (citable) accession number: Q5R6J7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	June 21, 2005
Last modified:	October 13, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)