Reviewed, UniProtKB/Swiss-Prot O15228 (GNPAT_HUMAN)

Names and origin

Protein names

Recommended name:
    Dihydroxyacetone phosphate acyltransferase
      Short name=DHAP-AT
      Short name=DAP-AT
    EC=2.3.1.42
Alternative name(s):
    Glycerone-phosphate O-acyltransferase
    Acyl-CoA:dihydroxyacetonephosphateacyltransferase

Gene names

Name:	GNPAT
Synonyms:	DAPAT, DHAPAT

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	680 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + glycerone phosphate = CoA + acylglycerone phosphate.
Pathway	Membrane lipid metabolism; glycerophospholipid metabolism.
Subunit structure	May be part of an heterotrimeric complex composed of DAP-AT, ADAP-S and a modified form of DAP-AT.
Subcellular location	Peroxisome membrane; Peripheral membrane protein; Matrix side By similarity. Note: Exclusively localized to the lumenal side of the peroxisomal membrane 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.
Involvement in disease	Defects in GNPAT are the cause of rhizomelic chondrodysplasia punctata type 2 (RCDP2) [MIM:222765]. RDCP2 is characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation. Ref.2 Ref.8
Sequence similarities	Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
Cellular component	Membrane Peroxisome
Disease	Cataract Disease mutation Dwarfism Rhizomelic chondrodysplasia punctata
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	fatty acid metabolic process Ref.1 Traceable author statement. Source: ProtInc organ morphogenesis Ref.2 Traceable author statement. Source: ProtInc
Cellular component	extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell peroxisome Ref.1 Traceable author statement. Source: ProtInc
Molecular function	glycerone-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 – 680	680	Dihydroxyacetone phosphate acyltransferase		PRO_0000195246
Regions
	Motif	162 – 167	6	HXXXXD motif
	Motif	678 – 680	3	Microbody targeting signal Potential
	Compositional bias	3 – 9	7	Poly-Ser
Amino acid modifications
	Modified residue	643	1	N6-acetyllysine Ref.7
Natural variations
	Natural variant	211	1	R → C in RCDP2. dbSNP rs28939697. Ref.2		VAR_006357
	Natural variant	211	1	R → H in RCDP2; complete loss of activity. dbSNP rs28939696. Ref.2 Ref.8		VAR_006358
	Natural variant	495	1	V → I: dbSNP rs11122266.		VAR_030696
	Natural variant	519	1	D → G in RCDP2; 70% reduction in activity. dbSNP rs11558492. Ref.8		VAR_025897
	Natural variant	586	1	Y → H: dbSNP rs17849315. Ref.5		VAR_030697
Experimental info
	Sequence conflict	26	1	S → K AA sequence Ref.2
	Sequence conflict	31	1	K → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O15228-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: BDF624CCD4D92477	FASTA	680	77,188
	10 20 30 40 50 60 MESSSSSNSY FSVGPTSPSA VVLLYSKELK KWDEFEDILE ERRHVSDLKF AMKCYTPLVY 70 80 90 100 110 120 KGITPCKPID IKCSVLNSEE IHYVIKQLSK ESLQSVDVLR EEVSEILDEM SHKLRLGAIR 130 140 150 160 170 180 FCAFTLSKVF KQIFSKVCVN EEGIQKLQRA IQEHPVVLLP SHRSYIDFLM LSFLLYNYDL 190 200 210 220 230 240 PVPVIAAGMD FLGMKMVGEL LRMSGAFFMR RTFGGNKLYW AVFSEYVKTM LRNGYAPVEF 250 260 270 280 290 300 FLEGTRSRSA KTLTPKFGLL NIVMEPFFKR EVFDTYLVPI SISYDKILEE TLYVYELLGV 310 320 330 340 350 360 PKPKESTTGL LKARKILSEN FGSIHVYFGD PVSLRSLAAG RMSRSSYNLV PRYIPQKQSE 370 380 390 400 410 420 DMHAFVTEVA YKMELLQIEN MVLSPWTLIV AVLLQNRPSM DFDALVEKTL WLKGLTQAFG 430 440 450 460 470 480 GFLIWPDNKP AEEVVPASIL LHSNIASLVK DQVILKVDSG DSEVVDGLML QHITLLMCSA 490 500 510 520 530 540 YRNQLLNIFV RPSLVAVALQ MTPGFRKEDV YSCFRFLRDV FADEFIFLPG NTLKDFEEGC 550 560 570 580 590 600 YLLCKSEAIQ VTTKDILVTE KGNTVLEFLV GLFKPFVESY QIICKYLLSE EEDHFSEEQY 610 620 630 640 650 660 LAAVRKFTSQ LLDQGTSQCY DVLSSDVQKN ALAACVRLGV VEKKKINNNC IFNVNEPATT 670 680 KLEEMLGCKT PIGKPATAKL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ether lipid biosynthesis: isolation and molecular characterization of human dihydroxyacetonephosphate acyltransferase." Thai T.-P., Heid H., Rackwitz H.-R., Hunziker A., Gorgas K., Just W.W. FEBS Lett. 420:205-211(1997) [PubMed: 9459311] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"Acyl-CoA:dihydroxyacetonephosphate acyltransferase: cloning of the human cDNA and resolution of the molecular basis in rhizomelic chondrodysplasia punctata type 2." Ofman R., Hettema E.H., Hogenhout E.M., Caruso U., Muijsers A.O., Wanders R.J.A. Hum. Mol. Genet. 7:847-853(1998) [PubMed: 9536089] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 12-33, VARIANTS RCDP2 CYS-211 AND HIS-211.
[3]	"Etherphospholipid biosynthesis and dihydroxyactetone-phosphate acyltransferase: resolution of the genomic organization of the human GNPAT gene and its use in the identification of novel mutations." Ofman R., Lajmir S., Wanders R.J.A. Biochem. Biophys. Res. Commun. 281:754-760(2001) [PubMed: 11237722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANT HIS-586. Tissue: Lung.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-643, MASS SPECTROMETRY.
[8]	"Impaired membrane traffic in defective ether lipid biosynthesis." Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K., Just W.W. Hum. Mol. Genet. 10:127-136(2001) [PubMed: 11152660] [Abstract] Cited for: VARIANTS RCDP2 HIS-211 AND GLY-519, CHARACTERIZATION OF VARIANTS RCDP2 HIS-211 AND GLY-519.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ002190 mRNA. Translation: CAA05242.1. AF043937 mRNA. Translation: AAC24505.1. AF218233 , AF218223, AF218224, AF218225, AF218226, AF218227, AF218228, AF218229, AF218230, AF218231, AF218232 Genomic DNA. Translation: AAG17547.1. AL137801, AL117352 Genomic DNA. Translation: CAI21988.1. AL117352, AL137801 Genomic DNA. Translation: CAI23094.1. BC000450 mRNA. Translation: AAH00450.1.
IPI	IPI00005677.
RefSeq	NP_055051.1.
UniGene	Hs.498028
3D structure databases
SMR	O15228. Positions 140-340.
ModBase	Search...
Protein-protein interaction databases
IntAct	O15228. 2 interactions.
STRING	O15228.
PTM databases
PhosphoSite	O15228.
Proteomic databases
PRIDE	O15228.
Genome annotation databases
Ensembl	ENST00000366647; ENSP00000355607; ENSG00000116906; Homo sapiens. [Genome view]
GeneID	8443.
KEGG	hsa:8443.
NMPDR	fig|9606.3.peg.3243.
UCSC	uc001hup.2. human.
Organism-specific databases
CTD	8443.
GeneCards	GC01P229443.
H-InvDB	HIX0001692.
HGNC	HGNC:4416. GNPAT.
MIM	222765. phenotype. 602744. gene.
Orphanet	177. Chondrodysplasia punctata, rhizomelic type.
PharmGKB	PA28795.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07351.
HOVERGEN	O15228.
InParanoid	O15228.
OMA	APWYDER.
OrthoDB	EOG9JWZ0T.
PhylomeDB	O15228.
Enzyme and pathway databases
BRENDA	2.3.1.42. 247.
Reactome	REACT_602. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	O15228.
Bgee	O15228.
CleanEx	HS_GNPAT.
Genevestigator	O15228.
GermOnline	ENSG00000116906. Homo sapiens.
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	31586.
SOURCE	Search...

Entry information

Entry name

GNPAT_HUMAN

Accession

Primary (citable) accession number: O15228
Secondary accession number(s): Q5TBH7, Q9BWC2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 1, 1998
Last modified:	February 9, 2010
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.