[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; DOI=10.1016/S0005-2760(97)00014-3; PubMed=9187299 [NCBI, ExPASy, EBI, Israel, Japan] de Vet E.C.J.M., van den Broek B.T.E., van den Bosch H.; "Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2."; Biochim. Biophys. Acta 1346:25-29(1997).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Kim J.W.; "Identification of a human aging-associated gene."; Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[3]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.
[4]	VARIANT RCDP3 HIS-419. DOI=10.1074/jbc.273.17.10296; PubMed=9553082 [NCBI, ExPASy, EBI, Israel, Japan] de Vet E.C.J.M., Ijlst L., Oostheim W., Wanders R.J.A., van den Bosch H.; "Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency."; J. Biol. Chem. 273:10296-10301(1998).
[5]	VARIANTS RCDP3 ILE-309 AND PRO-469. DOI=10.1093/hmg/10.2.127; PubMed=11152660 [NCBI, ExPASy, EBI, Israel, Japan] Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K., Just W.W.; "Impaired membrane traffic in defective ether lipid biosynthesis."; Hum. Mol. Genet. 10:127-136(2001).

Comments

CATALYTIC ACTIVITY: 1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.
COFACTOR: FAD.
PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis .
SUBUNIT: May be part of an heterotrimeric complex composed of DAP-AT, ADAP-S and a modified form of DAP-AT.
SUBCELLULAR LOCATION: Peroxisome membrane. Note=Localized to the inner aspect of the peroxisomal membrane.
DISEASE: Defects in AGPS are the cause of rhizomelic chondrodysplasia punctata type 3 (RCDP3) [MIM:600121]. RCDP3 is characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation.
SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=AGPS";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y09443; CAA70591.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY544121; AAT11152.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00010349; -.

NP_003650.1; -.

3D structure databases

ModBase

O00116.

PTM databases

PhosphoSite

O00116; -.

Enzyme and pathway databases

BRENDA

2.5.1.26; 247.

Reactome

REACT_1407; Synthesis of lysophosphatidic acid from dihydroxyacetone phosphate.

Organism-specific databases

GC02P177965; -.

HIX0029990; -.

HGNC:327; AGPS.

600121; phenotype. [NCBI / EBI]
603051; gene. [NCBI / EBI]

Orphanet

177; Chondrodysplasia punctata, rhizomelic type.

PharmGKB

PA24624; -.

Gene expression databases

O00116; -.

O00116; -.

HS_AGPS; -.

ENSG00000018510; Homo sapiens.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005778;	Cellular component: peroxisomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0008609;	Molecular function: alkylglycerone-phosphate synthase activity (inferred from direct assay from MGI).
GO:0050660;	Molecular function: FAD binding (inferred from electronic annotation from InterPro).
GO:0016491;	Molecular function: oxidoreductase activity (inferred from electronic annotation from InterPro).
GO:0008610;	Biological process: lipid biosynthetic process (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR016166; FAD-bd_2.
IPR016167; FAD-bd_2_sub1.
IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
IPR004113; FAD-linked_oxidase_C.
IPR006094; Oxid_FAD_bind_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.

Pfam

PF02913; FAD-oxidase_C; 1.
PF01565; FAD_binding_4; 1.
Pfam graphical view of domain structure.

PROSITE

PS51387; FAD_PCMH; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

O00116; -.

PRIDE

O00116; -.

Genome annotation databases

Ensembl

ENSG00000018510; Homo sapiens. [Contig view]

GeneID

8540; -.

KEGG

hsa:8540; -.

Phylogenomic databases

HOGENOM

O00116; -.

HOVERGEN

O00116; -.

OMA

O00116; FFFNKKG.

Other

31988; -.

AGPS; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cataract; Disease mutation; Dwarfism; FAD; Flavoprotein; Lipid synthesis; Membrane; Peroxisome; Phosphoprotein; Rhizomelic chondrodysplasia punctata; Transferase; Transit peptide.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 58`	`58`	`Peroxisome (By similarity).`
`CHAIN`	`59 658`	`600`	`Alkyldihydroxyacetonephosphate synthase, peroxisomal.`	`PRO_0000020431`
`DOMAIN`	`202 384`	`183`	`FAD-binding PCMH-type.`
`COMPBIAS`	`2 8`	`7`	`Poly-Ala.`
`ACT_SITE`	`578 578`		`By similarity.`
`MOD_RES`	`65 65`		`Phosphoserine (By similarity).`
`VARIANT`	`309 309`	`1`	`T -> I (in RCDP3).`	`VAR_025895`
`VARIANT`	`419 419`	`1`	`R -> H (in RCDP3).`	`VAR_005002`
`VARIANT`	`469 469`	`1`	`L -> P (in RCDP3).`	`VAR_025896`

Sequence information

Length: 658 AA [This is the length of the unprocessed precursor]

Molecular weight: 72912 Da [This is the MW of the unprocessed precursor]

CRC64: 0E97AE86B513DF32 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAEAAAAAGG TGLGAGASYG SAADRDRDPD PDRAGRRLRV LSGHLLGRPR EALSTNECKA 

        70         80         90        100        110        120 
RRAASAATAA PTATPAAQES GTIPKKRQEV MKWNGWGYND SKFIFNKKGQ IELTGKRYPL 

       130        140        150        160        170        180 
SGMGLPTFKE WIQNTLGVNV EHKTTSKASL NPSDTPPSVV NEDFLHDLKE TNISYSQEAD 

       190        200        210        220        230        240 
DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS 

       250        260        270        280        290        300 
VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH 

       310        320        330        340        350        360 
EPDSLEFSTV GGWVSTRASG MKKNIYGNIE DLVVHIKMVT PRGIIEKSCQ GPRMSTGPDI 

       370        380        390        400        410        420 
HHFIMGSEGT LGVITEATIK IRPVPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL 

       430        440        450        460        470        480 
MDNKQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH 

       490        500        510        520        530        540 
EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYIRDLALE YYVLGESFET SAPWDRVVDL 

       550        560        570        580        590        600 
CRNVKERITR ECKEKGVQFA PFSTCRVTQT YDAGACIYFY FAFNYRGISD PLTVFEQTEA 

       610        620        630        640        650 
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKEYVDPNN IFGNRNLL

O00116 in FASTA format

View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools