O00116 (ADAS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alkyldihydroxyacetonephosphate synthase, peroxisomal
Short name=Alkyl-DHAP synthase
EC=2.5.1.26

Alternative name(s):
Aging-associated gene 5 protein
Alkylglycerone-phosphate synthase

Gene names

Name:	AGPS
ORF Names:	AAG5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	658 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids By similarity.
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 structure	Homodimer By similarity.
Subcellular location	Peroxisome membrane. Note: Localized to the inner aspect of the peroxisomal membrane.
Involvement in disease	Rhizomelic chondrodysplasia punctata 3 (RCDP3) [MIM:600121]: A disease characterized by rhizomelic shortening of femur and humerus, vertebral disorders, cataract, cutaneous lesions and severe mental retardation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10
Sequence similarities	Belongs to the FAD-binding oxidoreductase/transferase type 4 family. Contains 1 FAD-binding PCMH-type domain.

Ontologies

Keywords
Biological process	Lipid biosynthesis Lipid metabolism
Cellular component	Membrane Peroxisome
Disease	Cataract Disease mutation Dwarfism Rhizomelic chondrodysplasia punctata
Domain	Transit peptide
Ligand	FAD Flavoprotein
Molecular function	Transferase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ether lipid biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal matrix Traceable author statement. Source: Reactome peroxisomal membrane Inferred from direct assay PubMed 21525035. Source: UniProtKB
Molecular_function	FAD binding Inferred from sequence or structural similarity. Source: UniProtKB UDP-N-acetylmuramate dehydrogenase activity Inferred from electronic annotation. Source: InterPro alkylglycerone-phosphate synthase activity Inferred from direct assay PubMed 10415121. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 58	58	Peroxisome By similarity
	Chain	59 – 658	600	Alkyldihydroxyacetonephosphate synthase, peroxisomal		PRO_0000020431
Regions
	Domain	202 – 384	183	FAD-binding PCMH-type
	Nucleotide binding	234 – 240	7	FAD By similarity
	Nucleotide binding	303 – 309	7	FAD By similarity
	Nucleotide binding	316 – 319	4	FAD By similarity
	Nucleotide binding	368 – 374	7	FAD By similarity
	Region	615 – 617	3	Important for enzyme activity By similarity
	Compositional bias	2 – 8	7	Poly-Ala
Sites
	Active site	578	1	Proton donor/acceptor By similarity
	Binding site	515	1	Substrate By similarity
	Site	419	1	Important for enzyme activity By similarity
Amino acid modifications
	Modified residue	65	1	Phosphoserine By similarity
	Modified residue	102	1	N6-acetyllysine Ref.6
	Modified residue	347	1	N6-acetyllysine Ref.6
Natural variations
	Natural variant	182	1	R → Q in RCDP3; severely reduced protein levels. Ref.10		VAR_066929
	Natural variant	309	1	T → I in RCDP3. Ref.9		VAR_025895
	Natural variant	419	1	R → H in RCDP3. Ref.8		VAR_005002
	Natural variant	469	1	L → P in RCDP3. Ref.9		VAR_025896
	Natural variant	471	1	E → K in RCDP3; severely reduced protein levels. Ref.10		VAR_066930
	Natural variant	568	1	T → M in RCDP3; does not affect protein levels. Ref.10		VAR_066931

Sequences

	Sequence		Length	Mass (Da)
	O00116 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 0E97AE86B513DF32	FASTA	658	72,912
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase cDNA reveals the presence of a peroxisomal targeting signal 2." de Vet E.C.J.M., van den Broek B.T.E., van den Bosch H. Biochim. Biophys. Acta 1346:25-29(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Identification of a human aging-associated gene." Kim J.W. Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Tongue.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102 AND LYS-347, MASS SPECTROMETRY.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]	"Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome biogenesis disorders and identification of the point mutation underlying a single enzyme deficiency." de Vet E.C.J.M., Ijlst L., Oostheim W., Wanders R.J.A., van den Bosch H. J. Biol. Chem. 273:10296-10301(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT RCDP3 HIS-419.
[9]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS RCDP3 ILE-309 AND PRO-469.
[10]	"Functional characterization of novel mutations in GNPAT and AGPS, causing rhizomelic chondrodysplasia punctata (RCDP) types 2 and 3." Itzkovitz B., Jiralerspong S., Nimmo G., Loscalzo M., Horovitz D.D., Snowden A., Moser A., Steinberg S., Braverman N. Hum. Mutat. 33:189-197(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568, CHARACTERIZATION OF VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y09443 mRNA. Translation: CAA70591.1. AY544121 mRNA. Translation: AAT11152.1. AK314259 mRNA. Translation: BAG36924.1. BC141820 mRNA. Translation: AAI41821.1.
IPI	IPI00010349.
RefSeq	NP_003650.1. NM_003659.3.
UniGene	Hs.516543.
3D structure databases
ProteinModelPortal	O00116.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00116. 6 interactions.
STRING	9606.ENSP00000264167.
PTM databases
PhosphoSite	O00116.
Proteomic databases
PaxDb	O00116.
PeptideAtlas	O00116.
PRIDE	O00116.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264167; ENSP00000264167; ENSG00000018510.
GeneID	8540.
KEGG	hsa:8540.
UCSC	uc002ull.2. human.
Organism-specific databases
CTD	8540.
GeneCards	GC02P178221.
HGNC	HGNC:327. AGPS.
HPA	HPA030209. HPA030210. HPA030211.
MIM	600121. phenotype. 603051. gene.
neXtProt	NX_O00116.
Orphanet	177. Rhizomelic chondrodysplasia punctata.
PharmGKB	PA24624.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0277.
HOGENOM	HOG000231620.
HOVERGEN	HBG004179.
InParanoid	O00116.
KO	K00803.
OMA	YLRDLGM.
OrthoDB	EOG44XJGD.
PhylomeDB	O00116.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
UniPathway	UPA00781.
Gene expression databases
ArrayExpress	O00116.
Bgee	O00116.
CleanEx	HS_AGPS.
Genevestigator	O00116.
GermOnline	ENSG00000018510. Homo sapiens.
Family and domain databases
Gene3D	3.30.43.10. 1 hit. 3.30.465.10. 1 hit.
InterPro	IPR025650. Alkyl-DHAP_Synthase. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR016167. FAD-bd_2_sub1. IPR016164. FAD-linked_Oxase-like_C. IPR004113. FAD-linked_oxidase_C. IPR006094. Oxid_FAD_bind_N. [Graphical view]
PANTHER	PTHR11748:SF3. PTHR11748:SF3. 1 hit.
Pfam	PF02913. FAD-oxidase_C. 1 hit. PF01565. FAD_binding_4. 1 hit. [Graphical view]
SUPFAM	SSF55103. FAD-binding_2. 1 hit. SSF56176. FAD-binding_2. 1 hit.
PROSITE	PS51387. FAD_PCMH. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	AGPS. human.
GenomeRNAi	8540.
NextBio	31988.
SOURCE	Search...

Entry information

Entry name

ADAS_HUMAN

Accession

Primary (citable) accession number: O00116
Secondary accession number(s): A5D8U9, Q2TU35

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.