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O00116 (ADAS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length658 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5858Peroxisome By similarity
Chain59 – 658600Alkyldihydroxyacetonephosphate synthase, peroxisomal
PRO_0000020431

Regions

Domain202 – 384183FAD-binding PCMH-type
Nucleotide binding234 – 2407FAD By similarity
Nucleotide binding303 – 3097FAD By similarity
Nucleotide binding316 – 3194FAD By similarity
Nucleotide binding368 – 3747FAD By similarity
Region615 – 6173Important for enzyme activity By similarity
Compositional bias2 – 87Poly-Ala

Sites

Active site5781Proton donor/acceptor By similarity
Binding site5151Substrate By similarity
Site4191Important for enzyme activity By similarity

Amino acid modifications

Modified residue1021N6-acetyllysine Ref.6
Modified residue3471N6-acetyllysine Ref.6

Natural variations

Natural variant1821R → Q in RCDP3; severely reduced protein levels. Ref.10
VAR_066929
Natural variant3091T → I in RCDP3. Ref.9
VAR_025895
Natural variant4191R → H in RCDP3. Ref.8
VAR_005002
Natural variant4691L → P in RCDP3. Ref.9
VAR_025896
Natural variant4711E → K in RCDP3; severely reduced protein levels. Ref.10
VAR_066930
Natural variant5681T → M in RCDP3; does not affect protein levels. Ref.10
VAR_066931

Sequences

Sequence LengthMass (Da)Tools
O00116 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 0E97AE86B513DF32

FASTA65872,912
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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

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.
RefSeqNP_003650.1. NM_003659.3.
UniGeneHs.516543.

3D structure databases

ProteinModelPortalO00116.
SMRO00116. Positions 81-658.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114110. 14 interactions.
IntActO00116. 7 interactions.
STRING9606.ENSP00000264167.

PTM databases

PhosphoSiteO00116.

Proteomic databases

PaxDbO00116.
PeptideAtlasO00116.
PRIDEO00116.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264167; ENSP00000264167; ENSG00000018510.
GeneID8540.
KEGGhsa:8540.
UCSCuc002ull.2. human.

Organism-specific databases

CTD8540.
GeneCardsGC02P178221.
HGNCHGNC:327. AGPS.
HPAHPA030209.
HPA030210.
HPA030211.
MIM600121. phenotype.
603051. gene.
neXtProtNX_O00116.
Orphanet309803. Rhizomelic chondrodysplasia punctata type 3.
PharmGKBPA24624.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0277.
HOGENOMHOG000231620.
HOVERGENHBG004179.
InParanoidO00116.
KOK00803.
OMAYLRDLGM.
OrthoDBEOG7DRJ2W.
PhylomeDBO00116.
TreeFamTF313830.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
UniPathwayUPA00781.

Gene expression databases

ArrayExpressO00116.
BgeeO00116.
CleanExHS_AGPS.
GenevestigatorO00116.

Family and domain databases

Gene3D3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProIPR025650. 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]
PANTHERPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAGPS. human.
GenomeRNAi8540.
NextBio31988.
PROO00116.
SOURCESearch...

Entry information

Entry nameADAS_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM