ID   ADAS_HUMAN              Reviewed;         658 AA.
AC   O00116; A5D8U9; Q2TU35;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-JAN-2012, entry version 104.
DE   RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE            Short=Alkyl-DHAP synthase;
DE            EC=2.5.1.26;
DE   AltName: Full=Aging-associated gene 5 protein;
DE   AltName: Full=Alkylglycerone-phosphate synthase;
DE   Flags: Precursor;
GN   Name=AGPS; ORFNames=AAG5;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RX   MEDLINE=97330864; PubMed=9187299; DOI=10.1016/S0005-2760(97)00014-3;
RA   de Vet E.C.J.M., van den Broek B.T.E., van den Bosch H.;
RT   "Nucleotide sequence of human alkyl-dihydroxyacetonephosphate synthase
RT   cDNA reveals the presence of a peroxisomal targeting signal 2.";
RL   Biochim. Biophys. Acta 1346:25-29(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of a human aging-associated gene.";
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tongue;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-102; LYS-169 AND LYS-347,
RP   AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7]
RP   VARIANT RCDP3 HIS-419.
RX   MEDLINE=98221159; PubMed=9553082; DOI=10.1074/jbc.273.17.10296;
RA   de Vet E.C.J.M., Ijlst L., Oostheim W., Wanders R.J.A.,
RA   van den Bosch H.;
RT   "Alkyl-dihydroxyacetonephosphate synthase. Fate in peroxisome
RT   biogenesis disorders and identification of the point mutation
RT   underlying a single enzyme deficiency.";
RL   J. Biol. Chem. 273:10296-10301(1998).
RN   [8]
RP   VARIANTS RCDP3 ILE-309 AND PRO-469.
RX   PubMed=11152660; DOI=10.1093/hmg/10.2.127;
RA   Thai T.P., Rodemer C., Jauch A., Hunziker A., Moser A., Gorgas K.,
RA   Just W.W.;
RT   "Impaired membrane traffic in defective ether lipid biosynthesis.";
RL   Hum. Mol. Genet. 10:127-136(2001).
RN   [9]
RP   VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568, AND CHARACTERIZATION OF
RP   VARIANTS RCDP3 GLN-182; LYS-471 AND MET-568.
RX   PubMed=21990100; DOI=10.1002/humu.21623;
RA   Itzkovitz B., Jiralerspong S., Nimmo G., Loscalzo M., Horovitz D.D.,
RA   Snowden A., Moser A., Steinberg S., Braverman N.;
RT   "Functional characterization of novel mutations in GNPAT and AGPS,
RT   causing rhizomelic chondrodysplasia punctata (RCDP) types 2 and 3.";
RL   Hum. Mutat. 0:0-0(2011).
CC   -!- CATALYTIC ACTIVITY: 1-acyl-glycerone 3-phosphate + a long-chain
CC       alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid
CC       anion.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC   -!- SUBUNIT: May be part of an heterotrimeric complex composed of DAP-
CC       AT, ADAP-S and a modified form of DAP-AT.
CC   -!- SUBCELLULAR LOCATION: Peroxisome membrane. Note=Localized to the
CC       inner aspect of the peroxisomal membrane.
CC   -!- DISEASE: Defects in AGPS are the cause of rhizomelic
CC       chondrodysplasia punctata type 3 (RCDP3) [MIM:600121]. RCDP3 is
CC       characterized by rhizomelic shortening of femur and humerus,
CC       vertebral disorders, cataract, cutaneous lesions and severe mental
CC       retardation.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase
CC       type 4 family.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
CC   -!- WEB RESOURCE: Name=GeneReviews;
CC       URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/AGPS";
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DR   EMBL; Y09443; CAA70591.1; -; mRNA.
DR   EMBL; AY544121; AAT11152.1; -; mRNA.
DR   EMBL; AK314259; BAG36924.1; -; mRNA.
DR   EMBL; BC141820; AAI41821.1; -; mRNA.
DR   IPI; IPI00010349; -.
DR   RefSeq; NP_003650.1; NM_003659.3.
DR   UniGene; Hs.516543; -.
DR   ProteinModelPortal; O00116; -.
DR   SMR; O00116; 82-657.
DR   IntAct; O00116; 3.
DR   STRING; O00116; -.
DR   PhosphoSite; O00116; -.
DR   PeptideAtlas; O00116; -.
DR   PRIDE; O00116; -.
DR   Ensembl; ENST00000264167; ENSP00000264167; ENSG00000018510.
DR   GeneID; 8540; -.
DR   KEGG; hsa:8540; -.
DR   UCSC; uc002ull.2; human.
DR   CTD; 8540; -.
DR   GeneCards; GC02P178221; -.
DR   H-InvDB; HIX0029990; -.
DR   HGNC; HGNC:327; AGPS.
DR   HPA; HPA030209; -.
DR   HPA; HPA030210; -.
DR   HPA; HPA030211; -.
DR   MIM; 600121; phenotype.
DR   MIM; 603051; gene.
DR   neXtProt; NX_O00116; -.
DR   Orphanet; 177; Chondrodysplasia punctata, rhizomelic type.
DR   PharmGKB; PA24624; -.
DR   eggNOG; prNOG05503; -.
DR   HOGENOM; HBG383004; -.
DR   HOVERGEN; HBG004179; -.
DR   InParanoid; O00116; -.
DR   OMA; YNDSKFF; -.
DR   OrthoDB; EOG44XJGD; -.
DR   PhylomeDB; O00116; -.
DR   Reactome; REACT_22258; Metabolism of lipids and lipoproteins.
DR   NextBio; 31988; -.
DR   ArrayExpress; O00116; -.
DR   Bgee; O00116; -.
DR   CleanEx; HS_AGPS; -.
DR   Genevestigator; O00116; -.
DR   GermOnline; ENSG00000018510; Homo sapiens.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; IDA:MGI.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0008611; P:ether lipid biosynthetic process; TAS:Reactome.
DR   InterPro; IPR016166; FAD-bd_2.
DR   InterPro; IPR016167; FAD-bd_2_sub1.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR016168; FAD-linked_Oxase_FAD-bd_sub2.
DR   InterPro; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Gene3D; G3DSA:3.30.43.10; FAD-binding_2_sub1; 1.
DR   Gene3D; G3DSA:3.30.465.20; FAD-linked_oxidase_FAD-bd_sub2; 1.
DR   Gene3D; G3DSA:1.10.45.10; Vanillyl_alc_oxidase_C-sub2; 1.
DR   KO; K00803; -.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; FAD-binding_2; 1.
DR   SUPFAM; SSF56176; FAD-binding_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cataract; Complete proteome; Disease mutation; Dwarfism;
KW   FAD; Flavoprotein; Lipid synthesis; Membrane; Peroxisome;
KW   Phosphoprotein; Reference proteome;
KW   Rhizomelic chondrodysplasia punctata; Transferase; Transit peptide.
FT   TRANSIT       1     58       Peroxisome (By similarity).
FT   CHAIN        59    658       Alkyldihydroxyacetonephosphate synthase,
FT                                peroxisomal.
FT                                /FTId=PRO_0000020431.
FT   DOMAIN      202    384       FAD-binding PCMH-type.
FT   COMPBIAS      2      8       Poly-Ala.
FT   ACT_SITE    578    578       By similarity.
FT   MOD_RES      65     65       Phosphoserine (By similarity).
FT   MOD_RES     102    102       N6-acetyllysine.
FT   MOD_RES     169    169       N6-acetyllysine.
FT   MOD_RES     347    347       N6-acetyllysine.
FT   VARIANT     182    182       R -> Q (in RCDP3; severely reduced
FT                                protein levels).
FT                                /FTId=VAR_066929.
FT   VARIANT     309    309       T -> I (in RCDP3).
FT                                /FTId=VAR_025895.
FT   VARIANT     419    419       R -> H (in RCDP3).
FT                                /FTId=VAR_005002.
FT   VARIANT     469    469       L -> P (in RCDP3).
FT                                /FTId=VAR_025896.
FT   VARIANT     471    471       E -> K (in RCDP3; severely reduced
FT                                protein levels).
FT                                /FTId=VAR_066930.
FT   VARIANT     568    568       T -> M (in RCDP3; does not affect protein
FT                                levels).
FT                                /FTId=VAR_066931.
SQ   SEQUENCE   658 AA;  72912 MW;  0E97AE86B513DF32 CRC64;
     MAEAAAAAGG TGLGAGASYG SAADRDRDPD PDRAGRRLRV LSGHLLGRPR EALSTNECKA
     RRAASAATAA PTATPAAQES GTIPKKRQEV MKWNGWGYND SKFIFNKKGQ IELTGKRYPL
     SGMGLPTFKE WIQNTLGVNV EHKTTSKASL NPSDTPPSVV NEDFLHDLKE TNISYSQEAD
     DRVFRAHGHC LHEIFLLREG MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS
     VSYGLMCPAD ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
     EPDSLEFSTV GGWVSTRASG MKKNIYGNIE DLVVHIKMVT PRGIIEKSCQ GPRMSTGPDI
     HHFIMGSEGT LGVITEATIK IRPVPEYQKY GSVAFPNFEQ GVACLREIAK QRCAPASIRL
     MDNKQFQFGH ALKPQVSSIF TSFLDGLKKF YITKFKGFDP NQLSVATLLF EGDREKVLQH
     EKQVYDIAAK FGGLAAGEDN GQRGYLLTYV IAYIRDLALE YYVLGESFET SAPWDRVVDL
     CRNVKERITR ECKEKGVQFA PFSTCRVTQT YDAGACIYFY FAFNYRGISD PLTVFEQTEA
     AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKEYVDPNN IFGNRNLL
//