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O00116

- ADAS_HUMAN

UniProt

O00116 - ADAS_HUMAN

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Protein

Alkyldihydroxyacetonephosphate synthase, peroxisomal

Gene

AGPS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 activityi

1-acyl-glycerone 3-phosphate + a long-chain alcohol = an alkyl-glycerone 3-phosphate + a long-chain acid anion.

Cofactori

FAD.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei419 – 4191Important for enzyme activityBy similarity
Binding sitei515 – 5151SubstrateBy similarity
Active sitei578 – 5781Proton donor/acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi234 – 2407FADBy similarity
Nucleotide bindingi303 – 3097FADBy similarity
Nucleotide bindingi316 – 3194FADBy similarity
Nucleotide bindingi368 – 3747FADBy similarity

GO - Molecular functioni

  1. alkylglycerone-phosphate synthase activity Source: UniProtKB
  2. FAD binding Source: UniProtKB
  3. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro

GO - Biological processi

  1. cellular lipid metabolic process Source: Reactome
  2. ether lipid biosynthetic process Source: UniProtKB
  3. lipid biosynthetic process Source: MGI
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_1407. Plasmalogen biosynthesis.
UniPathwayiUPA00781.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyldihydroxyacetonephosphate synthase, peroxisomal (EC:2.5.1.26)
Short name:
Alkyl-DHAP synthase
Alternative name(s):
Aging-associated gene 5 protein
Alkylglycerone-phosphate synthase
Gene namesi
Name:AGPS
ORF Names:AAG5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:327. AGPS.

Subcellular locationi

Peroxisome membrane
Note: Localized to the inner aspect of the peroxisomal membrane.

GO - Cellular componenti

  1. intracellular membrane-bounded organelle Source: HPA
  2. membrane Source: UniProtKB
  3. mitochondrion Source: UniProt
  4. nucleolus Source: HPA
  5. peroxisomal matrix Source: Reactome
  6. peroxisomal membrane Source: UniProtKB
  7. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Peroxisome

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821R → Q in RCDP3; severely reduced protein levels. 1 Publication
VAR_066929
Natural varianti309 – 3091T → I in RCDP3. 1 Publication
VAR_025895
Natural varianti419 – 4191R → H in RCDP3. 1 Publication
VAR_005002
Natural varianti469 – 4691L → P in RCDP3. 1 Publication
VAR_025896
Natural varianti471 – 4711E → K in RCDP3; severely reduced protein levels. 1 Publication
VAR_066930
Natural varianti568 – 5681T → M in RCDP3; does not affect protein levels. 1 Publication
VAR_066931

Keywords - Diseasei

Cataract, Disease mutation, Dwarfism, Rhizomelic chondrodysplasia punctata

Organism-specific databases

MIMi600121. phenotype.
Orphaneti309803. Rhizomelic chondrodysplasia punctata type 3.
PharmGKBiPA24624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5858PeroxisomeBy similarityAdd
BLAST
Chaini59 – 658600Alkyldihydroxyacetonephosphate synthase, peroxisomalPRO_0000020431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysine1 Publication
Modified residuei347 – 3471N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00116.
PaxDbiO00116.
PeptideAtlasiO00116.
PRIDEiO00116.

PTM databases

PhosphoSiteiO00116.

Expressioni

Gene expression databases

BgeeiO00116.
CleanExiHS_AGPS.
ExpressionAtlasiO00116. baseline and differential.
GenevestigatoriO00116.

Organism-specific databases

HPAiHPA030209.
HPA030210.
HPA030211.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi114110. 18 interactions.
IntActiO00116. 7 interactions.
STRINGi9606.ENSP00000264167.

Structurei

3D structure databases

ProteinModelPortaliO00116.
SMRiO00116. Positions 81-658.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini202 – 384183FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni615 – 6173Important for enzyme activityBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 87Poly-Ala

Sequence similaritiesi

Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0277.
GeneTreeiENSGT00530000063515.
HOGENOMiHOG000231620.
HOVERGENiHBG004179.
InParanoidiO00116.
KOiK00803.
OMAiSSALECP.
OrthoDBiEOG7DRJ2W.
PhylomeDBiO00116.
TreeFamiTF313830.

Family and domain databases

Gene3Di3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProiIPR025650. 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]
PANTHERiPTHR11748:SF3. PTHR11748:SF3. 1 hit.
PfamiPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMiSSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEiPS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00116 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAEAAAAAGG TGLGAGASYG SAADRDRDPD PDRAGRRLRV LSGHLLGRPR
60 70 80 90 100
EALSTNECKA RRAASAATAA PTATPAAQES GTIPKKRQEV MKWNGWGYND
110 120 130 140 150
SKFIFNKKGQ IELTGKRYPL SGMGLPTFKE WIQNTLGVNV EHKTTSKASL
160 170 180 190 200
NPSDTPPSVV NEDFLHDLKE TNISYSQEAD DRVFRAHGHC LHEIFLLREG
210 220 230 240 250
MFERIPDIVL WPTCHDDVVK IVNLACKYNL CIIPIGGGTS VSYGLMCPAD
260 270 280 290 300
ETRTIISLDT SQMNRILWVD ENNLTAHVEA GITGQELERQ LKESGYCTGH
310 320 330 340 350
EPDSLEFSTV GGWVSTRASG MKKNIYGNIE DLVVHIKMVT PRGIIEKSCQ
360 370 380 390 400
GPRMSTGPDI HHFIMGSEGT LGVITEATIK IRPVPEYQKY GSVAFPNFEQ
410 420 430 440 450
GVACLREIAK QRCAPASIRL MDNKQFQFGH ALKPQVSSIF TSFLDGLKKF
460 470 480 490 500
YITKFKGFDP NQLSVATLLF EGDREKVLQH EKQVYDIAAK FGGLAAGEDN
510 520 530 540 550
GQRGYLLTYV IAYIRDLALE YYVLGESFET SAPWDRVVDL CRNVKERITR
560 570 580 590 600
ECKEKGVQFA PFSTCRVTQT YDAGACIYFY FAFNYRGISD PLTVFEQTEA
610 620 630 640 650
AAREEILANG GSLSHHHGVG KLRKQWLKES ISDVGFGMLK SVKEYVDPNN

IFGNRNLL
Length:658
Mass (Da):72,912
Last modified:July 1, 1997 - v1
Checksum:i0E97AE86B513DF32
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821R → Q in RCDP3; severely reduced protein levels. 1 Publication
VAR_066929
Natural varianti309 – 3091T → I in RCDP3. 1 Publication
VAR_025895
Natural varianti419 – 4191R → H in RCDP3. 1 Publication
VAR_005002
Natural varianti469 – 4691L → P in RCDP3. 1 Publication
VAR_025896
Natural varianti471 – 4711E → K in RCDP3; severely reduced protein levels. 1 Publication
VAR_066930
Natural varianti568 – 5681T → M in RCDP3; does not affect protein levels. 1 Publication
VAR_066931

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09443 mRNA. Translation: CAA70591.1.
AY544121 mRNA. Translation: AAT11152.1.
AK314259 mRNA. Translation: BAG36924.1.
BC141820 mRNA. Translation: AAI41821.1.
CCDSiCCDS2275.1.
RefSeqiNP_003650.1. NM_003659.3.
UniGeneiHs.516543.

Genome annotation databases

EnsembliENST00000264167; ENSP00000264167; ENSG00000018510.
GeneIDi8540.
KEGGihsa:8540.
UCSCiuc002ull.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y09443 mRNA. Translation: CAA70591.1 .
AY544121 mRNA. Translation: AAT11152.1 .
AK314259 mRNA. Translation: BAG36924.1 .
BC141820 mRNA. Translation: AAI41821.1 .
CCDSi CCDS2275.1.
RefSeqi NP_003650.1. NM_003659.3.
UniGenei Hs.516543.

3D structure databases

ProteinModelPortali O00116.
SMRi O00116. Positions 81-658.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114110. 18 interactions.
IntActi O00116. 7 interactions.
STRINGi 9606.ENSP00000264167.

PTM databases

PhosphoSitei O00116.

Proteomic databases

MaxQBi O00116.
PaxDbi O00116.
PeptideAtlasi O00116.
PRIDEi O00116.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264167 ; ENSP00000264167 ; ENSG00000018510 .
GeneIDi 8540.
KEGGi hsa:8540.
UCSCi uc002ull.2. human.

Organism-specific databases

CTDi 8540.
GeneCardsi GC02P178221.
HGNCi HGNC:327. AGPS.
HPAi HPA030209.
HPA030210.
HPA030211.
MIMi 600121. phenotype.
603051. gene.
neXtProti NX_O00116.
Orphaneti 309803. Rhizomelic chondrodysplasia punctata type 3.
PharmGKBi PA24624.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0277.
GeneTreei ENSGT00530000063515.
HOGENOMi HOG000231620.
HOVERGENi HBG004179.
InParanoidi O00116.
KOi K00803.
OMAi SSALECP.
OrthoDBi EOG7DRJ2W.
PhylomeDBi O00116.
TreeFami TF313830.

Enzyme and pathway databases

UniPathwayi UPA00781 .
Reactomei REACT_1407. Plasmalogen biosynthesis.

Miscellaneous databases

ChiTaRSi AGPS. human.
GenomeRNAii 8540.
NextBioi 31988.
PROi O00116.
SOURCEi Search...

Gene expression databases

Bgeei O00116.
CleanExi HS_AGPS.
ExpressionAtlasi O00116. baseline and differential.
Genevestigatori O00116.

Family and domain databases

Gene3Di 3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR11748:SF3. PTHR11748:SF3. 1 hit.
Pfami PF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view ]
SUPFAMi SSF55103. SSF55103. 2 hits.
SSF56176. SSF56176. 1 hit.
PROSITEi PS51387. FAD_PCMH. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiADAS_HUMAN
AccessioniPrimary (citable) accession number: O00116
Secondary accession number(s): A5D8U9, Q2TU35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3