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Q8C0I1 (ADAS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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):
Alkylglycerone-phosphate synthase
Gene names
Name:Agps
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

FAD By similarity.

Pathway

Glycerolipid metabolism; ether lipid biosynthesis.

Subcellular location

Peroxisome By similarity.

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 – 4545Peroxisome By similarity
Chain46 – 645600Alkyldihydroxyacetonephosphate synthase, peroxisomal
PRO_0000231676

Regions

Domain189 – 371183FAD-binding PCMH-type

Sites

Active site5651 By similarity

Amino acid modifications

Modified residue521Phosphoserine Ref.4
Modified residue571Phosphoserine Ref.3 Ref.4
Modified residue891N6-acetyllysine By similarity
Modified residue1561N6-acetyllysine By similarity
Modified residue3341N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C0I1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: EED5030FB7BA4A8B

FASTA64571,684
        10         20         30         40         50         60 
MAEAAAGEAG ASERDPDAGR ARRRLRVLSG HLLGRPQEAP STNECKARRA ASAAGASPAA 

        70         80         90        100        110        120 
TPAAPESGTI PKKRQEVMKW NGWGYNDSKF LLNKKGQVEL TGKRYPLSGL VLPTLRDWIQ 

       130        140        150        160        170        180 
NTLGVSLEHK TTSKTSINPS EAPPSIVNED FLQELKEARI SYSQEADDRV FRAHGHCLHE 

       190        200        210        220        230        240 
IFLLREGMFE RIPDIVVWPT CHDDVVKIVN LACKYNLCII PIGGGTSVSY GLMCPADETR 

       250        260        270        280        290        300 
TIISLDTSQM NRILWVDENN LTAHVEAGIT GQDLERQLKE SGYCTGHEPD SLEFSTVGGW 

       310        320        330        340        350        360 
ISTRASGMKK NIYGNIEDLV VHMKMVTPRG VIEKSSQGPR MSTGPDIHHF IMGSEGTLGV 

       370        380        390        400        410        420 
ITEATIKIRP TPEYQKYGSV AFPNFEQGVA CLREIAKQRC APASIRLMDN QQFQFGHALK 

       430        440        450        460        470        480 
PQVSSIFTSF LDGLKKFYIT KFKGFDPNQI SVATLLFEGD REKVLQHEKQ VYDIAAKFGG 

       490        500        510        520        530        540 
LAAGEDNGQR GYLLTYVIAY IRDLGLEYYV IGESFETSAP WDRVIDLCRN VKERIRRECK 

       550        560        570        580        590        600 
ERGVQFAPLS TCRVTQTYDA GACIYFYFAF NYRGISDPLT VFEHTEAAAR EEILANGGSL 

       610        620        630        640 
SHHHGVGKIR KQWLKESISD VGFGMLKSVK EYVDPSNIFG NRNLL

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Embryo.
[3]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed: 15345747] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, MASS SPECTROMETRY.
Tissue: Embryonic brain.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-57, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK031049 mRNA. Translation: BAC27229.1.
BC063086 mRNA. Translation: AAH63086.1.
IPIIPI00223818.
RefSeqNP_766254.2. NM_172666.3.
UniGeneMm.31227.

3D structure databases

ProteinModelPortalQ8C0I1.
SMRQ8C0I1. Positions 69-644.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8C0I1.

PTM databases

PhosphoSiteQ8C0I1.

Proteomic databases

PRIDEQ8C0I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000111951; ENSMUSP00000107582; ENSMUSG00000042410.
GeneID228061.
KEGGmmu:228061.

Organism-specific databases

CTD8540.
MGIMGI:2443065. Agps.

Phylogenomic databases

GeneTreeENSGT00530000063515.
HOVERGENHBG004179.
InParanoidQ8C0I1.
OrthoDBEOG44XJGD.
PhylomeDBQ8C0I1.

Gene expression databases

ArrayExpressQ8C0I1.
BgeeQ8C0I1.
CleanExMM_AGPS.
GenevestigatorQ8C0I1.
GermOnlineENSMUSG00000042410. Mus musculus.

Family and domain databases

InterProIPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR016164. FAD-linked_Oxase-like_C.
IPR016168. FAD-linked_Oxase_FAD-bd_sub2.
IPR004113. FAD-linked_oxidase_C.
IPR006094. Oxid_FAD_bind_N.
[Graphical view]
Gene3DG3DSA:3.30.43.10. FAD-binding_2_sub1. 1 hit.
G3DSA:3.30.465.20. FAD-linked_oxidase_FAD-bd_sub2. 1 hit.
KOK00803.
PfamPF02913. FAD-oxidase_C. 1 hit.
PF01565. FAD_binding_4. 1 hit.
[Graphical view]
SUPFAMSSF55103. FAD-binding_2. 1 hit.
SSF56176. FAD-binding_2. 1 hit.
PROSITEPS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio378913.
SOURCESearch...

Entry information

Entry nameADAS_MOUSE
AccessionPrimary (citable) accession number: Q8C0I1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2003
Last modified: November 16, 2011
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents