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Protein

Alkyldihydroxyacetonephosphate synthase, peroxisomal

Gene

Agps

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

FADBy similarity

Pathwayi: ether lipid biosynthesis

This protein is involved in the pathway ether lipid biosynthesis, which is part of Glycerolipid metabolism.
View all proteins of this organism that are known to be involved in the pathway ether lipid biosynthesis and in Glycerolipid metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei406 – 4061Important for enzyme activityBy similarity
Binding sitei502 – 5021SubstrateBy similarity
Active sitei565 – 5651Proton donor/acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi221 – 2277FADBy similarity
Nucleotide bindingi290 – 2967FADBy similarity
Nucleotide bindingi303 – 3064FADBy similarity
Nucleotide bindingi355 – 3617FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

UniPathwayiUPA00781.

Chemistry

SwissLipidsiSLP:000000608.

Names & Taxonomyi

Protein namesi
Recommended name:
Alkyldihydroxyacetonephosphate synthase, peroxisomal (EC:2.5.1.26)
Short name:
Alkyl-DHAP synthase
Alternative name(s):
Alkylglycerone-phosphate synthase
Gene namesi
Name:Agps
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:2443065. Agps.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4545PeroxisomeBy similarityAdd
BLAST
Chaini46 – 645600Alkyldihydroxyacetonephosphate synthase, peroxisomalPRO_0000231676Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei52 – 521PhosphoserineCombined sources
Modified residuei57 – 571PhosphoserineCombined sources
Modified residuei61 – 611PhosphothreonineBy similarity
Modified residuei89 – 891N6-acetyllysineBy similarity
Modified residuei334 – 3341N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8C0I1.
MaxQBiQ8C0I1.
PaxDbiQ8C0I1.
PRIDEiQ8C0I1.

PTM databases

iPTMnetiQ8C0I1.
PhosphoSiteiQ8C0I1.

Expressioni

Gene expression databases

BgeeiQ8C0I1.
CleanExiMM_AGPS.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

IntActiQ8C0I1. 3 interactions.
MINTiMINT-4113860.
STRINGi10090.ENSMUSP00000041967.

Structurei

3D structure databases

ProteinModelPortaliQ8C0I1.
SMRiQ8C0I1. Positions 68-645.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini189 – 371183FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni602 – 6043Important for enzyme activityBy similarity

Sequence similaritiesi

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

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000231620.
HOVERGENiHBG004179.
InParanoidiQ8C0I1.
KOiK00803.

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.

Q8C0I1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEAAAGEAG ASERDPDAGR ARRRLRVLSG HLLGRPQEAP STNECKARRA
60 70 80 90 100
ASAAGASPAA TPAAPESGTI PKKRQEVMKW NGWGYNDSKF LLNKKGQVEL
110 120 130 140 150
TGKRYPLSGL VLPTLRDWIQ NTLGVSLEHK TTSKTSINPS EAPPSIVNED
160 170 180 190 200
FLQELKEARI SYSQEADDRV FRAHGHCLHE IFLLREGMFE RIPDIVVWPT
210 220 230 240 250
CHDDVVKIVN LACKYNLCII PIGGGTSVSY GLMCPADETR TIISLDTSQM
260 270 280 290 300
NRILWVDENN LTAHVEAGIT GQDLERQLKE SGYCTGHEPD SLEFSTVGGW
310 320 330 340 350
ISTRASGMKK NIYGNIEDLV VHMKMVTPRG VIEKSSQGPR MSTGPDIHHF
360 370 380 390 400
IMGSEGTLGV ITEATIKIRP TPEYQKYGSV AFPNFEQGVA CLREIAKQRC
410 420 430 440 450
APASIRLMDN QQFQFGHALK PQVSSIFTSF LDGLKKFYIT KFKGFDPNQI
460 470 480 490 500
SVATLLFEGD REKVLQHEKQ VYDIAAKFGG LAAGEDNGQR GYLLTYVIAY
510 520 530 540 550
IRDLGLEYYV IGESFETSAP WDRVIDLCRN VKERIRRECK ERGVQFAPLS
560 570 580 590 600
TCRVTQTYDA GACIYFYFAF NYRGISDPLT VFEHTEAAAR EEILANGGSL
610 620 630 640
SHHHGVGKIR KQWLKESISD VGFGMLKSVK EYVDPSNIFG NRNLL
Length:645
Mass (Da):71,684
Last modified:March 1, 2003 - v1
Checksum:iEED5030FB7BA4A8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031049 mRNA. Translation: BAC27229.1.
BC063086 mRNA. Translation: AAH63086.1.
RefSeqiNP_766254.2. NM_172666.3.
UniGeneiMm.31227.

Genome annotation databases

GeneIDi228061.
KEGGimmu:228061.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK031049 mRNA. Translation: BAC27229.1.
BC063086 mRNA. Translation: AAH63086.1.
RefSeqiNP_766254.2. NM_172666.3.
UniGeneiMm.31227.

3D structure databases

ProteinModelPortaliQ8C0I1.
SMRiQ8C0I1. Positions 68-645.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8C0I1. 3 interactions.
MINTiMINT-4113860.
STRINGi10090.ENSMUSP00000041967.

Chemistry

SwissLipidsiSLP:000000608.

PTM databases

iPTMnetiQ8C0I1.
PhosphoSiteiQ8C0I1.

Proteomic databases

EPDiQ8C0I1.
MaxQBiQ8C0I1.
PaxDbiQ8C0I1.
PRIDEiQ8C0I1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi228061.
KEGGimmu:228061.

Organism-specific databases

CTDi8540.
MGIiMGI:2443065. Agps.

Phylogenomic databases

eggNOGiKOG1233. Eukaryota.
COG0277. LUCA.
HOGENOMiHOG000231620.
HOVERGENiHBG004179.
InParanoidiQ8C0I1.
KOiK00803.

Enzyme and pathway databases

UniPathwayiUPA00781.

Miscellaneous databases

NextBioi378913.
PROiQ8C0I1.
SOURCEiSearch...

Gene expression databases

BgeeiQ8C0I1.
CleanExiMM_AGPS.

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]
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-57, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiADAS_MOUSE
AccessioniPrimary (citable) accession number: Q8C0I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: March 1, 2003
Last modified: April 13, 2016
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.