ADAS_MOUSE
ID ADAS_MOUSE Reviewed; 645 AA.
AC Q8C0I1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Alkyldihydroxyacetonephosphate synthase, peroxisomal;
DE Short=Alkyl-DHAP synthase;
DE EC=2.5.1.26 {ECO:0000269|PubMed:6833249};
DE AltName: Full=Alkylglycerone-phosphate synthase;
DE Flags: Precursor;
GN Name=Agps;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6833249; DOI=10.1016/s0021-9258(18)32603-6;
RA Brown A.J., Snyder F.;
RT "The mechanism of alkyldihydroxyacetone-P synthase. Formation of [3H]H2O
RT from acyl[1-R-3H]dihydroxyacetone-P by purified alkyldihydroxyacetone-P
RT synthase in the absence of acylhydrolase activity.";
RL J. Biol. Chem. 258:4184-4189(1983).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-57, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the exchange of the acyl chain in acyl-
CC dihydroxyacetonephosphate (acyl-DHAP) for a long chain fatty alcohol,
CC yielding the first ether linked intermediate, i.e. alkyl-
CC dihydroxyacetonephosphate (alkyl-DHAP), in the pathway of ether lipid
CC biosynthesis. {ECO:0000269|PubMed:6833249}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acylglycerone 3-phosphate + a long chain fatty alcohol =
CC 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+);
CC Xref=Rhea:RHEA:36171, ChEBI:CHEBI:15378, ChEBI:CHEBI:17135,
CC ChEBI:CHEBI:57534, ChEBI:CHEBI:57560, ChEBI:CHEBI:73315; EC=2.5.1.26;
CC Evidence={ECO:0000269|PubMed:6833249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36172;
CC Evidence={ECO:0000305|PubMed:6833249};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + hexadecan-1-ol = 1-O-
CC hexadecylglycerone 3-phosphate + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40659, ChEBI:CHEBI:7896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16125, ChEBI:CHEBI:58303, ChEBI:CHEBI:77429;
CC Evidence={ECO:0000269|PubMed:6833249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40660;
CC Evidence={ECO:0000305|PubMed:6833249};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoylglycerone 3-phosphate + a long-chain fatty acid
CC = a 1-acylglycerone 3-phosphate + hexadecanoate;
CC Xref=Rhea:RHEA:40727, ChEBI:CHEBI:7896, ChEBI:CHEBI:57534,
CC ChEBI:CHEBI:57560, ChEBI:CHEBI:58303;
CC Evidence={ECO:0000269|PubMed:6833249};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40728;
CC Evidence={ECO:0000305|PubMed:6833249};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000250|UniProtKB:P97275};
CC -!- PATHWAY: Glycerolipid metabolism; ether lipid biosynthesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P97275}.
CC -!- SUBCELLULAR LOCATION: Peroxisome membrane
CC {ECO:0000250|UniProtKB:P97275}. Peroxisome
CC {ECO:0000250|UniProtKB:P97275}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000305}.
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DR EMBL; AK031049; BAC27229.1; -; mRNA.
DR EMBL; BC063086; AAH63086.1; -; mRNA.
DR RefSeq; NP_766254.2; NM_172666.3.
DR AlphaFoldDB; Q8C0I1; -.
DR SMR; Q8C0I1; -.
DR BioGRID; 230710; 6.
DR IntAct; Q8C0I1; 1.
DR STRING; 10090.ENSMUSP00000041967; -.
DR SwissLipids; SLP:000000608; -.
DR iPTMnet; Q8C0I1; -.
DR PhosphoSitePlus; Q8C0I1; -.
DR EPD; Q8C0I1; -.
DR jPOST; Q8C0I1; -.
DR MaxQB; Q8C0I1; -.
DR PaxDb; Q8C0I1; -.
DR PRIDE; Q8C0I1; -.
DR ProteomicsDB; 285675; -.
DR DNASU; 228061; -.
DR GeneID; 228061; -.
DR KEGG; mmu:228061; -.
DR CTD; 8540; -.
DR MGI; MGI:2443065; Agps.
DR eggNOG; KOG1233; Eukaryota.
DR InParanoid; Q8C0I1; -.
DR OrthoDB; 824020at2759; -.
DR BRENDA; 2.5.1.26; 3474.
DR Reactome; R-MMU-75896; Plasmalogen biosynthesis.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR UniPathway; UPA00781; -.
DR BioGRID-ORCS; 228061; 6 hits in 75 CRISPR screens.
DR ChiTaRS; Agps; mouse.
DR PRO; PR:Q8C0I1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8C0I1; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:0008609; F:alkylglycerone-phosphate synthase activity; ISS:UniProtKB.
DR GO; GO:0071949; F:FAD binding; ISS:UniProtKB.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008611; P:ether lipid biosynthetic process; ISS:UniProtKB.
DR GO; GO:0008610; P:lipid biosynthetic process; ISO:MGI.
DR Gene3D; 1.10.45.10; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR025650; Alkyl-DHAP_Synthase.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR004113; FAD-linked_oxidase_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR46568; PTHR46568; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF55103; SSF55103; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; Peroxisome; Phosphoprotein; Reference proteome; Transferase;
KW Transit peptide.
FT TRANSIT 1..45
FT /note="Peroxisome"
FT /evidence="ECO:0000250"
FT CHAIN 46..645
FT /note="Alkyldihydroxyacetonephosphate synthase,
FT peroxisomal"
FT /id="PRO_0000231676"
FT DOMAIN 189..371
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..604
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT REGION 641..645
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT ACT_SITE 565
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 221..227
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 290..296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 303..306
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 355..361
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT BINDING 502
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT SITE 406
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P97275"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
FT MOD_RES 334
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00116"
SQ SEQUENCE 645 AA; 71684 MW; EED5030FB7BA4A8B CRC64;
MAEAAAGEAG ASERDPDAGR ARRRLRVLSG HLLGRPQEAP STNECKARRA ASAAGASPAA
TPAAPESGTI PKKRQEVMKW NGWGYNDSKF LLNKKGQVEL TGKRYPLSGL VLPTLRDWIQ
NTLGVSLEHK TTSKTSINPS EAPPSIVNED FLQELKEARI SYSQEADDRV FRAHGHCLHE
IFLLREGMFE RIPDIVVWPT CHDDVVKIVN LACKYNLCII PIGGGTSVSY GLMCPADETR
TIISLDTSQM NRILWVDENN LTAHVEAGIT GQDLERQLKE SGYCTGHEPD SLEFSTVGGW
ISTRASGMKK NIYGNIEDLV VHMKMVTPRG VIEKSSQGPR MSTGPDIHHF IMGSEGTLGV
ITEATIKIRP TPEYQKYGSV AFPNFEQGVA CLREIAKQRC APASIRLMDN QQFQFGHALK
PQVSSIFTSF LDGLKKFYIT KFKGFDPNQI SVATLLFEGD REKVLQHEKQ VYDIAAKFGG
LAAGEDNGQR GYLLTYVIAY IRDLGLEYYV IGESFETSAP WDRVIDLCRN VKERIRRECK
ERGVQFAPLS TCRVTQTYDA GACIYFYFAF NYRGISDPLT VFEHTEAAAR EEILANGGSL
SHHHGVGKIR KQWLKESISD VGFGMLKSVK EYVDPSNIFG NRNLL
