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Alpha-ketoglutarate-dependent dioxygenase FTO (EC 1.14.11.-) (Fat mass and obesity-associated protein) (Protein fatso)

 FTO_MOUSE               Reviewed;         502 AA.
Q8BGW1; Q3TTZ5; Q6ZPI7; Q8BR68; Q8CB66; Q8R250; Q9QZ13;
01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-MAR-2003, sequence version 1.
25-OCT-2017, entry version 112.
RecName: Full=Alpha-ketoglutarate-dependent dioxygenase FTO;
EC=1.14.11.- {ECO:0000250|UniProtKB:Q9C0B1};
AltName: Full=Fat mass and obesity-associated protein;
AltName: Full=Protein fatso;
Name=Fto; Synonyms=Kiaa1752;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10501967; DOI=10.1007/s003359901144;
Peters T., Ausmeier K., Ruether U.;
"Cloning of Fatso (Fto), a novel gene deleted by the Fused toes (Ft)
mouse mutation.";
Mamm. Genome 10:983-986(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
STRAIN=C57BL/6J, and NOD;
TISSUE=Aorta, Bone, Corpora quadrigemina, Skin, Thymus, and Vein;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, COFACTOR, ENZYME REGULATION, SUBCELLULAR LOCATION,
MUTAGENESIS OF HIS-304 AND ARG-313, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=17991826; DOI=10.1126/science.1151710;
Gerken T., Girard C.A., Tung Y.C., Webby C.J., Saudek V.,
Hewitson K.S., Yeo G.S., McDonough M.A., Cunliffe S., McNeill L.A.,
Galvanovskis J., Rorsman P., Robins P., Prieur X., Coll A.P., Ma M.,
Jovanovic Z., Farooqi I.S., Sedgwick B., Barroso I., Lindahl T.,
Ponting C.P., Ashcroft F.M., O'Rahilly S., Schofield C.J.;
"The obesity-associated FTO gene encodes a 2-oxoglutarate-dependent
nucleic acid demethylase.";
Science 318:1469-1472(2007).
[6]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18775698; DOI=10.1016/j.febslet.2008.08.019;
Jia G., Yang C.G., Yang S., Jian X., Yi C., Zhou Z., He C.;
"Oxidative demethylation of 3-methylthymine and 3-methyluracil in
single-stranded DNA and RNA by mouse and human FTO.";
FEBS Lett. 582:3313-3319(2008).
[7]
DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, FUNCTION, AND TISSUE
SPECIFICITY.
PubMed=19234441; DOI=10.1038/nature07848;
Fischer J., Koch L., Emmerling C., Vierkotten J., Peters T.,
Bruning J.C., Ruther U.;
"Inactivation of the Fto gene protects from obesity.";
Nature 458:894-898(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, CIRCULAR DICHROISM, AND
MUTAGENESIS OF ILE-367.
PubMed=19680540; DOI=10.1371/journal.pgen.1000599;
Church C., Lee S., Bagg E.A., McTaggart J.S., Deacon R., Gerken T.,
Lee A., Moir L., Mecinovic J., Quwailid M.M., Schofield C.J.,
Ashcroft F.M., Cox R.D.;
"A mouse model for the metabolic effects of the human fat mass and
obesity associated FTO gene.";
PLoS Genet. 5:E1000599-E1000599(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Dioxygenase that repairs alkylated DNA and RNA by
oxidative demethylation. Has highest activity towards single-
stranded RNA containing 3-methyluracil, followed by single-
stranded DNA containing 3-methylthymine. Has low demethylase
activity towards single-stranded DNA containing 1-methyladenine or
3-methylcytosine. Specifically demethylates N(6)-methyladenosine
(m6A) RNA, the most prevalent internal modification of messenger
RNA (mRNA) in higher eukaryotes. Has no activity towards 1-
methylguanine. Has no detectable activity towards double-stranded
DNA. Requires molecular oxygen, alpha-ketoglutarate and iron.
Contributes to the regulation of the global metabolic rate, energy
expenditure and energy homeostasis. Contributes to the regulation
of body size and body fat accumulation.
{ECO:0000269|PubMed:17991826, ECO:0000269|PubMed:18775698,
ECO:0000269|PubMed:19234441, ECO:0000269|PubMed:19680540}.
-!- CATALYTIC ACTIVITY: N(6)-methyladenosine in mRNA + 2-oxoglutarate
+ O(2) = adenosine in mRNA + formaldehyde + succinate + CO(2).
{ECO:0000250|UniProtKB:Q9C0B1}.
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000269|PubMed:17991826};
Note=Binds 1 Fe(2+) ion per subunit.
{ECO:0000269|PubMed:17991826};
-!- ENZYME REGULATION: Activated by ascorbate. Inhibited by N-
oxalylglycine, fumarate and succinate.
{ECO:0000269|PubMed:17991826}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.5-6. {ECO:0000269|PubMed:18775698};
-!- SUBUNIT: Monomer. May also exist as homodimer.
{ECO:0000269|PubMed:19680540}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17991826,
ECO:0000269|PubMed:19234441, ECO:0000269|PubMed:19680540}. Nucleus
speckle {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q8BGW1-1; Sequence=Displayed;
Name=2;
IsoId=Q8BGW1-2; Sequence=VSP_025011;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q8BGW1-3; Sequence=VSP_025009, VSP_025010;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q8BGW1-4; Sequence=VSP_025007, VSP_025008;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Detected in brain, brain cortex,
hypothalamus, cerebellum, liver, pancreas, heart, kidney, white
adipose tissue and skeletal muscle. Most abundant in the brain,
particularly in hypothalamic nuclei governing energy balance.
{ECO:0000269|PubMed:17991826, ECO:0000269|PubMed:19234441}.
-!- INDUCTION: Down-regulated in fasting animals.
{ECO:0000269|PubMed:17991826}.
-!- DOMAIN: The 3D-structure of the Fe2OG dioxygenase domain is
similar to that of the Fe2OG dioxygenase domain found in the
bacterial DNA repair dioxygenase alkB and its mammalian orthologs,
but sequence similarity is very low. As a consequence, the domain
is not detected by protein signature databases (By similarity).
{ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Elevated perinatal mortality. Mice have
normal body weight at birth, but show growth retardation from day
2 onwards, resulting in a weight reduction of 30-40% after 6
weeks, both in males and females. In addition, animals display
reduced nose to anus length. Fat mass is reduced by 60% in males
and by 23% in females. Lean body mass is reduced by 26% in males
and 19% in females. White adipose tissue decreases more and more
over time, while brown adipose tissue is not affected. Serum
leptin levels are decreased, while serum levels of adiponectin are
increased. Mice exhibit significant hyperphagia after correction
for body weight. They show increased oxygen consumption, carbon
dioxide production and heat generation, indicating increased
energy expenditure, in spite of reduced spontaneous locomotor
activity. Plasma adrenaline concentrations are significantly
increased. Overall glucose metabolism appears normal.
{ECO:0000269|PubMed:19234441}.
-!- SIMILARITY: Belongs to the fto family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC98247.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ237917; CAB59324.1; -; mRNA.
EMBL; AK129437; BAC98247.1; ALT_INIT; mRNA.
EMBL; AK036677; BAC29533.1; -; mRNA.
EMBL; AK040866; BAC30724.1; -; mRNA.
EMBL; AK045465; BAC32382.1; -; mRNA.
EMBL; AK049502; BAC33780.1; -; mRNA.
EMBL; AK088881; BAC40629.1; -; mRNA.
EMBL; AK161060; BAE36177.1; -; mRNA.
EMBL; BC022222; AAH22222.1; -; mRNA.
EMBL; BC057008; AAH57008.1; -; mRNA.
CCDS; CCDS22521.1; -. [Q8BGW1-1]
RefSeq; NP_036066.2; NM_011936.2. [Q8BGW1-1]
UniGene; Mm.4375; -.
ProteinModelPortal; Q8BGW1; -.
SMR; Q8BGW1; -.
BioGrid; 204941; 1.
STRING; 10090.ENSMUSP00000068380; -.
ChEMBL; CHEMBL3611964; -.
iPTMnet; Q8BGW1; -.
PhosphoSitePlus; Q8BGW1; -.
PaxDb; Q8BGW1; -.
PeptideAtlas; Q8BGW1; -.
PRIDE; Q8BGW1; -.
Ensembl; ENSMUST00000069718; ENSMUSP00000068380; ENSMUSG00000055932. [Q8BGW1-1]
Ensembl; ENSMUST00000125471; ENSMUSP00000147563; ENSMUSG00000055932. [Q8BGW1-4]
Ensembl; ENSMUST00000128081; ENSMUSP00000147548; ENSMUSG00000055932. [Q8BGW1-2]
Ensembl; ENSMUST00000136802; ENSMUSP00000147603; ENSMUSG00000055932. [Q8BGW1-3]
GeneID; 26383; -.
KEGG; mmu:26383; -.
UCSC; uc009msq.2; mouse. [Q8BGW1-4]
UCSC; uc009msr.2; mouse. [Q8BGW1-3]
UCSC; uc009mss.2; mouse. [Q8BGW1-2]
UCSC; uc009mst.2; mouse. [Q8BGW1-1]
CTD; 79068; -.
MGI; MGI:1347093; Fto.
eggNOG; ENOG410IJ5C; Eukaryota.
eggNOG; ENOG4111PKJ; LUCA.
GeneTree; ENSGT00390000017730; -.
HOVERGEN; HBG101847; -.
InParanoid; Q8BGW1; -.
KO; K19469; -.
OMA; PVCIGPD; -.
OrthoDB; EOG091G08LA; -.
PhylomeDB; Q8BGW1; -.
TreeFam; TF333296; -.
Reactome; R-MMU-73943; Reversal of alkylation damage by DNA dioxygenases.
ChiTaRS; Fto; mouse.
PRO; PR:Q8BGW1; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000055932; -.
CleanEx; MM_FTO; -.
ExpressionAtlas; Q8BGW1; baseline and differential.
Genevisible; Q8BGW1; MM.
GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043734; F:DNA-N1-methyladenine dioxygenase activity; IDA:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
GO; GO:0035516; F:oxidative DNA demethylase activity; IDA:BHF-UCL.
GO; GO:0035515; F:oxidative RNA demethylase activity; IDA:BHF-UCL.
GO; GO:1990931; F:RNA N6-methyladenosine dioxygenase activity; ISS:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IMP:UniProtKB.
GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:BHF-UCL.
GO; GO:0080111; P:DNA demethylation; IDA:BHF-UCL.
GO; GO:0070989; P:oxidative demethylation; IDA:BHF-UCL.
GO; GO:0035552; P:oxidative single-stranded DNA demethylation; IDA:BHF-UCL.
GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IDA:BHF-UCL.
GO; GO:0090335; P:regulation of brown fat cell differentiation; ISO:MGI.
GO; GO:0010883; P:regulation of lipid storage; IMP:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IMP:UniProtKB.
GO; GO:0044065; P:regulation of respiratory system process; IMP:UniProtKB.
GO; GO:0070350; P:regulation of white fat cell proliferation; IMP:UniProtKB.
GO; GO:0042245; P:RNA repair; IDA:BHF-UCL.
GO; GO:0001659; P:temperature homeostasis; IMP:UniProtKB.
Gene3D; 2.60.120.590; -; 1.
InterPro; IPR037151; AlkB-like_sf.
InterPro; IPR032868; FTO.
InterPro; IPR024366; FTO_C.
InterPro; IPR024367; FTO_cat_dom.
PANTHER; PTHR31291; PTHR31291; 1.
Pfam; PF12934; FTO_CTD; 1.
Pfam; PF12933; FTO_NTD; 1.
SMART; SM01223; FTO_NTD; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Dioxygenase;
DNA damage; DNA repair; Iron; Metal-binding; Nucleus; Obesity;
Oxidoreductase; Reference proteome; RNA repair.
CHAIN 1 502 Alpha-ketoglutarate-dependent dioxygenase
FTO.
/FTId=PRO_0000286164.
REGION 42 324 Fe2OG dioxygenase domain. {ECO:0000250}.
REGION 210 221 Loop L1; predicted to block binding of
double-stranded DNA or RNA.
{ECO:0000250}.
REGION 228 231 Substrate binding. {ECO:0000250}.
REGION 313 315 Alpha-ketoglutarate binding.
{ECO:0000250}.
METAL 228 228 Iron; catalytic. {ECO:0000250}.
METAL 230 230 Iron; catalytic. {ECO:0000250}.
METAL 304 304 Iron; catalytic. {ECO:0000250}.
BINDING 96 96 Substrate. {ECO:0000250}.
BINDING 108 108 Substrate. {ECO:0000250}.
BINDING 202 202 Alpha-ketoglutarate. {ECO:0000250}.
BINDING 292 292 Alpha-ketoglutarate. {ECO:0000250}.
BINDING 317 317 Alpha-ketoglutarate. {ECO:0000250}.
BINDING 319 319 Alpha-ketoglutarate. {ECO:0000250}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9C0B1}.
VAR_SEQ 296 316 DDLNATHQHCVLAGSQPRFSS -> GNVGSLRVGHLWGFEI
HFWIL (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025007.
VAR_SEQ 317 502 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025008.
VAR_SEQ 411 413 TNA -> VSA (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025009.
VAR_SEQ 414 502 Missing (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_025010.
VAR_SEQ 453 502 CQSRVVRTLPVQQKPDCRPYWEKDDPSMPLPFDLTDVVSEL
RGQLLEARS -> FVLLRGGVWCPCPSSARPAQRTKVEDIL
S (in isoform 2).
{ECO:0000303|PubMed:14621295}.
/FTId=VSP_025011.
MUTAGEN 304 304 H->A: Reduced enzyme activity.
{ECO:0000269|PubMed:17991826}.
MUTAGEN 313 313 R->A: Loss of enzyme activity.
{ECO:0000269|PubMed:17991826}.
MUTAGEN 367 367 I->A: Reduces enzyme activity by about
60%. {ECO:0000269|PubMed:19680540}.
MUTAGEN 367 367 I->F: Alters protein structure and causes
an increase in whole body metabolism,
leading to a lean phenotype in adult
males, but not in females.
{ECO:0000269|PubMed:19680540}.
CONFLICT 181 181 G -> R (in Ref. 3; BAC32382).
{ECO:0000305}.
CONFLICT 384 384 N -> S (in Ref. 1; CAB59324, 2; BAC98247,
3; BAC40629 and 4; AAH22222).
{ECO:0000305}.
CONFLICT 410 410 M -> V (in Ref. 2; BAC98247, 3; BAC40629
and 4; AAH22222). {ECO:0000305}.
CONFLICT 463 463 V -> A (in Ref. 3; BAC40629 and 4;
AAH22222). {ECO:0000305}.
SEQUENCE 502 AA; 58007 MW; 69223B824028D872 CRC64;
MKRVQTAEER EREAKKLRLL EELEDTWLPY LTPKDDEFYQ QWQLKYPKLV FREAGSIPEE
LHKEVPEAFL TLHKHGCLFR DVVRIQGKDV LTPVSRILIG DPGCTYKYLN TRLFTVPWPV
KGCTVKYTEA EIAAACQTFL KLNDYLQVET IQALEELAVR EKANEDAVPL CMAEFPRAGV
GPSCDDEVDL KSRAAYNVTL LNFMDPQKMP YLKEEPYFGM GKMAVSWHHD ENLVDRSAVA
VYSYSCEGSE DESEDESSFE GRDPDTWHVG FKISWDIETP GLTIPLHQGD CYFMLDDLNA
THQHCVLAGS QPRFSSTHRV AECSTGTLDY ILERCQLALQ NVLNDSDDGD VSLKSFDPAV
LKQGEEIHNE VEFEWLRQFW FQGNRYKLCT DWWCEPMTHL EGLWKKMESM TNAVLREVKR
EGLPVEQRSE ILSAILVPLT VRQNLRKEWH ARCQSRVVRT LPVQQKPDCR PYWEKDDPSM
PLPFDLTDVV SELRGQLLEA RS


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