AK10B_ARATH
ID AK10B_ARATH Reviewed; 569 AA.
AC Q9ZT92;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=RNA demethylase ALKBH10B {ECO:0000305};
DE EC=1.14.11.53 {ECO:0000269|PubMed:29180595};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 10B {ECO:0000305};
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 10B {ECO:0000305};
GN Name=ALKBH10B {ECO:0000303|PubMed:29180595};
GN OrderedLocusNames=At4g02940 {ECO:0000312|Araport:AT4G02940};
GN ORFNames=T4I9.18 {ECO:0000312|EMBL:AAC79112.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF HIS-366 AND GLU-368.
RX PubMed=29180595; DOI=10.1105/tpc.16.00912;
RA Duan H.C., Wei L.H., Zhang C., Wang Y., Chen L., Lu Z., Chen P.R., He C.,
RA Jia G.;
RT "ALKBH10B Is an RNA N6-Methyladenosine Demethylase Affecting Arabidopsis
RT Floral Transition.";
RL Plant Cell 29:2995-3011(2017).
CC -!- FUNCTION: Dioxygenase that demethylates RNA by oxidative demethylation:
CC specifically demethylates N(6)-methyladenosine (m6A) RNA, the most
CC prevalent internal modification of messenger RNA (mRNA) in higher
CC eukaryotes (PubMed:29180595). ALKBH10B-mediated mRNA m6A demethylation
CC stabilizes the mRNA of the key flowering time regulators FT, SPL3 and
CC SPL9, which are involved in the control of floral transition
CC (PubMed:29180595). {ECO:0000269|PubMed:29180595}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + an N(6)-methyladenosine in mRNA + O2 = an
CC adenosine in mRNA + CO2 + formaldehyde + succinate;
CC Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA-COMP:12417,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, ChEBI:CHEBI:74411,
CC ChEBI:CHEBI:74449; EC=1.14.11.53;
CC Evidence={ECO:0000269|PubMed:29180595};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:29180595};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000305|PubMed:29180595};
CC -!- DISRUPTION PHENOTYPE: Reduced vegetative growth and late flowering.
CC {ECO:0000269|PubMed:29180595}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; AF069442; AAC79112.1; -; Genomic_DNA.
DR EMBL; AL161495; CAB77779.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82253.1; -; Genomic_DNA.
DR EMBL; AY093043; AAM13042.1; -; mRNA.
DR EMBL; AY128924; AAM91324.1; -; mRNA.
DR PIR; T01399; T01399.
DR RefSeq; NP_192203.1; NM_116528.6.
DR AlphaFoldDB; Q9ZT92; -.
DR SMR; Q9ZT92; -.
DR IntAct; Q9ZT92; 1.
DR STRING; 3702.AT4G02940.1; -.
DR iPTMnet; Q9ZT92; -.
DR PaxDb; Q9ZT92; -.
DR PRIDE; Q9ZT92; -.
DR ProteomicsDB; 244921; -.
DR EnsemblPlants; AT4G02940.1; AT4G02940.1; AT4G02940.
DR GeneID; 828132; -.
DR Gramene; AT4G02940.1; AT4G02940.1; AT4G02940.
DR KEGG; ath:AT4G02940; -.
DR Araport; AT4G02940; -.
DR TAIR; locus:2139345; AT4G02940.
DR eggNOG; KOG4176; Eukaryota.
DR HOGENOM; CLU_026669_0_0_1; -.
DR InParanoid; Q9ZT92; -.
DR OMA; NCEARHA; -.
DR OrthoDB; 469905at2759; -.
DR PhylomeDB; Q9ZT92; -.
DR PRO; PR:Q9ZT92; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZT92; baseline and differential.
DR GO; GO:0032451; F:demethylase activity; IDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IPI:TAIR.
DR GO; GO:1990931; F:mRNA N6-methyladenosine dioxygenase activity; IMP:TAIR.
DR GO; GO:0006402; P:mRNA catabolic process; IMP:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR Gene3D; 2.60.120.590; -; 1.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR044842; ALKBH9B/ALKBH10B-like.
DR PANTHER; PTHR31447; PTHR31447; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Dioxygenase; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..569
FT /note="RNA demethylase ALKBH10B"
FT /id="PRO_0000445521"
FT REGION 164..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 118..151
FT /evidence="ECO:0000255"
FT COMPBIAS 554..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 366
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:29180595"
FT BINDING 368
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:29180595"
FT BINDING 421
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000305|PubMed:29180595"
FT BINDING 430
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000305|PubMed:29180595"
FT MUTAGEN 366
FT /note="H->A: Loss of catalytic activity; when associated
FT with A-368."
FT /evidence="ECO:0000269|PubMed:29180595"
FT MUTAGEN 368
FT /note="E->A: Loss of catalytic activity; when associated
FT with A-366."
FT /evidence="ECO:0000269|PubMed:29180595"
SQ SEQUENCE 569 AA; 62687 MW; 91AFB30CBE6C4466 CRC64;
MTIAAAPARQ TDRSATGFNP AYVTTAKAVS VPVQVPPATV VSEGLGKDAL ISWFRGEFAA
ANAIIDAMCS HLRIAEEAVS GSEYEAVFAA IHRRRLNWIP VLQMQKYHSI AEVAIELQKV
AAKKAEDLKQ KKTEEEAEED LKEVVATEEE EVKKECFNGE KVTENDVNGD VEDVEDDSPT
SDITDSGSHQ DVHQTVVADT AHQIICHSHE DCDARSCEIK PIKGFQAKEQ VKGHTVNVVK
GLKLYEELLK EDEISKLLDF VAELREAGIN GKLAGESFIL FNKQIKGNKR ELIQLGVPIF
GHVKADENSN DTNNSVNIEP IPPLLESVID HFVTWRLIPE YKRPNGCVIN FFEEGEYSQP
FLKPPHLEQP ISTLVLSEST MAYGRILSSD NEGNFRGPLT LSLKQGSLLV MRGNSADMAR
HVMCPSQNKR VSITFFRIRP DTYHNHSQPN SPRNDGVMTM WQPYQMTPTP FLNGYDHSID
MMPKLGVLRP PMVMMAPPPV QPMILPSPNV MGTGGGTGVF LPWASVNSSR KHVKHLPPRA
QKKRLLPLPP AASSSPAGGS TSEPVITVG
