ID ALKB5_XENTR Reviewed; 358 AA. AC Q66JG8; F6VI63; F6VRK9; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 08-MAY-2019, entry version 68. DE RecName: Full=RNA demethylase ALKBH5; DE EC=1.14.11.- {ECO:0000250|UniProtKB:Q6P6C2}; DE AltName: Full=Alkylated DNA repair protein alkB homolog 5; DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5; GN Name=alkbh5; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; OC Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=20431018; DOI=10.1126/science.1183670; RA Hellsten U., Harland R.M., Gilchrist M.J., Hendrix D., Jurka J., RA Kapitonov V., Ovcharenko I., Putnam N.H., Shu S., Taher L., RA Blitz I.L., Blumberg B., Dichmann D.S., Dubchak I., Amaya E., RA Detter J.C., Fletcher R., Gerhard D.S., Goodstein D., Graves T., RA Grigoriev I.V., Grimwood J., Kawashima T., Lindquist E., Lucas S.M., RA Mead P.E., Mitros T., Ogino H., Ohta Y., Poliakov A.V., Pollet N., RA Robert J., Salamov A., Sater A.K., Schmutz J., Terry A., Vize P.D., RA Warren W.C., Wells D., Wills A., Wilson R.K., Zimmerman L.B., RA Zorn A.M., Grainger R., Grammer T., Khokha M.K., Richardson P.M., RA Rokhsar D.S.; RT "The genome of the Western clawed frog Xenopus tropicalis."; RL Science 328:633-636(2010). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Embryo; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Dioxygenase that demethylates RNA by oxidative CC demethylation: specifically demethylates N(6)-methyladenosine CC (m6A) RNA, the most prevalent internal modification of messenger CC RNA (mRNA) in higher eukaryotes. Can also demethylate N(6)- CC methyladenosine in single-stranded DNA (in vitro) (By similarity). CC Requires molecular oxygen, alpha-ketoglutarate and iron (By CC similarity). Demethylation of m6A mRNA affects mRNA processing and CC export (By similarity). {ECO:0000250|UniProtKB:Q3TSG4, CC ECO:0000250|UniProtKB:Q6P6C2}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + N(6)-methyladenosine in mRNA + O2 = CC adenosine in mRNA + CO2 + formaldehyde + succinate; CC Xref=Rhea:RHEA:49520, Rhea:RHEA-COMP:12414, Rhea:RHEA- CC COMP:12417, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:30031, CC ChEBI:CHEBI:74411, ChEBI:CHEBI:74449; CC Evidence={ECO:0000250|UniProtKB:Q6P6C2}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000250|UniProtKB:Q6P6C2}; CC Note=Binds 1 Fe(2+) ion per subunit. CC {ECO:0000250|UniProtKB:Q6P6C2}; CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6P6C2}. CC -!- SUBCELLULAR LOCATION: Nucleus speckle CC {ECO:0000250|UniProtKB:Q6P6C2}. CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAMC01050884; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AAMC01050885; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC080920; AAH80920.1; -; mRNA. DR RefSeq; NP_001008038.1; NM_001008037.1. DR SMR; Q66JG8; -. DR STRING; 8364.ENSXETP00000059003; -. DR GeneID; 493400; -. DR KEGG; xtr:493400; -. DR CTD; 54890; -. DR Xenbase; XB-GENE-987580; alkbh5. DR HOGENOM; HOG000007505; -. DR InParanoid; Q66JG8; -. DR KO; K10767; -. DR OrthoDB; 722070at2759; -. DR TreeFam; TF329212; -. DR Reactome; R-XTR-73943; Reversal of alkylation damage by DNA dioxygenases. DR Proteomes; UP000008143; Unassembled WGS sequence. DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1990931; F:RNA N6-methyladenosine dioxygenase activity; ISS:UniProtKB. DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB. DR GO; GO:0006397; P:mRNA processing; ISS:UniProtKB. DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; ISS:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; ISS:UniProtKB. DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB. DR Gene3D; 2.60.120.590; -; 1. DR InterPro; IPR027450; AlkB-like. DR InterPro; IPR037151; AlkB-like_sf. DR InterPro; IPR032860; ALKBH5. DR PANTHER; PTHR32074; PTHR32074; 2. DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1. PE 2: Evidence at transcript level; KW Complete proteome; Dioxygenase; Iron; Metal-binding; Nucleus; KW Oxidoreductase; Reference proteome. FT CHAIN 1 358 RNA demethylase ALKBH5. FT /FTId=PRO_0000239286. FT REGION 159 161 Alpha-ketoglutarate binding. FT {ECO:0000250|UniProtKB:Q6P6C2}. FT COMPBIAS 34 47 Glu-rich. FT METAL 170 170 Iron; catalytic. FT {ECO:0000250|UniProtKB:Q6P6C2}. FT METAL 172 172 Iron; catalytic. FT {ECO:0000250|UniProtKB:Q6P6C2}. FT METAL 232 232 Iron; catalytic. FT {ECO:0000250|UniProtKB:Q6P6C2}. FT BINDING 243 243 Alpha-ketoglutarate. FT {ECO:0000250|UniProtKB:Q6P6C2}. SQ SEQUENCE 358 AA; 41677 MW; 69E3D4E37CC629C5 CRC64; MSATYTDLRE KLQSLYRDSP KEVRKRKQPT SDTEEEEAAS EPEEEEEARK VRSGIRQVRL FSPDECARIE AKIDEVVSRA EKGLYREHTV DRAPLRNKYF FGEGYTYGAQ LQRRGPGQER LYPKGEVDEI PAWVNELVIR RLVEHRVIPE GFVNSAVIND YQPGGCIVSH VDPIHIFERP IVSVSFFSDS ALCFGCKFQF KPIRVSEPVF FLPVQRGSVT VLSGYAADEI THCIRPQDIK ERRAVVILRK TRTEAPRLEM KSLSSSYQPE RLQGSNRQHI LKPKRSHRKA DPDAAHRPRI LEMDKEENRR SVLLPKQRRR SHFSSENYWR RSHDYVDTYT ETGEDDGSPV RKVKMRRH //