ALKB5_XENLA
ID ALKB5_XENLA Reviewed; 360 AA.
AC Q6GPB5;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=RNA demethylase ALKBH5;
DE EC=1.14.11.53 {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 laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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. Can also demethylate N(6)-methyladenosine in single-
CC stranded DNA (in vitro) (By similarity). Requires molecular oxygen,
CC alpha-ketoglutarate and iron (By similarity). Demethylation of m6A mRNA
CC affects mRNA processing and export (By similarity).
CC {ECO:0000250|UniProtKB:Q3TSG4, ECO:0000250|UniProtKB:Q6P6C2}.
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: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. {ECO:0000250|UniProtKB:Q6P6C2};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q6P6C2}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q6P6C2}.
CC -!- SIMILARITY: Belongs to the alkB family. {ECO:0000305}.
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DR EMBL; BC073226; AAH73226.1; -; mRNA.
DR RefSeq; NP_001085704.1; NM_001092235.1.
DR AlphaFoldDB; Q6GPB5; -.
DR SMR; Q6GPB5; -.
DR PRIDE; Q6GPB5; -.
DR GeneID; 444130; -.
DR CTD; 444130; -.
DR Xenbase; XB-GENE-987585; alkbh5.L.
DR Proteomes; UP000186698; Genome assembly.
DR Bgee; 444130; Expressed in muscle tissue and 19 other tissues.
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:mRNA 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; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
PE 2: Evidence at transcript level;
KW Dioxygenase; Iron; Metal-binding; Nucleus; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..360
FT /note="RNA demethylase ALKBH5"
FT /id="PRO_0000239285"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 161..163
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6P6C2"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6P6C2"
FT BINDING 174
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6P6C2"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6P6C2"
FT BINDING 245
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q6P6C2"
SQ SEQUENCE 360 AA; 41749 MW; F9DAEE8C4726BEEF CRC64;
MSATYTDLRE KLQSLNRDSP KEVRKRKQPA SDTEEEDEAG SEPEAEEEEA RKVRSGIRQM
RLFSPDECAA IESKIDEVVS RADKGLYQEH TVDRAPLRNK YFFGEGYTYG AQLQRRGPGQ
ERLYPKGEVD EIPGWVHELV IRRLVERRII PEGFVNSAVI NDYQPGGCIV SHVDPIHIFE
RPIVSVSFFS DSALCFGCKF QFKPIRVSEP VFFLPVRRGS VTVLSGYAAD EITHCIRPQD
IKERRAVVIL RKTRTEAPRL EMKSLSSSYQ PERLQGSNRQ HILKPKRSHR KADPDAAHRP
RILEMDKEEN RRSVLLPKQR RRSHFSSENY WRRSHDHVDT YTETGEDEGS PVRKVKMRRH
