ID M3XLT2_MUSPF Unreviewed; 394 AA.
AC M3XLT2;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=RNA demethylase ALKBH5 {ECO:0000256|ARBA:ARBA00018485};
DE EC=1.14.11.53 {ECO:0000256|ARBA:ARBA00012931};
DE AltName: Full=Alkylated DNA repair protein alkB homolog 5 {ECO:0000256|ARBA:ARBA00030726};
DE AltName: Full=Alpha-ketoglutarate-dependent dioxygenase alkB homolog 5 {ECO:0000256|ARBA:ARBA00033313};
GN Name=ALKBH5 {ECO:0000313|Ensembl:ENSMPUP00000000032.1,
GN ECO:0000313|RefSeq:XP_004776581.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000000032.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000000032.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004776581.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004776581.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033605};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
CC -!- SIMILARITY: Belongs to the alkB family.
CC {ECO:0000256|ARBA:ARBA00007879}.
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DR EMBL; AEYP01089332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01089333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01089334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004776581.1; XM_004776524.3.
DR STRING; 9669.ENSMPUP00000000032; -.
DR Ensembl; ENSMPUT00000000032.1; ENSMPUP00000000032.1; ENSMPUG00000000032.1.
DR GeneID; 101692442; -.
DR KEGG; mpuf:101692442; -.
DR CTD; 54890; -.
DR eggNOG; KOG4176; Eukaryota.
DR GeneTree; ENSGT00390000009298; -.
DR HOGENOM; CLU_047472_1_0_1; -.
DR OMA; ENYWRRD; -.
DR OrthoDB; 179931at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0042382; C:paraspeckles; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR GO; GO:1990931; F:mRNA N6-methyladenosine dioxygenase activity; IEA:Ensembl.
DR GO; GO:0046630; P:gamma-delta T cell proliferation; IEA:Ensembl.
DR GO; GO:0061157; P:mRNA destabilization; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl.
DR GO; GO:0140694; P:non-membrane-bounded organelle assembly; IEA:Ensembl.
DR GO; GO:0035553; P:oxidative single-stranded RNA demethylation; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR Gene3D; 2.60.120.590; Alpha-ketoglutarate-dependent dioxygenase AlkB-like; 1.
DR InterPro; IPR027450; AlkB-like.
DR InterPro; IPR037151; AlkB-like_sf.
DR InterPro; IPR032860; ALKBH5.
DR PANTHER; PTHR32074; RNA DEMETHYLASE ALKBH5; 1.
DR PANTHER; PTHR32074:SF2; RNA DEMETHYLASE ALKBH5; 1.
DR Pfam; PF13532; 2OG-FeII_Oxy_2; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000000715}.
FT DOMAIN 111..274
FT /note="Alpha-ketoglutarate-dependent dioxygenase AlkB-like"
FT /evidence="ECO:0000259|Pfam:PF13532"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 394 AA; 44256 MW; DEB7A3806BBDB3A0 CRC64;
MAAASGYTDL REKLKSMTSR DNYKAGSREA AAAAAAAVAA AAAAAAAAEP YPVSGAKRKY
QEDSDPERSD YEEQQLQKEE EARKVKSGIR QMRLFSQDEC AKIEARIDEV VSRAEKGLYN
EHTVDRAPLR NKYFFGEGYT YGAQLQKRGP GQERLYPPGD VDEIPEWVHQ LVIQKLVEHR
VIPEGFVNSA VINDYQPGGC IVSHVDPIHI FERPIVSVSF FSDSALCFGC KFQFKPIRVS
EPVLSLPVRR GSVTVLSGYA ADEITHCIRP QDIKERRAVI ILRKTRLDAP RLETKSLSSS
VLPPSYASDR LSGNNRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS VLLPTHRRRS
SFSSENYWRK SYESGEDCSE AAGSPARKVK MRRH
//
