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Database: UniProt
Entry: A0A452R4I5_URSAM
LinkDB: A0A452R4I5_URSAM
Original site: A0A452R4I5_URSAM 
ID   A0A452R4I5_URSAM        Unreviewed;       394 AA.
AC   A0A452R4I5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
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:ENSUAMP00000013335.1};
OS   Ursus americanus (American black bear) (Euarctos americanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX   NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000013335.1, ECO:0000313|Proteomes:UP000291022};
RN   [1] {ECO:0000313|Proteomes:UP000291022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA   Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT   "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT   in black bear kidneys.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSUAMP00000013335.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   AlphaFoldDB; A0A452R4I5; -.
DR   SMR; A0A452R4I5; -.
DR   STRING; 9643.ENSUAMP00000013335; -.
DR   Ensembl; ENSUAMT00000014957.1; ENSUAMP00000013335.1; ENSUAMG00000010729.1.
DR   GeneTree; ENSGT00390000009298; -.
DR   OMA; ENYWRRD; -.
DR   OrthoDB; 179931at2759; -.
DR   Proteomes; UP000291022; Unassembled WGS sequence.
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:UP000291022}.
FT   DOMAIN          114..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..83
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..83
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;  44255 MW;  7BE7F6853BEDB3A6 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 LSGNIRDPAL KPKRSHRKAD PDAAHRPRIL EMDKEENRRS VLLPTHRRRS
     SFSSENYWRK SYESGEDCSE AAGSPARKVK MRRH
//
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