RIR2B_PONAB
ID RIR2B_PONAB Reviewed; 351 AA.
AC Q5R9G0;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2 B;
DE EC=1.17.4.1;
GN Name=RRM2B;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a pivotal role in cell survival by repairing damaged
CC DNA in a p53/TP53-dependent manner. Supplies deoxyribonucleotides for
CC DNA repair in cells arrested at G1 or G2. Contains an iron-tyrosyl free
CC radical center required for catalysis. Forms an active ribonucleotide
CC reductase (RNR) complex with RRM1 which is expressed both in resting
CC and proliferating cells in response to DNA damage (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10014};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC Note=Binds 2 iron ions per subunit. {ECO:0000250};
CC -!- PATHWAY: Genetic information processing; DNA replication.
CC -!- SUBUNIT: Heterotetramer with large (RRM1) subunit. Interacts with
CC p53/TP53. Interacts with RRM1 in response to DNA damage (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Translocates from cytoplasm to nucleus in response to DNA damage.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; CR859428; CAH91600.1; -; mRNA.
DR RefSeq; NP_001125944.1; NM_001132472.1.
DR AlphaFoldDB; Q5R9G0; -.
DR SMR; Q5R9G0; -.
DR STRING; 9601.ENSPPYP00000021083; -.
DR Ensembl; ENSPPYT00000021926; ENSPPYP00000021083; ENSPPYG00000018796.
DR GeneID; 100172878; -.
DR KEGG; pon:100172878; -.
DR CTD; 50484; -.
DR eggNOG; KOG1567; Eukaryota.
DR GeneTree; ENSGT00390000013305; -.
DR HOGENOM; CLU_035339_2_0_1; -.
DR InParanoid; Q5R9G0; -.
DR OMA; APELQIY; -.
DR OrthoDB; 680824at2759; -.
DR TreeFam; TF300465; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000001595; Chromosome 8.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:GOC.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009265; P:2'-deoxyribonucleotide biosynthetic process; IEA:Ensembl.
DR GO; GO:0009200; P:deoxyribonucleoside triphosphate metabolic process; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0006264; P:mitochondrial DNA replication; IEA:Ensembl.
DR GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IEA:Ensembl.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0003014; P:renal system process; IEA:Ensembl.
DR GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR GO; GO:0009185; P:ribonucleoside diphosphate metabolic process; IEA:Ensembl.
DR CDD; cd01049; RNRR2; 1.
DR Gene3D; 1.10.620.20; -; 1.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR033909; RNR_small.
DR InterPro; IPR030475; RNR_small_AS.
DR InterPro; IPR000358; RNR_small_fam.
DR PANTHER; PTHR23409; PTHR23409; 1.
DR Pfam; PF00268; Ribonuc_red_sm; 1.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00368; RIBORED_SMALL; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Deoxyribonucleotide synthesis; DNA damage; DNA repair; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome.
FT CHAIN 1..351
FT /note="Ribonucleoside-diphosphate reductase subunit M2 B"
FT /id="PRO_0000228153"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 100
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 131
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 194
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 228
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 351 AA; 40764 MW; 55CB774EE0CBF179 CRC64;
MGDPERPEAA GLDQDERSSS DTNENEIKSN EEPLLRKSSR RFVIFPIQYP DIWKMYKQAQ
ASFWTAEEVD LSKDLPHWNK LKADEKYFIS HILAFFAASD GIVNENLVER FSQEVQVPEA
RCFYGFQILI ENVHSEMYSL LIDTYIRDPK KREFLFNAIE TMPYVKKKAD WALRWIADRK
STFGERVVAF AAVEGVFFSG SFAAIFWLKK RGLMPGLTFS NELISRDEGL HCDFACLMFQ
YLVNKPSEER VREIIVDAVK IEQEFLTEAL PVGLIGMNCI LMKQYIEFVA DRLLVELGFS
KVFQAENPFD FMENISLEGK TNFFEKRVSE YQRFAVMAET TDNVFTLDAD F
