RIR2_MESAU
ID RIR2_MESAU Reviewed; 386 AA.
AC Q60561;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ribonucleoside-diphosphate reductase subunit M2;
DE EC=1.17.4.1;
DE AltName: Full=Ribonucleotide reductase small chain;
DE AltName: Full=Ribonucleotide reductase small subunit;
GN Name=RRM2;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=1384717; DOI=10.1016/0167-4781(92)90151-o;
RA Chaudhuri M.M., Tonin P.N., Srinivasan P.R.;
RT "cDNA sequence of the small subunit of the hamster ribonucleotide
RT reductase.";
RL Biochim. Biophys. Acta 1171:117-121(1992).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides (By similarity). Inhibits Wnt signaling
CC (By similarity). {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: Heterodimer of a large and a small subunit. Interacts (via Cy
CC motif and when phosphorylated at Thr-33) with CCNF; the interaction
CC occurs exclusively in G2 and early M (By similarity).
CC {ECO:0000250|UniProtKB:P31350}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P31350}. Nucleus
CC {ECO:0000250|UniProtKB:P31350}. Note=Localized to the cytoplasm in S
CC phase cells. May localize to the nucleus in G2 phase cells.
CC {ECO:0000250|UniProtKB:P31350}.
CC -!- PTM: Phosphorylation on Ser-20 relieves the inhibitory effect on Wnt
CC signaling (By similarity). Phosphorylated on Thr-33 by CDK1 and CDK2;
CC predominantly in G2 and M phase (By similarity).
CC {ECO:0000250|UniProtKB:P31350}.
CC -!- PTM: Ubiquitinated by the SCF(CCNF) E3 ubiquitin-protein ligase
CC complex; leading to its degradation by the proteasome.
CC {ECO:0000250|UniProtKB:P31350}.
CC -!- MISCELLANEOUS: Two distinct regulatory sites have been defined: the
CC specificity site, which controls substrate specificity, and the
CC activity site which regulates overall catalytic activity. A substrate-
CC binding catalytic site, located on M1, is formed only in the presence
CC of the second subunit M2.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; X68127; CAA48232.1; -; mRNA.
DR PIR; S27153; S27153.
DR AlphaFoldDB; Q60561; -.
DR SMR; Q60561; -.
DR STRING; 10036.XP_005082089.1; -.
DR eggNOG; KOG1567; Eukaryota.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; ISS:UniProtKB.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniPathway.
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; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..386
FT /note="Ribonucleoside-diphosphate reductase subunit M2"
FT /id="PRO_0000190449"
FT MOTIF 49..51
FT /note="Cy"
FT /evidence="ECO:0000250|UniProtKB:P31350"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 139
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 170
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 233
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 270
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P11157"
FT MOD_RES 33
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P11157"
SQ SEQUENCE 386 AA; 44482 MW; 8B057993D859F9A6 CRC64;
MFSVRVPLAT ITDQQQLQVS PLKALSLADK ENTPPSLSAT PVLASKVARR ILQDVAEPES
KVSTNPSVED EPLLRENPRR FVVFPIEYHD IWKMYKKAEA SFWTAEEVDL SKDIQHWEAL
KPDERHFISH VLAFFAASDG IVNENLVERF SQEVQVTEAR CFYGFQIAME NIHSEMYSLL
IDTYIKDSKE REYLFNAIET MPCVKKKADW ALRWIGDKEA TYGERVVAFA AVEGIFFSGS
FASIFWLKKR GLMPGLTFSN ELISRDEGLH CDFACLMFKH LVHKPSEQRV QEIITNAVRI
EQEFLTEALP VKLIGMNCTL MKQYIEFVAD RLMLELGFNK IFKVENPFDF MENISLEGKT
NFFEKRVGEY QRMGVMSNSF TLDADF
