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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
 
 
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