RIR2_MACFA
ID RIR2_MACFA Reviewed; 389 AA.
AC Q4R7Q7;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; ORFNames=QtsA-14617;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase small
CC chain family. {ECO:0000305}.
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DR EMBL; AB168758; BAE00865.1; -; mRNA.
DR RefSeq; NP_001271095.1; NM_001284166.1.
DR AlphaFoldDB; Q4R7Q7; -.
DR SMR; Q4R7Q7; -.
DR STRING; 9541.XP_005576631.1; -.
DR GeneID; 101865103; -.
DR CTD; 6241; -.
DR eggNOG; KOG1567; Eukaryota.
DR OrthoDB; 680824at2759; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000233100; 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..389
FT /note="Ribonucleoside-diphosphate reductase subunit M2"
FT /id="PRO_0000190448"
FT MOTIF 49..51
FT /note="Cy"
FT /evidence="ECO:0000250|UniProtKB:P31350"
FT ACT_SITE 176
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 138
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 169
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10014"
FT BINDING 232
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 269
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 389 AA; 44804 MW; 973BAF4471AF2039 CRC64;
MLSVRIPLAP ITNPQQLQLS PLKGLSLVDK ENTPPALSGA RVLASKTARR IFQEPAEPKT
KAAAPGVEDE PLLRENPRRF VIFPIEYHDI WQMYKKAEAS FWTAEEVDLS KDIQHWESLK
PEERYFISHV LAFFAASDGI VNENLVERFS QEVQITEARC FYGFQIAMEN IHSEMYSLLI
DTYIKDPKER EFLFNAIETM PCVEKKADWA LRWIGDKEAT YGERVVAFAA VEGIFFSGSF
ASIFWLKKRG LMPGLTFSNE LISRDEGLHC DFACLMFKHL VHKPSEERVR EIIINAVRVE
QEFLTEALPV KLIGMNCTLM KQYIEFVADR LMLELGFSKV FRVENPFDFM ENISLEGKTN
FFEKRVGEYQ RMGVMSSPTE NSFTLDADF
