UPP2_MOUSE
ID UPP2_MOUSE Reviewed; 320 AA.
AC Q8CGR7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Uridine phosphorylase 2 {ECO:0000250|UniProtKB:O95045};
DE Short=UPase 2 {ECO:0000250|UniProtKB:O95045};
DE Short=UrdPase 2 {ECO:0000250|UniProtKB:O95045};
DE EC=2.4.2.3 {ECO:0000269|PubMed:14715930};
DE AltName: Full=Liver-specific uridine phosphorylase {ECO:0000303|PubMed:14715930};
DE Short=L-UrdPase {ECO:0000303|PubMed:14715930};
GN Name=Upp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=C57BL/6 X 129;
RX PubMed=14715930; DOI=10.1210/me.2003-0285;
RA Zhang Y., Repa J.J., Inoue Y., Hayhurst G.P., Gonzalez F.J.,
RA Mangelsdorf D.J.;
RT "Identification of a liver-specific uridine phosphorylase that is regulated
RT by multiple lipid-sensing nuclear receptors.";
RL Mol. Endocrinol. 18:851-862(2004).
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate
CC (PubMed:14715930). The produced molecules are then utilized as carbon
CC and energy sources or in the rescue of pyrimidine bases for nucleotide
CC synthesis (Probable). {ECO:0000269|PubMed:14715930, ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC Evidence={ECO:0000269|PubMed:14715930};
CC -!- ACTIVITY REGULATION: A conditional disulfide bridge can form within the
CC protein that dislocates a critical phosphate-coordinating arginine Arg-
CC 100 away from the active site, disabling the enzyme.
CC {ECO:0000250|UniProtKB:O95045}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=241.7 uM for uridine {ECO:0000269|PubMed:14715930};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1.
CC {ECO:0000269|PubMed:14715930}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O95045}.
CC -!- TISSUE SPECIFICITY: Liver specific. {ECO:0000269|PubMed:14715930}.
CC -!- INDUCTION: Directly up-regulated in liver by HNF-4-alpha (HNF4A)
CC binding to the promoter. May also be indirectly regulated by signaling
CC via various orphan nuclear receptors. Strongly up-regulated by a liver
CC X receptor (LXR) agonist. Slightly up-regulated by a pregnane X
CC receptor (PXR) agonist. Strongly repressed by a peroxisome
CC proliferator-activated receptor alpha (PPAR-alpha) agonist. Slightly
CC repressed by a farnesoid X receptor (FXR) agonist. Shows a diurnal
CC expression pattern with peak levels 12 hours after light onset and
CC lowest levels 0 hours after light onset. {ECO:0000269|PubMed:14715930}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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DR EMBL; AY152393; AAO05705.1; -; mRNA.
DR CCDS; CCDS16051.1; -.
DR RefSeq; NP_083968.1; NM_029692.3.
DR RefSeq; XP_006498472.1; XM_006498409.3.
DR RefSeq; XP_006498473.1; XM_006498410.3.
DR RefSeq; XP_006498474.1; XM_006498411.3.
DR AlphaFoldDB; Q8CGR7; -.
DR SMR; Q8CGR7; -.
DR STRING; 10090.ENSMUSP00000099816; -.
DR iPTMnet; Q8CGR7; -.
DR PhosphoSitePlus; Q8CGR7; -.
DR jPOST; Q8CGR7; -.
DR MaxQB; Q8CGR7; -.
DR PaxDb; Q8CGR7; -.
DR PRIDE; Q8CGR7; -.
DR ProteomicsDB; 299642; -.
DR Antibodypedia; 33709; 136 antibodies from 22 providers.
DR DNASU; 76654; -.
DR Ensembl; ENSMUST00000102755; ENSMUSP00000099816; ENSMUSG00000026839.
DR GeneID; 76654; -.
DR KEGG; mmu:76654; -.
DR UCSC; uc008jsw.2; mouse.
DR CTD; 151531; -.
DR MGI; MGI:1923904; Upp2.
DR VEuPathDB; HostDB:ENSMUSG00000026839; -.
DR eggNOG; KOG3728; Eukaryota.
DR GeneTree; ENSGT00940000161094; -.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; Q8CGR7; -.
DR OMA; CVKSPRR; -.
DR OrthoDB; 1423938at2759; -.
DR TreeFam; TF314310; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR SABIO-RK; Q8CGR7; -.
DR UniPathway; UPA00574; UER00633.
DR BioGRID-ORCS; 76654; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q8CGR7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q8CGR7; protein.
DR Bgee; ENSMUSG00000026839; Expressed in gall bladder and 80 other tissues.
DR ExpressionAtlas; Q8CGR7; baseline and differential.
DR Genevisible; Q8CGR7; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0045098; C:type III intermediate filament; ISS:UniProtKB.
DR GO; GO:0047847; F:deoxyuridine phosphorylase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0004850; F:uridine phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006248; P:CMP catabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; ISO:MGI.
DR GO; GO:0046050; P:UMP catabolic process; IDA:MGI.
DR GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR GO; GO:0006218; P:uridine catabolic process; IDA:UniProtKB.
DR CDD; cd17763; UP_hUPP-like; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR010059; Uridine_phosphorylase_euk.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01719; euk_UDPppase; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycosyltransferase; Redox-active center;
KW Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="Uridine phosphorylase 2"
FT /id="PRO_0000063194"
FT BINDING 66
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 100
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:O95045"
FT BINDING 144..147
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:O95045"
FT BINDING 148..149
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000250|UniProtKB:O95045"
FT BINDING 223..225
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000250|UniProtKB:O95045"
FT DISULFID 95..102
FT /note="Redox-active"
FT /evidence="ECO:0000250|UniProtKB:O95045"
SQ SEQUENCE 320 AA; 35755 MW; A8FEF664BF1A048C CRC64;
MASILPASNR SMRPDKNTYE RKRSVYVKNP YLEGMDEDIL YHLDLGTKTH NLPAMFGDVK
FVCVGGSPNR MKAFAQFMHK ELRLEGDGED IEDICAGTDR YCMFKTGPVL SVSHGMGIPS
ISIMLHELIK LLHHAHCCDV TIIRIGTSGG IGIAPGSVVI TDTAVDSFFK PRFEQVILDN
VVTRSTELDK ELANDLFNCS REIPNVPTLI GHTMCTYDFY EGQGRLDGAL CSFSREKKLD
YLKRAYRAGV RNIEMESTVF AAMCGLCGLR AAVVCVTLLD RLESDQINLS HDVLVEYQQR
PQLLISNFIK KQLGLCDQMS
