UPP1_MOUSE
ID UPP1_MOUSE Reviewed; 311 AA.
AC P52624; Q8JZX0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Uridine phosphorylase 1;
DE Short=UPase 1;
DE Short=UrdPase 1;
DE EC=2.4.2.3 {ECO:0000269|PubMed:7744869};
GN Name=Upp1; Synonyms=Up, Upp;
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], PROTEIN SEQUENCE OF 67-86 AND 277-293,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND INDUCTION.
RC STRAIN=BALB/cJ;
RX PubMed=7744869; DOI=10.1074/jbc.270.20.12191;
RA Watanabe S., Hino A., Wada K., Eliason J.F., Uchida T.;
RT "Purification, cloning, and expression of murine uridine phosphorylase.";
RL J. Biol. Chem. 270:12191-12196(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate
CC (PubMed:7744869). The produced molecules are then utilized as carbon
CC and energy sources or in the rescue of pyrimidine bases for nucleotide
CC synthesis. {ECO:0000269|PubMed:7744869, 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:7744869};
CC -!- ACTIVITY REGULATION: Strongly inhibited by 2,2'-anhydro-5-ethyluridine,
CC a competitive inhibitor. {ECO:0000269|PubMed:7744869}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=64 uM for uridine {ECO:0000269|PubMed:7744869};
CC KM=148 uM for thymidine {ECO:0000269|PubMed:7744869};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC uracil from uridine (phosphorylase route): step 1/1. {ECO:0000305}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q16831}.
CC -!- INDUCTION: By a mixture of inflammatory cytokines: TNF-alpha, IL-1 and
CC interferon gamma. {ECO:0000269|PubMed:7744869}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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DR EMBL; D44464; BAA07916.1; -; mRNA.
DR EMBL; BC036559; AAH36559.1; -; mRNA.
DR CCDS; CCDS24432.1; -.
DR PIR; A57501; A57501.
DR RefSeq; NP_001152873.1; NM_001159401.1.
DR RefSeq; NP_001152874.1; NM_001159402.1.
DR RefSeq; NP_033503.2; NM_009477.3.
DR RefSeq; XP_006514730.1; XM_006514667.2.
DR AlphaFoldDB; P52624; -.
DR SMR; P52624; -.
DR STRING; 10090.ENSMUSP00000020677; -.
DR BindingDB; P52624; -.
DR ChEMBL; CHEMBL3718; -.
DR PhosphoSitePlus; P52624; -.
DR SwissPalm; P52624; -.
DR jPOST; P52624; -.
DR PaxDb; P52624; -.
DR PeptideAtlas; P52624; -.
DR PRIDE; P52624; -.
DR ProteomicsDB; 298204; -.
DR Antibodypedia; 27594; 166 antibodies from 25 providers.
DR DNASU; 22271; -.
DR Ensembl; ENSMUST00000020677; ENSMUSP00000020677; ENSMUSG00000020407.
DR Ensembl; ENSMUST00000101525; ENSMUSP00000099063; ENSMUSG00000020407.
DR Ensembl; ENSMUST00000164791; ENSMUSP00000127473; ENSMUSG00000020407.
DR GeneID; 22271; -.
DR KEGG; mmu:22271; -.
DR UCSC; uc007hzw.2; mouse.
DR CTD; 7378; -.
DR MGI; MGI:1097668; Upp1.
DR VEuPathDB; HostDB:ENSMUSG00000020407; -.
DR eggNOG; KOG3728; Eukaryota.
DR GeneTree; ENSGT00940000157781; -.
DR HOGENOM; CLU_054104_0_0_1; -.
DR InParanoid; P52624; -.
DR OMA; FIHLCNP; -.
DR OrthoDB; 1423938at2759; -.
DR PhylomeDB; P52624; -.
DR TreeFam; TF314310; -.
DR Reactome; R-MMU-73614; Pyrimidine salvage.
DR Reactome; R-MMU-73621; Pyrimidine catabolism.
DR UniPathway; UPA00574; UER00633.
DR BioGRID-ORCS; 22271; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Upp1; mouse.
DR PRO; PR:P52624; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P52624; protein.
DR Bgee; ENSMUSG00000020407; Expressed in ectoplacental cone and 148 other tissues.
DR ExpressionAtlas; P52624; baseline and differential.
DR Genevisible; P52624; MM.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0047847; F:deoxyuridine phosphorylase activity; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0009032; F:thymidine phosphorylase activity; IMP:MGI.
DR GO; GO:0004850; F:uridine phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR GO; GO:0006248; P:CMP catabolic process; IDA:MGI.
DR GO; GO:0006249; P:dCMP catabolic process; IDA:MGI.
DR GO; GO:0046074; P:dTMP catabolic process; IMP:MGI.
DR GO; GO:0046079; P:dUMP catabolic process; IDA:MGI.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IMP:MGI.
DR GO; GO:0046050; P:UMP catabolic process; IDA:MGI.
DR GO; GO:0044206; P:UMP salvage; IMP:MGI.
DR GO; GO:0006218; P:uridine catabolic process; IDA:UniProtKB.
DR GO; GO:0046108; P:uridine metabolic process; IMP:MGI.
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 Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..311
FT /note="Uridine phosphorylase 1"
FT /id="PRO_0000063192"
FT BINDING 61
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 95
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 139..142
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 143..144
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT BINDING 218..220
FT /ligand="uridine"
FT /ligand_id="ChEBI:CHEBI:16704"
FT /evidence="ECO:0000250|UniProtKB:Q16831"
FT CONFLICT 260
FT /note="S -> G (in Ref. 1; BAA07916)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 34086 MW; A7DFC46BF9129302 CRC64;
MAATGTEAKD LENHHNDCFI QLSNPNIAAM KEDVLYHFNL STSTHDFPAM FGDVKFVCVG
GSSSRMNTFI KYVAAELGLD HPGKEYPNIC AGTDRYAMYK AGPVLSVSHG MGIPSIGIML
HELIKMLYHA RCSNITIIRI GTSGGIGLEP GSVVITQQAV NECFKPEFEQ IVLGKRVIRN
TNLDAQLVQE LVQCSSDLNE FPMVVGNTMC TLDFYEGQGR LDGALCSYTE KDKQSYLRAA
HAAGVRNIEM ESSVFATMCS ACGLKAAVVC VTLLDRLQGD QINTPHDVLV EYQQRPQRLV
GHFIKKSLGR A
