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UTPP_CAEEL
ID   UTPP_CAEEL              Reviewed;         295 AA.
AC   Q23588;
DT   18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 137.
DE   RecName: Full=Uridine and thymidine phosphorylase {ECO:0000303|PubMed:19645718};
DE            EC=2.4.2.2 {ECO:0000269|PubMed:19645718};
DE   AltName: Full=Pyrimidine-nucleoside phosphorylase {ECO:0000305};
GN   Name=upp-1 {ECO:0000312|WormBase:ZK783.2};
GN   ORFNames=ZK783.2 {ECO:0000312|WormBase:ZK783.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, DISRUPTION
RP   PHENOTYPE, AND MUTAGENESIS OF THR-128 AND TYR-209.
RX   PubMed=19645718; DOI=10.1111/j.1742-4658.2009.07168.x;
RA   Kim S., Park D.H., Kim T.H., Hwang M., Shim J.;
RT   "Functional analysis of pyrimidine biosynthesis enzymes using the
RT   anticancer drug 5-fluorouracil in Caenorhabditis elegans.";
RL   FEBS J. 276:4715-4726(2009).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC       and thymidine to uracil and ribose-phosphate or thymine and
CC       deoxyribose-1-phosphate (PubMed:19645718). The produced molecules are
CC       then utilized as carbon and energy sources or in the rescue of
CC       pyrimidine bases for nucleotide synthesis (Probable). Required for
CC       normal lifespan (PubMed:19645718). {ECO:0000269|PubMed:19645718,
CC       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=2.4.2.2;
CC         Evidence={ECO:0000269|PubMed:19645718};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate +
CC         thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC         Evidence={ECO:0000269|PubMed:19645718};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC         phosphate + uracil; Xref=Rhea:RHEA:22824, ChEBI:CHEBI:16450,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2;
CC         Evidence={ECO:0000269|PubMed:19645718};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       uracil from uridine (phosphorylase route): step 1/1.
CC       {ECO:0000269|PubMed:19645718}.
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2. {ECO:0000269|PubMed:19645718}.
CC   -!- TISSUE SPECIFICITY: Expressed in hypodermis, pharynx, spermatheca and
CC       gonad. {ECO:0000269|PubMed:19645718}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown causes resistance to 5-
CC       fluorouracil (5-FU)-mediated toxicity. {ECO:0000269|PubMed:19645718}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. {ECO:0000305}.
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DR   EMBL; BX284603; CCD65249.1; -; Genomic_DNA.
DR   PIR; T34514; T34514.
DR   RefSeq; NP_498671.2; NM_066270.6.
DR   AlphaFoldDB; Q23588; -.
DR   SMR; Q23588; -.
DR   STRING; 6239.ZK783.2; -.
DR   World-2DPAGE; 0011:Q23588; -.
DR   EPD; Q23588; -.
DR   PaxDb; Q23588; -.
DR   PeptideAtlas; Q23588; -.
DR   EnsemblMetazoa; ZK783.2.1; ZK783.2.1; WBGene00022817.
DR   GeneID; 176077; -.
DR   KEGG; cel:CELE_ZK783.2; -.
DR   CTD; 176077; -.
DR   WormBase; ZK783.2; CE34466; WBGene00022817; upp-1.
DR   eggNOG; KOG3728; Eukaryota.
DR   GeneTree; ENSGT00940000167337; -.
DR   HOGENOM; CLU_054104_0_0_1; -.
DR   InParanoid; Q23588; -.
DR   OMA; FIHLCNP; -.
DR   OrthoDB; 1423938at2759; -.
DR   PhylomeDB; Q23588; -.
DR   Reactome; R-CEL-73614; Pyrimidine salvage.
DR   Reactome; R-CEL-73621; Pyrimidine catabolism.
DR   UniPathway; UPA00574; UER00633.
DR   UniPathway; UPA00578; UER00638.
DR   PRO; PR:Q23588; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00022817; Expressed in adult organism and 4 other tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047847; F:deoxyuridine phosphorylase activity; IEA:RHEA.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IDA:WormBase.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IDA:WormBase.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0046104; P:thymidine metabolic process; IDA:WormBase.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006212; P:uracil catabolic process; IMP:WormBase.
DR   GO; GO:0019860; P:uracil metabolic process; IMP:WormBase.
DR   GO; GO:0006218; P:uridine catabolic process; IMP:WormBase.
DR   GO; GO:0046108; P:uridine metabolic process; IDA:WormBase.
DR   CDD; cd17763; UP_hUPP-like; 1.
DR   Gene3D; 3.40.50.1580; -; 1.
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.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Pyrimidine biosynthesis; Reference proteome;
KW   Transferase.
FT   CHAIN           1..295
FT                   /note="Uridine and thymidine phosphorylase"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000438779"
FT   BINDING         81
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:Q16831"
FT   BINDING         125..128
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000250|UniProtKB:Q16831"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16831"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q16831"
FT   MUTAGEN         128
FT                   /note="T->I: In jg1; 80 percent reduction in uridine and
FT                   thymidine phosphorylase activity. Reduced lifespan.
FT                   Resistance to 5-fluorouracil (5-FU) or 5-deoxy-5-
FT                   fluorouridine (5dFUR)-mediated toxicity."
FT                   /evidence="ECO:0000269|PubMed:19645718"
FT   MUTAGEN         209
FT                   /note="Y->F: In jg2; 80 percent reduction in uridine and
FT                   thymidine phosphorylase activity. Reduced lifespan.
FT                   Resistance to 5-fluorouracil (5-FU)-mediated toxicity."
FT                   /evidence="ECO:0000269|PubMed:19645718"
SQ   SEQUENCE   295 AA;  33042 MW;  2C4D45011BF775DF CRC64;
     MNGLVKNGNV EKPNKYFDIK DKRDFLYHFG FGVDTLDIPA VFGDTKFVCT GGSPGRFKLY
     AEWFAKEANI PCSENLSRSD RFVIYKTGPV CWINHGMGTP SLSIMLVESF KLMHHAGVKN
     PTFIRLGTSG GVGVPPGTVV VSTEAMNAEL GDTYVQIIAG KRIERPTQLD AALREALCEV
     GKEKSIPVET GKTMCADDFY EGQMRLDGYF CDYEEEDKYA FLRKLNALGV RNIEMESTCF
     ASFTCRAGFQ SAIVCVTLLN RMDGDQVQIA KEQYIEYEER PFRLVTAYIR KQTGI
 
 
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