ID   TYPH_MOUSE              Reviewed;         471 AA.
AC   Q99N42;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Thymidine phosphorylase;
DE            Short=TP;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=Tymp; Synonyms=Ecgf1;
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].
RA   Ishikawa F., Toyoshima H., Miyazono K., Haraguchi M.;
RT   "Mouse thymidine phosphorylase.";
RL   Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible phosphorolysis of thymidine. The
CC       produced molecules are then utilized as carbon and energy sources or in
CC       the rescue of pyrimidine bases for nucleotide synthesis (By
CC       similarity). {ECO:0000250}.
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=2.4.2.4;
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000305}.
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DR   EMBL; AB060274; BAB41208.1; -; mRNA.
DR   CCDS; CCDS27747.1; -.
DR   RefSeq; NP_612175.1; NM_138302.1.
DR   AlphaFoldDB; Q99N42; -.
DR   SMR; Q99N42; -.
DR   STRING; 10090.ENSMUSP00000023285; -.
DR   BindingDB; Q99N42; -.
DR   ChEMBL; CHEMBL2606; -.
DR   iPTMnet; Q99N42; -.
DR   PhosphoSitePlus; Q99N42; -.
DR   jPOST; Q99N42; -.
DR   MaxQB; Q99N42; -.
DR   PaxDb; 10090-ENSMUSP00000023285; -.
DR   PeptideAtlas; Q99N42; -.
DR   ProteomicsDB; 298078; -.
DR   Antibodypedia; 253; 957 antibodies from 36 providers.
DR   DNASU; 72962; -.
DR   Ensembl; ENSMUST00000023285.5; ENSMUSP00000023285.5; ENSMUSG00000022615.8.
DR   GeneID; 72962; -.
DR   KEGG; mmu:72962; -.
DR   UCSC; uc007xgl.2; mouse.
DR   AGR; MGI:1920212; -.
DR   CTD; 1890; -.
DR   MGI; MGI:1920212; Tymp.
DR   VEuPathDB; HostDB:ENSMUSG00000022615; -.
DR   eggNOG; ENOG502QPRY; Eukaryota.
DR   GeneTree; ENSGT00390000009250; -.
DR   HOGENOM; CLU_025040_0_2_1; -.
DR   InParanoid; Q99N42; -.
DR   OMA; VWGGATN; -.
DR   OrthoDB; 178187at2759; -.
DR   PhylomeDB; Q99N42; -.
DR   TreeFam; TF332198; -.
DR   BRENDA; 2.4.2.4; 3474.
DR   Reactome; R-MMU-73614; Pyrimidine salvage.
DR   Reactome; R-MMU-73621; Pyrimidine catabolism.
DR   SABIO-RK; Q99N42; -.
DR   UniPathway; UPA00578; UER00638.
DR   BioGRID-ORCS; 72962; 2 hits in 63 CRISPR screens.
DR   ChiTaRS; Tymp; mouse.
DR   PRO; PR:Q99N42; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; Q99N42; Protein.
DR   Bgee; ENSMUSG00000022615; Expressed in liver and 80 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004645; F:1,4-alpha-oligoglucan phosphorylase activity; TAS:MGI.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IMP:MGI.
DR   GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
DR   GO; GO:0006935; P:chemotaxis; TAS:MGI.
DR   GO; GO:0046074; P:dTMP catabolic process; IMP:MGI.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; ISO:MGI.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISO:MGI.
DR   GO; GO:1905333; P:regulation of gastric motility; ISO:MGI.
DR   GO; GO:0031641; P:regulation of myelination; ISO:MGI.
DR   GO; GO:0051969; P:regulation of transmission of nerve impulse; ISO:MGI.
DR   Gene3D; 3.40.1030.10; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   Gene3D; 3.90.1170.30; Pyrimidine nucleoside phosphorylase-like, C-terminal domain; 1.
DR   InterPro; IPR000312; Glycosyl_Trfase_fam3.
DR   InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom.
DR   InterPro; IPR036320; Glycosyl_Trfase_fam3_N_dom_sf.
DR   InterPro; IPR035902; Nuc_phospho_transferase.
DR   InterPro; IPR036566; PYNP-like_C_sf.
DR   InterPro; IPR013102; PYNP_C.
DR   InterPro; IPR018090; Pyrmidine_PPas_bac/euk.
DR   InterPro; IPR000053; Thymidine/pyrmidine_PPase.
DR   NCBIfam; TIGR02644; Y_phosphoryl; 1.
DR   PANTHER; PTHR10515; THYMIDINE PHOSPHORYLASE; 1.
DR   PANTHER; PTHR10515:SF0; THYMIDINE PHOSPHORYLASE; 1.
DR   Pfam; PF02885; Glycos_trans_3N; 1.
DR   Pfam; PF00591; Glycos_transf_3; 1.
DR   Pfam; PF07831; PYNP_C; 1.
DR   PIRSF; PIRSF000478; TP_PyNP; 1.
DR   SMART; SM00941; PYNP_C; 1.
DR   SUPFAM; SSF52418; Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain; 1.
DR   SUPFAM; SSF47648; Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain; 1.
DR   SUPFAM; SSF54680; Pyrimidine nucleoside phosphorylase C-terminal domain; 1.
DR   Genevisible; Q99N42; MM.
PE   2: Evidence at transcript level;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..471
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000059047"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5FVR2"
SQ   SEQUENCE   471 AA;  49336 MW;  C6AC64FC004DFF7E CRC64;
     MAAPGTPPPS ASGGGGGEPR QLPELIRLKR DGGHLREADI RNFVHAVIDG RAQDTQIGAM
     LMAIRLQGMN LEETSVLTRA LAESGQQLEW PKAWHQQLVD KHSTGGVGDK VSLVLAPALA
     ACGCKVPMIS GRSLGHTGGT LDKLESIPGF GVTQSPEQML HILEEVGCCI VGQSAKLVPA
     DGILYAARDV TATVDSVPLI TASILSKKAV EGLSTLVVDV KFGGAAVFPD QEKARELAKM
     LVRVGVSLGL KVAAALTAMD NPLGRSVGHT LEVEEALLCL DGAGPPDLRD LVIRLGGAIL
     WISGQAETQD QGAARVAAAL DDGSARRRFQ LMLSAQGVDP GLAKALCSGS PTQRRQLLPH
     AREQEELLAP ADGIVECVRA LPLARVLHDL GAGRSRAGQP IRPGVGAEVL VDVGQCLSRG
     TPWLRVHLDG PALSSQQRRT LQGALVLSDR APFKVPSPFA ELVLPPTIAQ P
//