ID   TYPH_RAT                Reviewed;         476 AA.
AC   Q5FVR2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=Thymidine phosphorylase;
DE            Short=TP;
DE            EC=2.4.2.4;
DE   AltName: Full=TdRPase;
GN   Name=Tymp; Synonyms=Ecgf1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6 AND THR-475, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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; BC089830; AAH89830.1; -; mRNA.
DR   RefSeq; NP_001012122.1; NM_001012122.1.
DR   AlphaFoldDB; Q5FVR2; -.
DR   SMR; Q5FVR2; -.
DR   STRING; 10116.ENSRNOP00000039935; -.
DR   BindingDB; Q5FVR2; -.
DR   ChEMBL; CHEMBL1075244; -.
DR   iPTMnet; Q5FVR2; -.
DR   PhosphoSitePlus; Q5FVR2; -.
DR   PaxDb; 10116-ENSRNOP00000039935; -.
DR   Ensembl; ENSRNOT00000040541.5; ENSRNOP00000039935.3; ENSRNOG00000032394.6.
DR   Ensembl; ENSRNOT00065028522; ENSRNOP00065022576; ENSRNOG00065017079.
DR   GeneID; 315219; -.
DR   KEGG; rno:315219; -.
DR   AGR; RGD:1305756; -.
DR   CTD; 1890; -.
DR   RGD; 1305756; Tymp.
DR   eggNOG; ENOG502QPRY; Eukaryota.
DR   GeneTree; ENSGT00390000009250; -.
DR   HOGENOM; CLU_025040_0_2_1; -.
DR   InParanoid; Q5FVR2; -.
DR   OMA; VWGGATN; -.
DR   OrthoDB; 178187at2759; -.
DR   PhylomeDB; Q5FVR2; -.
DR   TreeFam; TF332198; -.
DR   Reactome; R-RNO-73614; Pyrimidine salvage.
DR   Reactome; R-RNO-73621; Pyrimidine catabolism.
DR   UniPathway; UPA00578; UER00638.
DR   PRO; PR:Q5FVR2; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Bgee; ENSRNOG00000032394; Expressed in liver and 19 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; IEA:InterPro.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; ISO:RGD.
DR   GO; GO:0046074; P:dTMP catabolic process; ISO:RGD.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; ISO:RGD.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; ISO:RGD.
DR   GO; GO:1905333; P:regulation of gastric motility; ISO:RGD.
DR   GO; GO:0031641; P:regulation of myelination; ISO:RGD.
DR   GO; GO:0051969; P:regulation of transmission of nerve impulse; ISO:RGD.
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.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT   CHAIN           1..476
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000319099"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         475
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   476 AA;  49901 MW;  1BB6068E2D94D24A CRC64;
     MAAPGTPPPL APETAGADSG GGSGEHRQLP ELIRLKRNGG HLSEADIRNF VHALMDGRAQ
     DTQIGAMLMA IRLQGMDLEE TSVLTQALAE SGQQLEWPKA WHQQLVDKHS TGGVGDKVSL
     VLAPALAACG CKVPMISGRS LGHTGGTLDK LESIPGFSVT QSPEQMLQIL EEVGCCIVGQ
     SEKLVPADGI LYAARDVTAT VDSVPLITAS ILSKKAVEGL STLVVDVKFG GAAVFPDQEK
     ARELAKMLVR VGMGLGLQVA AALTAMDNPL GRNVGHTLEV EEALLCLDGA GPPDLRDLVI
     RLGGAILWLS GQAETQDQGA ARVAAALDDG SALHRFQLML SAQGVDPGLA RALCSGSPTQ
     RRQLLPHARK QEELLSPADG IVECVRALPL ACVLHELGAG RSRAGQPIRP GVGAELLVDV
     GQWLSRGTPW LRVHLDGPAL SSQQRRTLLG ALVLSDRAPF KAPSPFAELV LPPTTP
//