ID   TYPH_HUMAN              Reviewed;         482 AA.
AC   P19971; A8MW15; H9KVA0; Q13390; Q8WVB7;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 2.
DT   27-MAR-2024, entry version 242.
DE   RecName: Full=Thymidine phosphorylase {ECO:0000305};
DE            Short=TP;
DE            EC=2.4.2.4 {ECO:0000269|PubMed:1590793};
DE   AltName: Full=Gliostatin;
DE   AltName: Full=Platelet-derived endothelial cell growth factor;
DE            Short=PD-ECGF;
DE   AltName: Full=TdRPase;
DE   Flags: Precursor;
GN   Name=TYMP {ECO:0000312|HGNC:HGNC:3148}; Synonyms=ECGF1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP   VARIANT LEU-471.
RC   TISSUE=Placenta;
RX   PubMed=2467210; DOI=10.1038/338557a0;
RA   Ishikawa F., Miyazono K., Hellman U., Drexler H., Wernstedt C.,
RA   Hagiwara K., Usuki K., Takaku F., Risau W., Heldin C.-H.;
RT   "Identification of angiogenic activity and the cloning and expression of
RT   platelet-derived endothelial cell growth factor.";
RL   Nature 338:557-562(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1580101; DOI=10.1002/yea.320080106;
RA   Finnis C., Goodey A., Courtney M., Sleep D.;
RT   "Expression of recombinant platelet-derived endothelial cell growth factor
RT   in the yeast Saccharomyces cerevisiae.";
RL   Yeast 8:57-60(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Dermoid cancer;
RA   Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA   Tanaka A., Yokoyama S.;
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-471.
RC   TISSUE=Brain, and 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   [6]
RP   NUCLEOTIDE SEQUENCE OF 149-244, AND PROTEIN SEQUENCE OF 125-178 AND
RP   236-244.
RX   PubMed=1570012; DOI=10.1038/356668a0;
RA   Furukawa T., Yoshimura A., Sumizawa T., Haraguchi M., Akiyama S., Fukui K.,
RA   Yamada Y.;
RT   "Angiogenic factor.";
RL   Nature 356:668-668(1992).
RN   [7]
RP   PARTIAL PROTEIN SEQUENCE.
RX   PubMed=1400349; DOI=10.1016/s0021-9258(19)88703-3;
RA   Asai K., Nakanishi K., Isobe I., Eksioglu Y.Z., Hirano A., Hama K.,
RA   Miyamoto T., Kato T.;
RT   "Neurotrophic action of gliostatin on cortical neurons. Identity of
RT   gliostatin and platelet-derived endothelial cell growth factor.";
RL   J. Biol. Chem. 267:20311-20316(1992).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=1590793; DOI=10.1016/s0006-291x(05)80025-7;
RA   Usuki K., Saras J., Waltenberger J., Miyazono K., Pierce G., Thomason A.,
RA   Heldin C.-H.;
RT   "Platelet-derived endothelial cell growth factor has thymidine
RT   phosphorylase activity.";
RL   Biochem. Biophys. Res. Commun. 184:1311-1316(1992).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 12-482 IN COMPLEX WITH INHIBITOR,
RP   AND SUBUNIT.
RX   PubMed=14725767; DOI=10.1016/j.str.2003.11.018;
RA   Norman R.A., Barry S.T., Bate M., Breed J., Colls J.G., Ernill R.J.,
RA   Luke R.W., Minshull C.A., McAlister M.S., McCall E.J., McMiken H.H.,
RA   Paterson D.S., Timms D., Tucker J.A., Pauptit R.A.;
RT   "Crystal structure of human thymidine phosphorylase in complex with a small
RT   molecule inhibitor.";
RL   Structure 12:75-84(2004).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS), AND SUBUNIT.
RX   PubMed=16803458; DOI=10.1042/bj20060513;
RA   El Omari K., Bronckaers A., Liekens S., Perez-Perez M.J., Balzarini J.,
RA   Stammers D.K.;
RT   "Structural basis for non-competitive product inhibition in human thymidine
RT   phosphorylase: implications for drug design.";
RL   Biochem. J. 399:199-204(2006).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) ALONE AND IN COMPLEX WITH
RP   5-IODOURACIL, SUBSTRATE-BINDING SITES, AND MUTAGENESIS OF TYR-199.
RX   PubMed=19555658; DOI=10.1016/j.bbrc.2009.06.104;
RA   Mitsiki E., Papageorgiou A.C., Iyer S., Thiyagarajan N., Prior S.H.,
RA   Sleep D., Finnis C., Acharya K.R.;
RT   "Structures of native human thymidine phosphorylase and in complex with 5-
RT   iodouracil.";
RL   Biochem. Biophys. Res. Commun. 386:666-670(2009).
RN   [14]
RP   VARIANTS MTDPS1 ARG-145; SER-153; ARG-222; ALA-289 AND 397-LEU-ALA-398 DEL.
RX   PubMed=9924029; DOI=10.1126/science.283.5402.689;
RA   Nishino I., Spinazzola A., Hirano M.;
RT   "Thymidine phosphorylase gene mutations in MNGIE, a human mitochondrial
RT   disorder.";
RL   Science 283:689-692(1999).
RN   [15]
RP   VARIANT MTDPS1 GLN-44.
RX   PubMed=12177387; DOI=10.1212/wnl.59.3.455;
RA   Gamez J., Ferreiro C., Accarino M.L., Guarner L., Tadesse S., Marti R.A.,
RA   Andreu A.L., Raguer N., Cervera C., Hirano M.;
RT   "Phenotypic variability in a Spanish family with MNGIE.";
RL   Neurology 59:455-457(2002).
CC   -!- FUNCTION: May have a role in maintaining the integrity of the blood
CC       vessels. Has growth promoting activity on endothelial cells, angiogenic
CC       activity in vivo and chemotactic activity on endothelial cells in
CC       vitro. {ECO:0000269|PubMed:1590793}.
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.
CC       {ECO:0000269|PubMed:1590793}.
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         Evidence={ECO:0000269|PubMed:1590793};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16038;
CC         Evidence={ECO:0000305|PubMed:1590793};
CC   -!- PATHWAY: Pyrimidine metabolism; dTMP biosynthesis via salvage pathway;
CC       dTMP from thymine: step 1/2. {ECO:0000269|PubMed:1590793}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14725767,
CC       ECO:0000269|PubMed:16803458, ECO:0000269|PubMed:19555658}.
CC   -!- INTERACTION:
CC       P19971; Q14696: MESD; NbExp=3; IntAct=EBI-2556931, EBI-6165891;
CC       P19971; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-2556931, EBI-12030590;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P19971-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P19971-2; Sequence=VSP_045556;
CC   -!- DISEASE: Mitochondrial DNA depletion syndrome 1, MNGIE type (MTDPS1)
CC       [MIM:603041]: A multisystem disease associated with mitochondrial
CC       dysfunction. It is clinically characterized by onset between the second
CC       and fifth decades of life, ptosis, progressive external
CC       ophthalmoplegia, gastrointestinal dysmotility (often
CC       pseudoobstruction), diffuse leukoencephalopathy, cachexia, peripheral
CC       neuropathy, and myopathy. {ECO:0000269|PubMed:12177387,
CC       ECO:0000269|PubMed:9924029}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside
CC       phosphorylase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/40397/TYMP";
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DR   EMBL; M63193; AAA60043.1; -; mRNA.
DR   EMBL; AK225269; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; U62317; AAB03344.2; -; Genomic_DNA.
DR   EMBL; BC018160; AAH18160.1; -; mRNA.
DR   EMBL; BC052211; AAH52211.1; -; mRNA.
DR   CCDS; CCDS14096.1; -. [P19971-1]
DR   CCDS; CCDS58811.1; -. [P19971-2]
DR   PIR; S03904; S03904.
DR   RefSeq; NP_001107227.1; NM_001113755.2. [P19971-1]
DR   RefSeq; NP_001107228.1; NM_001113756.2. [P19971-1]
DR   RefSeq; NP_001244917.1; NM_001257988.1. [P19971-1]
DR   RefSeq; NP_001244918.1; NM_001257989.1. [P19971-2]
DR   RefSeq; NP_001944.1; NM_001953.4. [P19971-1]
DR   PDB; 1UOU; X-ray; 2.11 A; A=12-482.
DR   PDB; 2J0F; X-ray; 2.31 A; A/B/C/D=1-482.
DR   PDB; 2WK5; X-ray; 2.99 A; A/B/C/D=1-482.
DR   PDB; 2WK6; X-ray; 2.50 A; A/B=1-482.
DR   PDBsum; 1UOU; -.
DR   PDBsum; 2J0F; -.
DR   PDBsum; 2WK5; -.
DR   PDBsum; 2WK6; -.
DR   AlphaFoldDB; P19971; -.
DR   SMR; P19971; -.
DR   BioGRID; 108219; 123.
DR   IntAct; P19971; 17.
DR   STRING; 9606.ENSP00000379038; -.
DR   BindingDB; P19971; -.
DR   ChEMBL; CHEMBL3106; -.
DR   DrugBank; DB01101; Capecitabine.
DR   DrugBank; DB00369; Cidofovir.
DR   DrugBank; DB00322; Floxuridine.
DR   DrugBank; DB00544; Fluorouracil.
DR   DrugBank; DB06433; Tezacitabine.
DR   DrugBank; DB09343; Tipiracil.
DR   DrugBank; DB00432; Trifluridine.
DR   DrugCentral; P19971; -.
DR   MoonDB; P19971; Curated.
DR   MoonProt; P19971; -.
DR   GlyGen; P19971; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P19971; -.
DR   PhosphoSitePlus; P19971; -.
DR   SwissPalm; P19971; -.
DR   BioMuta; TYMP; -.
DR   DMDM; 67477361; -.
DR   OGP; P19971; -.
DR   EPD; P19971; -.
DR   jPOST; P19971; -.
DR   MassIVE; P19971; -.
DR   MaxQB; P19971; -.
DR   PaxDb; 9606-ENSP00000379038; -.
DR   PeptideAtlas; P19971; -.
DR   PRIDE; P19971; -.
DR   ProteomicsDB; 46247; -.
DR   ProteomicsDB; 53705; -. [P19971-1]
DR   Pumba; P19971; -.
DR   Antibodypedia; 253; 957 antibodies from 36 providers.
DR   DNASU; 1890; -.
DR   Ensembl; ENST00000252029.8; ENSP00000252029.3; ENSG00000025708.14. [P19971-1]
DR   Ensembl; ENST00000395678.7; ENSP00000379036.3; ENSG00000025708.14. [P19971-1]
DR   Ensembl; ENST00000395680.6; ENSP00000379037.1; ENSG00000025708.14. [P19971-1]
DR   Ensembl; ENST00000395681.6; ENSP00000379038.1; ENSG00000025708.14. [P19971-2]
DR   Ensembl; ENST00000487577.5; ENSP00000498844.1; ENSG00000025708.14. [P19971-1]
DR   GeneID; 1890; -.
DR   KEGG; hsa:1890; -.
DR   MANE-Select; ENST00000252029.8; ENSP00000252029.3; NM_001953.5; NP_001944.1.
DR   UCSC; uc003bmb.7; human. [P19971-1]
DR   AGR; HGNC:3148; -.
DR   CTD; 1890; -.
DR   DisGeNET; 1890; -.
DR   GeneCards; TYMP; -.
DR   GeneReviews; TYMP; -.
DR   HGNC; HGNC:3148; TYMP.
DR   HPA; ENSG00000025708; Low tissue specificity.
DR   MalaCards; TYMP; -.
DR   MIM; 131222; gene.
DR   MIM; 603041; phenotype.
DR   neXtProt; NX_P19971; -.
DR   OpenTargets; ENSG00000025708; -.
DR   Orphanet; 298; Mitochondrial neurogastrointestinal encephalomyopathy.
DR   PharmGKB; PA162407502; -.
DR   VEuPathDB; HostDB:ENSG00000025708; -.
DR   eggNOG; ENOG502QPRY; Eukaryota.
DR   GeneTree; ENSGT00390000009250; -.
DR   HOGENOM; CLU_025040_0_2_1; -.
DR   InParanoid; P19971; -.
DR   OMA; VWGGATN; -.
DR   OrthoDB; 178187at2759; -.
DR   PhylomeDB; P19971; -.
DR   TreeFam; TF332198; -.
DR   BioCyc; MetaCyc:HS00442-MONOMER; -.
DR   BRENDA; 2.4.2.4; 2681.
DR   PathwayCommons; P19971; -.
DR   Reactome; R-HSA-73614; Pyrimidine salvage.
DR   Reactome; R-HSA-73621; Pyrimidine catabolism.
DR   SABIO-RK; P19971; -.
DR   SignaLink; P19971; -.
DR   UniPathway; UPA00578; UER00638.
DR   BioGRID-ORCS; 1890; 8 hits in 1158 CRISPR screens.
DR   ChiTaRS; TYMP; human.
DR   EvolutionaryTrace; P19971; -.
DR   GeneWiki; ECGF1; -.
DR   GenomeRNAi; 1890; -.
DR   Pharos; P19971; Tclin.
DR   PRO; PR:P19971; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; P19971; Protein.
DR   Bgee; ENSG00000025708; Expressed in right uterine tube and 168 other cell types or tissues.
DR   ExpressionAtlas; P19971; baseline and differential.
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:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:CAFA.
DR   GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:InterPro.
DR   GO; GO:0009032; F:thymidine phosphorylase activity; IDA:CAFA.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0046074; P:dTMP catabolic process; IEA:Ensembl.
DR   GO; GO:0000002; P:mitochondrial genome maintenance; IMP:CAFA.
DR   GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro.
DR   GO; GO:0006213; P:pyrimidine nucleoside metabolic process; IDA:CAFA.
DR   GO; GO:1905333; P:regulation of gastric motility; IMP:CAFA.
DR   GO; GO:0031641; P:regulation of myelination; IMP:CAFA.
DR   GO; GO:0051969; P:regulation of transmission of nerve impulse; IMP:CAFA.
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; IPR017872; Pyrmidine_PPase_CS.
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   PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
DR   Genevisible; P19971; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Angiogenesis; Chemotaxis;
KW   Developmental protein; Differentiation; Direct protein sequencing;
KW   Disease variant; Glycosyltransferase; Growth factor; Neuropathy;
KW   Phosphoprotein; Primary mitochondrial disease;
KW   Progressive external ophthalmoplegia; Reference proteome; Repeat;
KW   Transferase.
FT   PROPEP          1..10
FT                   /id="PRO_0000035874"
FT   CHAIN           11..482
FT                   /note="Thymidine phosphorylase"
FT                   /id="PRO_0000035875"
FT   REPEAT          265..279
FT                   /note="R-V-A-A-A-L-X(5,6)-L-G-R"
FT   REPEAT          329..342
FT                   /note="R-V-A-A-A-L-X(5,6)-L-G-R"
FT   REPEAT          393..401
FT                   /note="R-A-L-X-X-A-L-V-L"
FT   REPEAT          453..461
FT                   /note="R-A-L-X-X-A-L-V-L"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="substrate"
FT   BINDING         202
FT                   /ligand="substrate"
FT   BINDING         217
FT                   /ligand="substrate"
FT   BINDING         221
FT                   /ligand="substrate"
FT   MOD_RES         6
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5FVR2"
FT   VAR_SEQ         386
FT                   /note="D -> DAPLPA (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_045556"
FT   VARIANT         44
FT                   /note="R -> Q (in MTDPS1; dbSNP:rs28931613)"
FT                   /evidence="ECO:0000269|PubMed:12177387"
FT                   /id="VAR_016777"
FT   VARIANT         145
FT                   /note="G -> R (in MTDPS1; dbSNP:rs121913037)"
FT                   /evidence="ECO:0000269|PubMed:9924029"
FT                   /id="VAR_007643"
FT   VARIANT         153
FT                   /note="G -> S (in MTDPS1; dbSNP:rs121913038)"
FT                   /evidence="ECO:0000269|PubMed:9924029"
FT                   /id="VAR_007644"
FT   VARIANT         222
FT                   /note="K -> R (in MTDPS1; dbSNP:rs149977726)"
FT                   /evidence="ECO:0000269|PubMed:9924029"
FT                   /id="VAR_007645"
FT   VARIANT         289
FT                   /note="E -> A (in MTDPS1; dbSNP:rs121913036)"
FT                   /evidence="ECO:0000269|PubMed:9924029"
FT                   /id="VAR_007646"
FT   VARIANT         397..398
FT                   /note="Missing (in MTDPS1)"
FT                   /evidence="ECO:0000269|PubMed:9924029"
FT                   /id="VAR_007647"
FT   VARIANT         471
FT                   /note="S -> L (in dbSNP:rs11479)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2467210"
FT                   /id="VAR_007648"
FT   MUTAGEN         199
FT                   /note="Y->A: Abolishes catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19555658"
FT   MUTAGEN         199
FT                   /note="Y->F: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19555658"
FT   MUTAGEN         199
FT                   /note="Y->L: Reduced catalytic activity."
FT                   /evidence="ECO:0000269|PubMed:19555658"
FT   CONFLICT        195
FT                   /note="D -> E (in Ref. 5; AAH18160)"
FT                   /evidence="ECO:0000305"
FT   HELIX           36..44
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           51..63
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           68..81
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           85..96
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           106..111
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          112..118
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           125..134
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   TURN            135..137
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          139..143
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           154..158
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           170..180
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          181..185
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           193..204
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           211..224
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          228..236
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          240..244
FT                   /evidence="ECO:0007829|PDB:2J0F"
FT   HELIX           245..261
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          266..272
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          280..283
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           284..294
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           300..316
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          319..322
FT                   /evidence="ECO:0007829|PDB:2J0F"
FT   HELIX           323..335
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           338..349
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           354..362
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           365..371
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          376..382
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          387..392
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           394..405
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          409..412
FT                   /evidence="ECO:0007829|PDB:2WK5"
FT   STRAND          420..423
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          436..446
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   HELIX           449..458
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          459..464
FT                   /evidence="ECO:0007829|PDB:1UOU"
FT   STRAND          475..477
FT                   /evidence="ECO:0007829|PDB:1UOU"
SQ   SEQUENCE   482 AA;  49955 MW;  0652FA0B8F3BDE28 CRC64;
     MAALMTPGTG APPAPGDFSG EGSQGLPDPS PEPKQLPELI RMKRDGGRLS EADIRGFVAA
     VVNGSAQGAQ IGAMLMAIRL RGMDLEETSV LTQALAQSGQ QLEWPEAWRQ QLVDKHSTGG
     VGDKVSLVLA PALAACGCKV PMISGRGLGH TGGTLDKLES IPGFNVIQSP EQMQVLLDQA
     GCCIVGQSEQ LVPADGILYA ARDVTATVDS LPLITASILS KKLVEGLSAL VVDVKFGGAA
     VFPNQEQARE LAKTLVGVGA SLGLRVAAAL TAMDKPLGRC VGHALEVEEA LLCMDGAGPP
     DLRDLVTTLG GALLWLSGHA GTQAQGAARV AAALDDGSAL GRFERMLAAQ GVDPGLARAL
     CSGSPAERRQ LLPRAREQEE LLAPADGTVE LVRALPLALV LHELGAGRSR AGEPLRLGVG
     AELLVDVGQR LRRGTPWLRV HRDGPALSGP QSRALQEALV LSDRAPFAAP SPFAELVLPP
     QQ
//