TYPH_HUMAN
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 03-AUG-2022, entry version 233.
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="http://atlasgeneticsoncology.org/Genes/TYMPID40397ch22q13.html";
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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; 118.
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; P19971; -.
DR PeptideAtlas; P19971; -.
DR PRIDE; P19971; -.
DR ProteomicsDB; 46247; -.
DR ProteomicsDB; 53705; -. [P19971-1]
DR Antibodypedia; 253; 873 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 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; DVWRRMI; -.
DR OrthoDB; 1214417at2759; -.
DR PhylomeDB; P19971; -.
DR TreeFam; TF332198; -.
DR BioCyc; MetaCyc:HS00442-MON; -.
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 1085 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 166 other tissues.
DR ExpressionAtlas; P19971; baseline and differential.
DR Genevisible; P19971; HS.
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; -; 1.
DR Gene3D; 3.90.1170.30; -; 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 PANTHER; PTHR10515; PTHR10515; 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; SSF47648; SSF47648; 1.
DR SUPFAM; SSF52418; SSF52418; 1.
DR SUPFAM; SSF54680; SSF54680; 1.
DR TIGRFAMs; TIGR02644; Y_phosphoryl; 1.
DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1.
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
