ID   THI72_YEAST             Reviewed;         599 AA.
AC   Q08579; D6W2P8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   08-NOV-2023, entry version 153.
DE   RecName: Full=Thiamine transporter THI72;
GN   Name=THI72; OrderedLocusNames=YOR192C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [3]
RP   FUNCTION.
RX   PubMed=9235906; DOI=10.1074/jbc.272.31.19165;
RA   Enjo F., Nosaka K., Ogata M., Iwashima A., Nishimura H.;
RT   "Isolation and characterization of a thiamin transport gene, THI10, from
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 272:19165-19170(1997).
RN   [4]
RP   INDUCTION.
RX   PubMed=16194233; DOI=10.1111/j.1365-2958.2005.04835.x;
RA   Nosaka K., Onozuka M., Konno H., Kawasaki Y., Nishimura H., Sano M.,
RA   Akaji K.;
RT   "Genetic regulation mediated by thiamin pyrophosphate-binding motif in
RT   Saccharomyces cerevisiae.";
RL   Mol. Microbiol. 58:467-479(2005).
CC   -!- FUNCTION: Low affinity thiamine transporter responsible for intake of
CC       thiamine. It is possible that the primary function is the uptake of
CC       closely related compounds and that thiamine transport is a secondary
CC       activity of these proteins. {ECO:0000269|PubMed:9235906}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- INDUCTION: Induced by limited extracellular thiamine levels.
CC       {ECO:0000269|PubMed:16194233}.
CC   -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC       {ECO:0000305}.
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DR   EMBL; Z75100; CAA99401.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10964.1; -; Genomic_DNA.
DR   PIR; S67084; S67084.
DR   RefSeq; NP_014835.3; NM_001183611.3.
DR   AlphaFoldDB; Q08579; -.
DR   SMR; Q08579; -.
DR   BioGRID; 34587; 62.
DR   DIP; DIP-7926N; -.
DR   IntAct; Q08579; 2.
DR   MINT; Q08579; -.
DR   STRING; 4932.YOR192C; -.
DR   MaxQB; Q08579; -.
DR   PaxDb; 4932-YOR192C; -.
DR   PeptideAtlas; Q08579; -.
DR   EnsemblFungi; YOR192C_mRNA; YOR192C; YOR192C.
DR   GeneID; 854364; -.
DR   KEGG; sce:YOR192C; -.
DR   AGR; SGD:S000005718; -.
DR   SGD; S000005718; THI72.
DR   VEuPathDB; FungiDB:YOR192C; -.
DR   eggNOG; KOG2466; Eukaryota.
DR   GeneTree; ENSGT00940000176299; -.
DR   HOGENOM; CLU_021555_3_0_1; -.
DR   InParanoid; Q08579; -.
DR   OMA; GLCVNMI; -.
DR   OrthoDB; 1218881at2759; -.
DR   BioCyc; YEAST:G3O-33701-MONOMER; -.
DR   BioGRID-ORCS; 854364; 0 hits in 10 CRISPR screens.
DR   PRO; PR:Q08579; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q08579; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:1903089; F:5-amino-1-ribofuranosylimidazole-4-carboxamide transmembrane transporter activity; IGI:SGD.
DR   GO; GO:0015205; F:nucleobase transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:1903088; P:5-amino-1-ribofuranosylimidazole-4-carboxamide transmembrane transport; IGI:SGD.
DR   GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR   GO; GO:0015888; P:thiamine transport; IGI:SGD.
DR   CDD; cd11482; SLC-NCS1sbd_NRT1-like; 1.
DR   Gene3D; 1.10.4160.10; Hydantoin permease; 1.
DR   InterPro; IPR012681; NCS1.
DR   InterPro; IPR001248; Pur-cyt_permease.
DR   InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR   NCBIfam; TIGR00800; ncs1; 1.
DR   PANTHER; PTHR30618; NCS1 FAMILY PURINE/PYRIMIDINE TRANSPORTER; 1.
DR   PANTHER; PTHR30618:SF15; NICOTINAMIDE RIBOSIDE TRANSPORTER 1-RELATED; 1.
DR   Pfam; PF02133; Transp_cyt_pur; 1.
PE   2: Evidence at transcript level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..599
FT                   /note="Thiamine transporter THI72"
FT                   /id="PRO_0000197928"
FT   TRANSMEM        42..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        372..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          553..599
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..569
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..592
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q05998"
FT   MOD_RES         572
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q08485"
SQ   SEQUENCE   599 AA;  67186 MW;  43872C34C352A2AA CRC64;
     MSFGTRISRA LRFLEIPVKN RASVNFLRNP DLQPIKSVNQ TWGFWSNFAY WGVLSFNVGM
     WIGGSSALTV GLSYSETIGA FIIADLLTIL FALANSCPGY DWKVGFTLAQ RFVFGIYGSA
     LGIIIRILMS IVYYGSNAWL GGLCVNMILD SWSHHYLHLP NTLSSKVAMT TKELIGFIIF
     HILTAFCYFM KPYHMNYILI WSCVGTFFAM LGMVIYLTKS AHGVGDLFTS THSTVTGSKK
     AWAWVYTISY WYGSVSPGCT NQSDFSRFGS SNCAIWTGTI VALLIPATLI PVFGIIGASA
     CEKLYGQTFW MPMDIFDNWL TTNYSAGARA ATFFCGFCFV MSQISYTISN CGFASGMDLA
     GLLPKYVDIK RGAIFAACVS WACLPWNFYN SSSTFLTVMS SFGVVMTPII TVMICDNFLI
     RKRQYSVTNA FVLKGEYYFT KGVNWRAIVA WVCGMAPGLP GIAWEVNNDY FHNTGIINFF
     YGDSFFSFLI SFFVYWGLCL LFPFKITVKH DDKDYYGAFT DEEARKKGMV PYSEISEEEI
     RAYTLGECFT SGHEYKPESS DDELPELTKT SSENTKVFEI VHQKDNEKES STSSEKQIA
//