THI72_YEAST
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 03-AUG-2022, entry version 149.
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; Q08579; -.
DR PRIDE; Q08579; -.
DR EnsemblFungi; YOR192C_mRNA; YOR192C; YOR192C.
DR GeneID; 854364; -.
DR KEGG; sce:YOR192C; -.
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 BioCyc; YEAST:G3O-33701-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 InterPro; IPR012681; NCS1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR TIGRFAMs; TIGR00800; ncs1; 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
