THI73_YEAST
ID THI73_YEAST Reviewed; 523 AA.
AC Q07904; D6VY06;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Thiamine pathway transporter THI73;
GN Name=THI73; OrderedLocusNames=YLR004C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 INDUCTION.
RX PubMed=10869563; DOI=10.1016/s0014-5793(00)01698-7;
RA Llorente B., Dujon B.;
RT "Transcriptional regulation of the Saccharomyces cerevisiae DAL5 gene
RT family and identification of the high affinity nicotinic acid permease TNA1
RT (YGR260w).";
RL FEBS Lett. 475:237-241(2000).
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).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16850348; DOI=10.1007/s00438-006-0130-z;
RA Mojzita D., Hohmann S.;
RT "Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 276:147-161(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
CC -!- FUNCTION: Transports either thiamine or, rather, a related metabolite
CC involved in the thiamine biosynthesis pathway.
CC {ECO:0000269|PubMed:16850348}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16850348}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:16850348}. Cell membrane
CC {ECO:0000305|PubMed:16850348}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:16850348}.
CC -!- INDUCTION: Induced by limited extracellular thiamine levels.
CC {ECO:0000269|PubMed:10869563, ECO:0000269|PubMed:16194233}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC permease family. {ECO:0000305}.
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DR EMBL; Z73176; CAA97526.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09322.1; -; Genomic_DNA.
DR PIR; S64826; S64826.
DR RefSeq; NP_013104.1; NM_001181891.1.
DR AlphaFoldDB; Q07904; -.
DR SMR; Q07904; -.
DR BioGRID; 31277; 47.
DR DIP; DIP-8846N; -.
DR STRING; 4932.YLR004C; -.
DR TCDB; 2.A.1.14.36; the major facilitator superfamily (mfs).
DR PaxDb; Q07904; -.
DR PRIDE; Q07904; -.
DR EnsemblFungi; YLR004C_mRNA; YLR004C; YLR004C.
DR GeneID; 850690; -.
DR KEGG; sce:YLR004C; -.
DR SGD; S000003994; THI73.
DR VEuPathDB; FungiDB:YLR004C; -.
DR eggNOG; KOG2533; Eukaryota.
DR HOGENOM; CLU_001265_0_5_1; -.
DR InParanoid; Q07904; -.
DR OMA; ITNIYIW; -.
DR BioCyc; YEAST:G3O-32165-MON; -.
DR PRO; PR:Q07904; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07904; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0022857; F:transmembrane transporter activity; ISS:SGD.
DR GO; GO:0055085; P:transmembrane transport; ISS:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..523
FT /note="Thiamine pathway transporter THI73"
FT /id="PRO_0000247182"
FT TOPO_DOM 1..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..141
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..176
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..207
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..345
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..400
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..432
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..466
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 523 AA; 58531 MW; 8D6289D98C2ED493 CRC64;
MKNMSQRSMD VEKKAANADS CSVSTSSINV DDADVALRFL KQNGLDESST ANEDDVVAGE
EANFYGSHEL SPKVLRKVDL FILPFLCCTY LLMFLDKALL NYAASMGIKD HLKGNEFSNL
GTIFSAAYIF MEPVVTYLIQ KFPISKILGT FITVWGIVLA CHAACKTYAS LMVVRTLLGL
FESSSAVGCI AISGMYYTKS EQSARIGFWA TQAGTGYIVG GLISFGFLHY HGTAFTSWQI
MFLVVGLVTV AFGVLTFLYL PDNVTNAWFL NKEEKIQVVE HIRANQTGLE TKKFKKQQVK
ELFLHDKFTW PMLLLTACSQ ISTGAIGTFS VTITGTFGFD KYETALLQLP IGAITAMIIL
ITTQMLSRWG HITLITTSMY IPAIIGCIVL ISLPLSHKIG NLFSLYLLYS GSCVITNIYI
WNSCNTSGYT KRVFRNAITM IVYNVSCIIA PQMFRAYSAP RYIPAKIALL VTQCVCVPLQ
LYIGYICKKE NEKRDKEQEG QERKKYQFLD LTDIENRNFR YIY
