NRT1_YEAST
ID NRT1_YEAST Reviewed; 598 AA.
AC Q08485; D6W2D4; O00029;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Nicotinamide riboside transporter 1;
DE AltName: Full=Thiamine transport protein 71;
GN Name=NRT1; Synonyms=THI71; OrderedLocusNames=YOR071C; ORFNames=YOR29-22;
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 [GENOMIC DNA].
RX PubMed=9133743;
RX DOI=10.1002/(sici)1097-0061(19970330)13:4<379::aid-yea85>3.0.co;2-g;
RA Valens M., Bohn C., Daignan-Fornier B., Dang V.-D., Bolotin-Fukuhara M.;
RT "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT presence of two tRNAs and 24 new open reading frames.";
RL Yeast 13:379-390(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP FUNCTION.
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 FUNCTION.
RX PubMed=16845689; DOI=10.1002/yea.1387;
RA Paluszynski J.P., Klassen R., Rohe M., Meinhardt F.;
RT "Various cytosine/adenine permease homologues are involved in the toxicity
RT of 5-fluorocytosine in Saccharomyces cerevisiae.";
RL Yeast 23:707-715(2006).
RN [7]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND INDUCTION.
RX PubMed=18258590; DOI=10.1074/jbc.c800021200;
RA Belenky P.A., Moga T.G., Brenner C.;
RT "Saccharomyces cerevisiae YOR071C encodes the high affinity nicotinamide
RT riboside transporter Nrt1.";
RL J. Biol. Chem. 283:8075-8079(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP FUNCTION.
RX PubMed=19416965; DOI=10.1074/jbc.m109.004010;
RA Lu S.P., Kato M., Lin S.J.;
RT "Assimilation of endogenous nicotinamide riboside is essential for calorie
RT restriction-mediated life span extension in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 284:17110-17119(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [11]
RP FUNCTION.
RX PubMed=21349851; DOI=10.1074/jbc.m110.217885;
RA Lu S.P., Lin S.J.;
RT "Phosphate responsive signaling pathway is a novel component of NAD+
RT metabolism in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 286:14271-14281(2011).
CC -!- FUNCTION: High-affinity pH-dependent nicotinamide riboside transporter
CC which also transports thiamine with low affinity. Involved in 5-
CC fluorocytosine sensitivity. {ECO:0000269|PubMed:16845689,
CC ECO:0000269|PubMed:16850348, ECO:0000269|PubMed:18258590,
CC ECO:0000269|PubMed:19416965, ECO:0000269|PubMed:21349851,
CC ECO:0000269|PubMed:9235906}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=21 uM for nicotinamide riboside {ECO:0000269|PubMed:18258590};
CC pH dependence:
CC Optimum pH is 3.5-6.5. {ECO:0000269|PubMed:18258590};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- INDUCTION: Expression is controlled by the transcription repressors
CC SUM1, HST1 and RFM1. {ECO:0000269|PubMed:18258590}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR EMBL; Z70678; CAA94556.1; -; Genomic_DNA.
DR EMBL; Z74979; CAA99264.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10850.1; -; Genomic_DNA.
DR PIR; S66954; S66954.
DR RefSeq; NP_014714.1; NM_001183490.1.
DR AlphaFoldDB; Q08485; -.
DR SMR; Q08485; -.
DR BioGRID; 34470; 74.
DR DIP; DIP-7934N; -.
DR IntAct; Q08485; 1.
DR MINT; Q08485; -.
DR STRING; 4932.YOR071C; -.
DR TCDB; 2.A.39.4.2; the nucleobase:cation symporter-1 (ncs1) family.
DR iPTMnet; Q08485; -.
DR MaxQB; Q08485; -.
DR PaxDb; Q08485; -.
DR PRIDE; Q08485; -.
DR EnsemblFungi; YOR071C_mRNA; YOR071C; YOR071C.
DR GeneID; 854237; -.
DR KEGG; sce:YOR071C; -.
DR SGD; S000005597; NRT1.
DR VEuPathDB; FungiDB:YOR071C; -.
DR eggNOG; KOG2466; Eukaryota.
DR GeneTree; ENSGT00940000176299; -.
DR HOGENOM; CLU_021555_3_0_1; -.
DR InParanoid; Q08485; -.
DR OMA; WEVNNNY; -.
DR BioCyc; YEAST:G3O-33610-MON; -.
DR PRO; PR:Q08485; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08485; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:SGD.
DR GO; GO:1903089; F:5-amino-1-ribofuranosylimidazole-4-carboxamide transmembrane transporter activity; IMP:SGD.
DR GO; GO:0034257; F:nicotinamide riboside transmembrane transporter activity; IMP: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; IMP:SGD.
DR GO; GO:0034258; P:nicotinamide riboside transport; IMP: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 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..598
FT /note="Nicotinamide riboside transporter 1"
FT /id="PRO_0000197927"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
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 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
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 MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 598 AA; 67193 MW; 7EB67439C7D5EB6B CRC64;
MSFSSIVSKF LRYLEIPAKN RTAVNFLRNP DLQPIKSANQ TWGFWSNLAY WGAVSFTAGT
WMSGSAALSV GLSYPETIVS FLLGNVLTII FTMANSYPGY DWKIGFTLAQ RFVFGIYGSA
FGIIIRILMS IVNYGSNAWL GGLSINMILD SWSHHYLHLP NTLSPSVAMT TKQLVGFIIF
HVLTALCYFM KPYHMNYLLI WSCVATCFAM LGIVIYLTKN AHGVGELFTS TKSTVTGSKR
AWAWVYMISY WFGSISPGST NQSDYSRFGS SNLAIWTGSV CALLIPATLV PIFGVISAST
CDKLYGKQFW MPMDIFDYWL TNNYSAGARA GAFFCGLCFT MSQMSSTISN CGFATGMDMA
GLLPKYVDIK RGALFCACIS WACLPWNFYN SSSTFLTVMS SFGVVMTPII AVMICDNFLI
RKRQYSITNA FILKGEYYFT KGVNWRAIVA WVCGMAPGLP GIAWEVNNNY FHDSGIVKFF
YGDSFFSFLI SFFVYWGLCV FFPFKITVRH DDKDYYGAFT DEEARKKGMI PYSEISEEEI
RAYTLGECYT TGHEYKPESS DNESPELIKT SSENTNVFEI VHQKDDEKHS FSTTQQVV
