ID   TNA1_YEAST              Reviewed;         534 AA.
AC   P53322; D6VV39;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 162.
DE   RecName: Full=High-affinity nicotinic acid transporter;
DE   AltName: Full=Nicotinic acid permease;
GN   Name=TNA1; OrderedLocusNames=YGR260W;
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].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=9090059;
RX   DOI=10.1002/(sici)1097-0061(19970315)13:3<287::aid-yea75>3.0.co;2-5;
RA   Clemente M.L., Sartori G., Cardazzo B., Carignani G.;
RT   "Analysis of an 11.6 kb region from the right arm of chromosome VII of
RT   Saccharomyces cerevisiae between the RAD2 and the MES1 genes reveals the
RT   presence of three new genes.";
RL   Yeast 13:287-290(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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   CHARACTERIZATION.
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   [5]
RP   UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-283, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=SUB592;
RX   PubMed=12872131; DOI=10.1038/nbt849;
RA   Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA   Roelofs J., Finley D., Gygi S.P.;
RT   "A proteomics approach to understanding protein ubiquitination.";
RL   Nat. Biotechnol. 21:921-926(2003).
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).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   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).
CC   -!- FUNCTION: Involved in the uptake of nicotinic acid.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC       permease family. {ECO:0000305}.
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DR   EMBL; Y07777; CAA69082.1; -; Genomic_DNA.
DR   EMBL; Z73044; CAA97289.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08350.1; -; Genomic_DNA.
DR   PIR; S64593; S64593.
DR   RefSeq; NP_011776.1; NM_001181389.1.
DR   AlphaFoldDB; P53322; -.
DR   SMR; P53322; -.
DR   BioGRID; 33511; 312.
DR   DIP; DIP-8004N; -.
DR   STRING; 4932.YGR260W; -.
DR   TCDB; 2.A.1.14.11; the major facilitator superfamily (mfs).
DR   iPTMnet; P53322; -.
DR   MaxQB; P53322; -.
DR   PaxDb; 4932-YGR260W; -.
DR   PeptideAtlas; P53322; -.
DR   EnsemblFungi; YGR260W_mRNA; YGR260W; YGR260W.
DR   GeneID; 853175; -.
DR   KEGG; sce:YGR260W; -.
DR   AGR; SGD:S000003492; -.
DR   SGD; S000003492; TNA1.
DR   VEuPathDB; FungiDB:YGR260W; -.
DR   eggNOG; KOG2533; Eukaryota.
DR   HOGENOM; CLU_001265_0_1_1; -.
DR   InParanoid; P53322; -.
DR   OMA; CTAWVKN; -.
DR   OrthoDB; 1405370at2759; -.
DR   BioCyc; YEAST:G3O-30929-MONOMER; -.
DR   BioGRID-ORCS; 853175; 10 hits in 10 CRISPR screens.
DR   PRO; PR:P53322; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53322; Protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR   GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IMP:SGD.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046942; P:carboxylic acid transport; IMP:SGD.
DR   GO; GO:1903222; P:quinolinic acid transmembrane transport; IMP:SGD.
DR   CDD; cd17327; MFS_FEN2_like; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 2.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR43791:SF24; HIGH-AFFINITY NICOTINIC ACID TRANSPORTER; 1.
DR   PANTHER; PTHR43791; PERMEASE-RELATED; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
PE   1: Evidence at protein level;
KW   Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation.
FT   CHAIN           1..534
FT                   /note="High-affinity nicotinic acid transporter"
FT                   /id="PRO_0000121369"
FT   TOPO_DOM        1..130
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        174..187
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        188..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        209..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..250
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        272..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        324..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        345..355
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        377..384
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        385..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        406..410
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        411..431
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        432..444
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        466..474
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        475..495
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        496..534
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          21..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CROSSLNK        283
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000269|PubMed:12872131"
SQ   SEQUENCE   534 AA;  60135 MW;  ADE7C1DE793FDAA2 CRC64;
     MSNKFTMESP KHLVDDVLFI SPTNDGSEEK PTEVTFQEDE GHDASLHNRS HDKKSELATE
     REIMATTTDD DGIPSPSHPM EKRVLRKMDI YLIPLMGMLY FLSNLDKSNI GNAEVAGLSK
     DIHLVGTQYN TCVTVFFATY VLFDPIGTNL LKIMGPPLMM SICLTCFGAI SLGTAWVKNY
     AQLIVVRLLL GAFEGMIYPA INMYLSVCYR REQYALRFAF VFSAACLSSS FGGLIAYGCS
     KISGSLKDWQ YIYIVEGCIS LGFVPFYAFG LSKNLEDSWF FNKEEKEYIS ERYKTMNTFD
     PDEKFEWFQV WQAVKDVKTW ASAVALFGID LTTFGLTVFL PIIITSMGFT NVRAQLMTVP
     IYFLTAIVFF ICAVWSDRIK LRSPFILGAC LTTSIGIAIV LGSQVHGVRY FGVYILCMGI
     YVNAACNCLW LSGNTGNYFK RATALGINLF FGSGSGLVSG QIFVAKDKPR YIKGLSISLA
     FQVFSIFMTV VQIFLYKREN DKKKAIIDRC NELGEPIPYD ERLSDKNPEF KYMY
//