TNA1_YEAST
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 03-AUG-2022, entry version 154.
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 BioGRID; 33511; 297.
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; P53322; -.
DR PRIDE; P53322; -.
DR EnsemblFungi; YGR260W_mRNA; YGR260W; YGR260W.
DR GeneID; 853175; -.
DR KEGG; sce:YGR260W; -.
DR SGD; S000003492; TNA1.
DR VEuPathDB; FungiDB:YGR260W; -.
DR eggNOG; KOG2533; Eukaryota.
DR HOGENOM; CLU_001265_0_1_1; -.
DR InParanoid; P53322; -.
DR OMA; FTAYMSD; -.
DR BioCyc; YEAST:G3O-30929-MON; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031224; C:intrinsic component of membrane; IBA:GO_Central.
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 Gene3D; 1.20.1250.20; -; 2.
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 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
