TAT2_YEAST
ID TAT2_YEAST Reviewed; 592 AA.
AC P38967; D6W245;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Tryptophan permease;
DE AltName: Full=Tryptophan amino acid transporter;
GN Name=TAT2; Synonyms=LTG3, SAB2, SCM2, TAP2; OrderedLocusNames=YOL020W;
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=JK9-3D;
RX PubMed=7523855; DOI=10.1128/mcb.14.10.6597-6606.1994;
RA Schmidt A., Hall M.N., Koller A.;
RT "Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1
RT and TAT2, encode amino acid permeases mediating tyrosine and tryptophan
RT uptake.";
RL Mol. Cell. Biol. 14:6597-6606(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8058037; DOI=10.1007/bf00285453;
RA Chen X.H., Xiao Z., Fitzgerald-Hayes M.;
RT "SCM2, a tryptophan permease in Saccharomyces cerevisiae, is important for
RT cell growth.";
RL Mol. Gen. Genet. 244:260-268(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IFO 10151 / YNN140;
RA Kawamura D., Yamashita I., Nimi O., Toh-e A.;
RT "Cloning and nucleotide sequence of a gene conferring ability to grow at a
RT low temperature on Saccharomyces cerevisiae tryptophan auxotroph.";
RL J. Ferment. Bioeng. 77:1-9(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Shin Y.H., Goo D.M., So I.S., Rhode P.R., Campbell J.L., Kim J.;
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
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 [7]
RP FUNCTION IN L-CYSTEINE UPTAKE.
RX PubMed=10467005; DOI=10.1007/s002940050459;
RA During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C.,
RA Hansen J.;
RT "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple
RT permeases.";
RL Curr. Genet. 35:609-617(1999).
RN [8]
RP FUNCTION.
RX PubMed=10654085; DOI=10.1007/s002940050506;
RA Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
RT "Substrate specificity and gene expression of the amino-acid permeases in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 36:317-328(1999).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
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: Required for high-affinity tryptophan transport. Also
CC transports cysteine, phenyalanine and tyrosine.
CC {ECO:0000269|PubMed:10467005, ECO:0000269|PubMed:10654085}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; X79150; CAA55777.1; -; Genomic_DNA.
DR EMBL; L33461; AAA60324.1; -; Genomic_DNA.
DR EMBL; D16304; BAA03811.1; -; Genomic_DNA.
DR EMBL; U66834; AAB07526.1; -; Genomic_DNA.
DR EMBL; Z74761; CAA99019.1; -; Genomic_DNA.
DR EMBL; Z74762; CAA99020.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10761.1; -; Genomic_DNA.
DR PIR; S46273; S46273.
DR RefSeq; NP_014622.1; NM_001183274.1.
DR AlphaFoldDB; P38967; -.
DR SMR; P38967; -.
DR BioGRID; 34382; 102.
DR DIP; DIP-1782N; -.
DR IntAct; P38967; 4.
DR MINT; P38967; -.
DR STRING; 4932.YOL020W; -.
DR TCDB; 2.A.3.10.8; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P38967; -.
DR SwissPalm; P38967; -.
DR MaxQB; P38967; -.
DR PaxDb; P38967; -.
DR PRIDE; P38967; -.
DR TopDownProteomics; P38967; -.
DR EnsemblFungi; YOL020W_mRNA; YOL020W; YOL020W.
DR GeneID; 854139; -.
DR KEGG; sce:YOL020W; -.
DR SGD; S000005380; TAT2.
DR VEuPathDB; FungiDB:YOL020W; -.
DR eggNOG; KOG1286; Eukaryota.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P38967; -.
DR OMA; HLIMIAI; -.
DR BioCyc; YEAST:G3O-33436-MON; -.
DR PRO; PR:P38967; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38967; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015173; F:aromatic amino acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0005300; F:high-affinity tryptophan transmembrane transporter activity; IMP:SGD.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0015801; P:aromatic amino acid transport; IDA:SGD.
DR GO; GO:0015827; P:tryptophan transport; IMP:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR Pfam; PF00324; AA_permease; 1.
DR SUPFAM; SSF55205; SSF55205; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..592
FT /note="Tryptophan permease"
FT /id="PRO_0000054160"
FT TOPO_DOM 1..87
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..160
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 182..192
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..226
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 248..266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 288..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 328..358
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..514
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 536..592
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 187
FT /note="Q -> T (in Ref. 3; BAA03811)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 592 AA; 65404 MW; A233BAD16264B319 CRC64;
MTEDFISSVK RSNEELKERK SNFGFVEYKS KQLTSSSSHN SNSSHHDDDN QHGKRNIFQR
CVDSFKSPLD GSFDTSNLKR TLKPRHLIMI AIGGSIGTGL FVGSGKAIAE GGPLGVVIGW
AIAGSQIIGT IHGLGEITVR FPVVGAFANY GTRFLDPSIS FVVSTIYVLQ WFFVLPLEII
AAAMTVQYWN SSIDPVIWVA IFYAVIVSIN LFGVRGFGEA EFAFSTIKAI TVCGFIILCV
VLICGGGPDH EFIGAKYWHD PGCLANGFPG VLSVLVVASY SLGGIEMTCL ASGETDPKGL
PSAIKQVFWR ILFFFLISLT LVGFLVPYTN QNLLGGSSVD NSPFVIAIKL HHIKALPSIV
NAVILISVLS VGNSCIFASS RTLCSMAHQG LIPWWFGYID RAGRPLVGIM ANSLFGLLAF
LVKSGSMSEV FNWLMAIAGL ATCIVWLSIN LSHIRFRLAM KAQGKSLDEL EFVSAVGIWG
SAYSALINCL ILIAQFYCSL WPIGGWTSGK ERAKIFFQNY LCALIMLFIF IVHKIYYKCQ
TGKWWGVKAL KDIDLETDRK DIDIEIVKQE IAEKKMYLDS RPWYVRQFHF WC
