YCT1_YEAST
ID YCT1_YEAST Reviewed; 531 AA.
AC Q12235; D6VXV3;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=High affinity cysteine transporter;
GN Name=YCT1; OrderedLocusNames=YLL055W; ORFNames=L0578;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP INDUCTION.
RX PubMed=11113969;
RX DOI=10.1002/1097-0061(200012)16:16<1457::aid-yea635>3.0.co;2-3;
RA Ahmed Khan S., Zhang N., Ismail T., El-Moghazy A.-N., Butt A., Wu J.,
RA Merlotti C., Hayes A., Gardner D.C.J., Oliver S.G.;
RT "Functional analysis of eight open reading frames on chromosomes XII and
RT XIV of Saccharomyces cerevisiae.";
RL Yeast 16:1457-1468(2000).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=17435223; DOI=10.1534/genetics.107.070342;
RA Kaur J., Bachhawat A.K.;
RT "Yct1p, a novel, high-affinity, cysteine-specific transporter from the
RT yeast Saccharomyces cerevisiae.";
RL Genetics 176:877-890(2007).
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 INDUCTION.
RX PubMed=18794233; DOI=10.1093/toxsci/kfn193;
RA Pereira Y., Lagniel G., Godat E., Baudouin-Cornu P., Junot C., Labarre J.;
RT "Chromate causes sulfur starvation in yeast.";
RL Toxicol. Sci. 106:400-412(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-500 AND SER-501, 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 INDUCTION.
RX PubMed=20233714; DOI=10.1074/jbc.m110.121947;
RA Staschke K.A., Dey S., Zaborske J.M., Palam L.R., McClintick J.N., Pan T.,
RA Edenberg H.J., Wek R.C.;
RT "Integration of general amino acid control and target of rapamycin (TOR)
RT regulatory pathways in nitrogen assimilation in yeast.";
RL J. Biol. Chem. 285:16893-16911(2010).
CC -!- FUNCTION: High affinity cysteine-specific transporter. Major
CC contributor to cysteine transport when cysteine, at low concentrations,
CC is provided as the sole sulfur source. {ECO:0000269|PubMed:17435223}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55.4 uM for cysteine {ECO:0000269|PubMed:17435223};
CC Vmax=22.4 nmol/min/mg enzyme for cysteine transport
CC {ECO:0000269|PubMed:17435223};
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced under nitrogen starvation conditions, co-regulated
CC by GCN4 and GLN3. Regulated by the MET4-based sulfur regulatory
CC network. Expression is maximum in nonrepressing sulfur conditions and
CC considerably repressed in the presence of organic sulfur. Induced by
CC chromate. {ECO:0000269|PubMed:11113969, ECO:0000269|PubMed:17435223,
CC ECO:0000269|PubMed:18794233, ECO:0000269|PubMed:20233714}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Allantoate
CC permease family. {ECO:0000305}.
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DR EMBL; Z47973; CAA88002.1; -; Genomic_DNA.
DR EMBL; Z73160; CAA97508.1; -; Genomic_DNA.
DR EMBL; AY692634; AAT92653.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09269.1; -; Genomic_DNA.
DR PIR; S50965; S50965.
DR RefSeq; NP_013045.1; NM_001181875.1.
DR AlphaFoldDB; Q12235; -.
DR SMR; Q12235; -.
DR BioGRID; 31260; 51.
DR MINT; Q12235; -.
DR STRING; 4932.YLL055W; -.
DR TCDB; 2.A.1.14.20; the major facilitator superfamily (mfs).
DR iPTMnet; Q12235; -.
DR PaxDb; Q12235; -.
DR PRIDE; Q12235; -.
DR EnsemblFungi; YLL055W_mRNA; YLL055W; YLL055W.
DR GeneID; 850671; -.
DR KEGG; sce:YLL055W; -.
DR SGD; S000003978; YCT1.
DR VEuPathDB; FungiDB:YLL055W; -.
DR eggNOG; KOG2533; Eukaryota.
DR HOGENOM; CLU_001265_0_5_1; -.
DR InParanoid; Q12235; -.
DR OMA; FLHCTAY; -.
DR BioCyc; YEAST:G3O-32154-MON; -.
DR SABIO-RK; Q12235; -.
DR PRO; PR:Q12235; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12235; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA: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:0033229; F:cysteine transmembrane transporter activity; IDA:SGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042883; P:cysteine transport; IDA: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 Amino-acid transport; Cell membrane; Coiled coil; Endoplasmic reticulum;
KW Glycoprotein; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..531
FT /note="High affinity cysteine transporter"
FT /id="PRO_0000247151"
FT TOPO_DOM 1..54
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..97
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 98..118
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 119..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..154
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..218
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..285
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..324
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..373
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..378
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 414..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..447
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT COILED 469..498
FT /evidence="ECO:0000255"
FT MOD_RES 500
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 501
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 531 AA; 58905 MW; 7C008873BBB54A0D CRC64;
MSKVDVKIGA DSISSSDEIL VPSRLADVTL AFMEENDAAV PEITPEQEKK LKRKLFLTIF
TFVSAINLLL YMDKATLSYD SILGFFEDTG LTQNTYNTVN TLFYVGFAIG QFPGQYLAQK
LPLGKFLGGL LATWTILIFL SCTAYNFSGV VALRFFLGLT ESVVIPILIT TMGMFFDASE
RAAAQPFFFA ACMGSPIPTG FIAYGVLHIT NPSISLWKIF TIIIGGLTFI MTVVVILWFP
NNPADVKFFS IQERVWIIRR VQASTGSSIE QKVFKKSQFR EAMKDYITWL FGLFFLLQQL
ANNLPYQQNL LFEGMGGVDA LGSTLVSVAG AGFAVVCAFI ATLMLAKWKN ISALTAIFWT
LPALVGSIAA AALPWDNKIG ILANICMAGQ IFGIPFIIAL SWASSSASGY TKKLTRSSVS
LFAMGIANII SPQIWREKDS PRFLPAWIVQ IVLSFSLAPA ILLLIHFILK RRNNQRLKNY
DENLQNYLDR IQLIESENPS SIEEGKVVTH ENNLAVFDLT DLENETFIYP L
