ERC1_YEAST
ID ERC1_YEAST Reviewed; 581 AA.
AC P38767; D3DKX9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Ethionine resistance-conferring protein 1;
GN Name=ERC1; OrderedLocusNames=YHR032W;
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=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
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 FUNCTION.
RX PubMed=18592490; DOI=10.1002/bit.260351107;
RA Shiomi N., Fukuda H., Fukuda Y., Murata K., Kimura A.;
RT "Production of S-adenosyl-L-methionine by Saccharomyces cerevisiae cells
RT carrying a gene for ethionine resistance.";
RL Biotechnol. Bioeng. 35:1120-1124(1990).
RN [4]
RP FUNCTION.
RX PubMed=7765914; DOI=10.1007/bf00171953;
RA Shiomi N., Fukuda H., Murata K., Kimura A.;
RT "Improvement of S-adenosylmethionine production by integration of the
RT ethionine-resistance gene into chromosomes of the yeast Saccharomyces
RT cerevisiae.";
RL Appl. Microbiol. Biotechnol. 42:730-733(1995).
RN [5]
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: Probable transporter involved in ethionine resistance.
CC Overproduction leads to accumulation of S-adenosylmethionine.
CC {ECO:0000269|PubMed:18592490, ECO:0000269|PubMed:7765914}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) (TC
CC 2.A.66.1) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00062; AAB68911.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06723.1; -; Genomic_DNA.
DR PIR; S46742; S46742.
DR RefSeq; NP_011897.1; NM_001179162.1.
DR AlphaFoldDB; P38767; -.
DR SMR; P38767; -.
DR BioGRID; 36463; 52.
DR DIP; DIP-1785N; -.
DR IntAct; P38767; 1.
DR MINT; P38767; -.
DR STRING; 4932.YHR032W; -.
DR TCDB; 2.A.66.1.5; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily.
DR PaxDb; P38767; -.
DR PRIDE; P38767; -.
DR EnsemblFungi; YHR032W_mRNA; YHR032W; YHR032W.
DR GeneID; 856427; -.
DR KEGG; sce:YHR032W; -.
DR SGD; S000001074; ERC1.
DR VEuPathDB; FungiDB:YHR032W; -.
DR eggNOG; KOG1347; Eukaryota.
DR HOGENOM; CLU_012893_1_2_1; -.
DR InParanoid; P38767; -.
DR OMA; FAIMSKQ; -.
DR BioCyc; YEAST:G3O-31092-MON; -.
DR Reactome; R-SCE-425366; Transport of bile salts and organic acids, metal ions and amine compounds.
DR ChiTaRS; ERC1; yeast.
DR PRO; PR:P38767; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38767; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015297; F:antiporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IMP:SGD.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR CDD; cd13132; MATE_eukaryotic; 1.
DR InterPro; IPR045069; MATE_euk.
DR InterPro; IPR002528; MATE_fam.
DR Pfam; PF01554; MatE; 2.
DR TIGRFAMs; TIGR00797; matE; 1.
PE 1: Evidence at protein level;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..581
FT /note="Ethionine resistance-conferring protein 1"
FT /id="PRO_0000164256"
FT TOPO_DOM 1..172
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..60
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 64209 MW; B0592C480589319B CRC64;
MSKQFSHTTN DRRSSIIYST SVGKAGLFTP ADYIPQESEE NLIEGEEQEG SEEEPSYTGN
DDETEREGEY HSLLDANNSR TLQQEAWQQG YDSHDRKRLL DEERDLLIDN KLLSQHGNGG
GDIESHGHGQ AIGPDEEERP AEIANTWESA IESGQKISTT FKRETQVITM NALPLIFTFI
LQNSLSLASI FSVSHLGTKE LGGVTLGSMT ANITGLAAIQ GLCTCLDTLC AQAYGAKNYH
LVGVLVQRCA VITILAFLPM MYVWFVWSEK ILALMIPERE LCALAANYLR VTAFGVPGFI
LFECGKRFLQ CQGIFHASTI VLFVCAPLNA LMNYLLVWND KIGIGYLGAP LSVVINYWLM
TLGLLIYAMT TKHKERPLKC WNGIIPKEQA FKNWRKMINL AIPGVVMVEA EFLGFEVLTI
FASHLGTDAL GAQSIVATIA SLAYQVPFSI SVSTSTRVAN FIGASLYDSC MITCRVSLLL
SFVCSSMNMF VICRYKEQIA SLFSTESAVV KMVVDTLPLL AFMQLFDAFN ASTAGCLRGQ
GRQKNRWVHQ PSRILLPRCA HGICVSIPVS SGCRRLMVGY N
