ATR1_YEAST
ID ATR1_YEAST Reviewed; 542 AA.
AC P13090; D6W0G8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Aminotriazole resistance protein;
GN Name=ATR1; Synonyms=SNQ1; OrderedLocusNames=YML116W; ORFNames=YM8339.03;
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].
RX PubMed=3280970; DOI=10.1128/mcb.8.2.664-673.1988;
RA Kanazawa S., Driscoll M., Struhl K.;
RT "ATR1, a Saccharomyces cerevisiae gene encoding a transmembrane protein
RT required for aminotriazole resistance.";
RL Mol. Cell. Biol. 8:664-673(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 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 [5]
RP CHARACTERIZATION.
RX PubMed=2123132; DOI=10.1007/bf00321122;
RA Goempel-Klein P., Brendel M.;
RT "Allelism of SNQ1 and ATR1, genes of the yeast Saccharomyces cerevisiae
RT required for controlling sensitivity to 4-nitroquinoline-N-oxide and
RT aminotriazole.";
RL Curr. Genet. 18:93-96(1990).
RN [6]
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 [7]
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 [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).
CC -!- FUNCTION: Putative component of the machinery responsible for pumping
CC aminotriazole (and possibly other toxic compounds) out of the cell.
CC Probable ATP-dependent export permease. Appears to confer resistance
CC only to aminotriazole.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- DOMAIN: Deletion of the C-terminal 34 residues abolishes ATR1 activity,
CC while deletion of the C-terminal 23 residues have a minor effect.
CC -!- MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; M20319; AAA34449.1; -; Genomic_DNA.
DR EMBL; Z49210; CAA89102.1; -; Genomic_DNA.
DR EMBL; AY723850; AAU09767.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09782.1; -; Genomic_DNA.
DR PIR; S53956; S53956.
DR RefSeq; NP_013591.1; NM_001182478.1.
DR AlphaFoldDB; P13090; -.
DR SMR; P13090; -.
DR BioGRID; 35088; 25.
DR DIP; DIP-3953N; -.
DR IntAct; P13090; 4.
DR MINT; P13090; -.
DR STRING; 4932.YML116W; -.
DR TCDB; 2.A.1.3.1; the major facilitator superfamily (mfs).
DR iPTMnet; P13090; -.
DR MaxQB; P13090; -.
DR PaxDb; P13090; -.
DR EnsemblFungi; YML116W_mRNA; YML116W; YML116W.
DR GeneID; 854924; -.
DR KEGG; sce:YML116W; -.
DR SGD; S000004584; ATR1.
DR VEuPathDB; FungiDB:YML116W; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000176573; -.
DR HOGENOM; CLU_000960_27_4_1; -.
DR InParanoid; P13090; -.
DR OMA; IWGMVIG; -.
DR BioCyc; YEAST:G3O-32697-MON; -.
DR PRO; PR:P13090; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P13090; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0005773; C:vacuole; IDA:SGD.
DR GO; GO:0080139; F:borate efflux transmembrane transporter activity; IMP:SGD.
DR GO; GO:0046713; P:borate transport; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..542
FT /note="Aminotriazole resistance protein"
FT /id="PRO_0000173367"
FT TOPO_DOM 1..108
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..136
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 158..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..198
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..371
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..399
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..542
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 531..542
FT /note="ARAAAEYDCTVA -> QELLQNTIALWLSGKRY (in Ref. 1;
FT AAA34449)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 542 AA; 59983 MW; 5DDA45815068CD41 CRC64;
MGNQSLVVLT ESKGEYENET ELPVKKSSRD NNIGESLTAT AFTQSEDEMV DSNQKWQNPN
YFKYAWQEYL FIFTCMISQL LNQAGTTQTL SIMNILSDSF GSEGNSKSWL MASFPLVSGS
FILISGRLGD IYGLKKMLLV GYVLVIIWSL ICGITKYSGS DTFFIISRAF QGLGIAFVLP
NVLGIIGNIY VGGTFRKNIV ISFVGAMAPI GATLGCLFAG LIGTEDPKQW PWAFYAYSIA
AFINFVLSIY AIPSTIPTNI HHFSMDWIGS VLGVIGLILL NFVWNQAPIS GWNQAYIIVI
LIISVIFLVV FIIYEIRFAK TPLLPRAVIK DRHMIQIMLA LFFGWGSFGI FTFYYFQFQL
NIRQYTALWA GGTYFMFLIW GIIAALLVGF TIKNVSPSVF LFFSMVAFNV GSIMASVTPV
HETYFRTQLG TMIILSFGMD LSFPASSIIF SDNLPMEYQG MAGSLVNTVV NYSMSLCLGM
GATVETQVNS DGKHLLKGYR GAQYLGIGLA SLACMISGLY MVESFIKGRR ARAAAEYDCT
VA
