ARR3_YEAST
ID ARR3_YEAST Reviewed; 404 AA.
AC Q06598; D6W4J9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Arsenical-resistance protein 3 {ECO:0000305};
DE AltName: Full=Arsenic compounds resistance protein 3 {ECO:0000303|PubMed:9234670};
DE AltName: Full=As(III)/H(+) and Sb(III)/H(+)antiporter {ECO:0000305};
GN Name=ARR3 {ECO:0000312|SGD:S000006405};
GN Synonyms=ACR3 {ECO:0000303|PubMed:9234670};
GN OrderedLocusNames=YPR201W {ECO:0000312|SGD:S000006405}; ORFNames=P9677.2;
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], AND FUNCTION.
RX PubMed=9234670;
RX DOI=10.1002/(sici)1097-0061(199707)13:9<819::aid-yea142>3.0.co;2-y;
RA Bobrowicz P., Wysocki R., Owsianik G., Goffeau A., Ulaszewski S.;
RT "Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in
RT resistance to arsenic compounds in the yeast Saccharomyces cerevisiae.";
RL Yeast 13:819-828(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9374482; DOI=10.1074/jbc.272.48.30061;
RA Wysocki R., Bobrowicz P., Ulaszewski S.;
RT "The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane protein
RT involved in arsenite transport.";
RL J. Biol. Chem. 272:30061-30066(1997).
RN [5]
RP INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20655873; DOI=10.1016/j.bbamem.2010.07.017;
RA Maciaszczyk-Dziubinska E., Wawrzycka D., Sloma E., Migocka M., Wysocki R.;
RT "The yeast permease Acr3p is a dual arsenite and antimonite plasma membrane
RT transporter.";
RL Biochim. Biophys. Acta 1798:2170-2175(2010).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=21447319; DOI=10.1016/j.bbamem.2011.03.014;
RA Maciaszczyk-Dziubinska E., Migocka M., Wysocki R.;
RT "Acr3p is a plasma membrane antiporter that catalyzes As(III)/H(+) and
RT Sb(III)/H(+) exchange in Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1808:1855-1859(2011).
RN [7]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=22380876; DOI=10.1111/j.1469-8137.2012.04092.x;
RA Ali W., Isner J.C., Isayenkov S.V., Liu W., Zhao F.J., Maathuis F.J.;
RT "Heterologous expression of the yeast arsenite efflux system ACR3 improves
RT Arabidopsis thaliana tolerance to arsenic stress.";
RL New Phytol. 194:716-723(2012).
RN [8]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=22107880; DOI=10.1093/pcp/pcr161;
RA Duan G., Kamiya T., Ishikawa S., Arao T., Fujiwara T.;
RT "Expressing ScACR3 in rice enhanced arsenite efflux and reduced arsenic
RT accumulation in rice grains.";
RL Plant Cell Physiol. 53:154-163(2012).
RN [9]
RP MUTAGENESIS OF CYS-90; CYS-151; CYS-169; CYS-192; CYS-283; CYS-316;
RP CYS-318; CYS-333 AND CYS-344, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=24291645; DOI=10.1016/j.bbamem.2013.11.013;
RA Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D., Markowska K.,
RA Wysocki R.;
RT "Multiple cysteine residues are necessary for sorting and transport
RT activity of the arsenite permease Acr3p from Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1838:747-755(2014).
RN [10]
RP MUTAGENESIS OF ASN-117; ARG-150; TRP-158; ASN-176; ARG-230; PHE-266;
RP TYR-290; PHE-345; SER-349; ASN-351; PHE-352; GLU-353 AND GLU-380,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=26123064; DOI=10.1111/mmi.13113;
RA Markowska K., Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D.,
RA Wysocki R.;
RT "Identification of critical residues for transport activity of Acr3p, the
RT Saccharomyces cerevisiae As(III)/H(+) antiporter.";
RL Mol. Microbiol. 98:162-174(2015).
CC -!- FUNCTION: Plasma membrane transporter that confers resistance to toxic
CC metalloids by mediating extrusion of arsenite (As(III)) and antimonite
CC (Sb(III)) out of cells. Displays low-affinity As(III)/H(+) and
CC Sb(III)/H(+) exchange activity. {ECO:0000269|PubMed:20655873,
CC ECO:0000269|PubMed:21447319, ECO:0000269|PubMed:22107880,
CC ECO:0000269|PubMed:22380876, ECO:0000269|PubMed:24291645,
CC ECO:0000269|PubMed:26123064, ECO:0000269|PubMed:9234670,
CC ECO:0000269|PubMed:9374482}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 mM for arsenite export {ECO:0000269|PubMed:21447319};
CC KM=2 mM for antimonite export {ECO:0000269|PubMed:21447319};
CC Note=Vmax for arsenite is approximately 3 times higher than for
CC antimonite. {ECO:0000269|PubMed:21447319};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20655873,
CC ECO:0000269|PubMed:21447319, ECO:0000269|PubMed:24291645,
CC ECO:0000269|PubMed:26123064, ECO:0000305|PubMed:9374482}; Multi-pass
CC membrane protein {ECO:0000255, ECO:0000305|PubMed:9374482}.
CC -!- INDUCTION: Expression is highly induced by arsenite and antimonite.
CC {ECO:0000269|PubMed:20655873}.
CC -!- DISRUPTION PHENOTYPE: Leads to sensitivity to antimony, tellurite,
CC cadmium, and phenylarsine oxide. {ECO:0000269|PubMed:9374482}.
CC -!- BIOTECHNOLOGY: Heterologous expression endows plants with greater
CC arsenic resistance by enhancing arsenite efflux. Reduces arsenic
CC accumulation in rice grains (PubMed:22107880). Does not lower
CC significantly arsenic tissue levels in Arabidopsis (PubMed:22380876).
CC {ECO:0000269|PubMed:22107880, ECO:0000269|PubMed:22380876}.
CC -!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC 2.A.59)
CC family. {ECO:0000305}.
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DR EMBL; U25841; AAB64629.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11615.1; -; Genomic_DNA.
DR PIR; S58830; S58830.
DR RefSeq; NP_015527.1; NM_001184298.1.
DR AlphaFoldDB; Q06598; -.
DR BioGRID; 36371; 91.
DR DIP; DIP-3797N; -.
DR IntAct; Q06598; 3.
DR MINT; Q06598; -.
DR STRING; 4932.YPR201W; -.
DR TCDB; 2.A.59.1.1; the arsenical resistance-3 (acr3) family.
DR iPTMnet; Q06598; -.
DR PaxDb; Q06598; -.
DR PRIDE; Q06598; -.
DR EnsemblFungi; YPR201W_mRNA; YPR201W; YPR201W.
DR GeneID; 856331; -.
DR KEGG; sce:YPR201W; -.
DR SGD; S000006405; ARR3.
DR VEuPathDB; FungiDB:YPR201W; -.
DR eggNOG; ENOG502QPKH; Eukaryota.
DR GeneTree; ENSGT00950000182808; -.
DR HOGENOM; CLU_022869_0_0_1; -.
DR InParanoid; Q06598; -.
DR OMA; CTAMVLM; -.
DR BioCyc; MetaCyc:G3O-34321-MON; -.
DR BioCyc; YEAST:G3O-34321-MON; -.
DR PRO; PR:Q06598; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06598; protein.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015104; F:antimonite transmembrane transporter activity; IMP:SGD.
DR GO; GO:0015297; F:antiporter activity; IMP:SGD.
DR GO; GO:0015105; F:arsenite transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015699; P:antimonite transport; IMP:SGD.
DR GO; GO:0015700; P:arsenite transport; IMP:SGD.
DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1530.20; -; 1.
DR InterPro; IPR004706; Arsenical-R_Acr3.
DR InterPro; IPR002657; BilAc:Na_symport/Acr3.
DR InterPro; IPR038770; Na+/solute_symporter_sf.
DR PANTHER; PTHR43057; PTHR43057; 1.
DR Pfam; PF01758; SBF; 1.
DR PIRSF; PIRSF005508; Acr3; 1.
DR TIGRFAMs; TIGR00832; acr3; 1.
PE 1: Evidence at protein level;
KW Antiport; Arsenical resistance; Cell membrane; Glycoprotein; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..404
FT /note="Arsenical-resistance protein 3"
FT /id="PRO_0000064440"
FT TOPO_DOM 1..34
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 56..69
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..169
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 191..216
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..245
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..280
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..369
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:9374482"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 391..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9374482"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 90
FT /note="C->A: Leads to ER retention and arsenite
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 117
FT /note="N->A: Impairs cell membrane localization, and leads
FT to arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 150
FT /note="R->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 151
FT /note="C->V: Leads to complete loss of metalloid transport
FT function."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 158
FT /note="W->A: Impairs cell membrane localization, and leads
FT to arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 169
FT /note="C->A: Greatly reduces arsenite efflux."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 176
FT /note="N->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 192
FT /note="C->A: Results in moderate reduction of arsenite
FT transport capacities and sorting perturbations."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 230
FT /note="R->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 266
FT /note="F->A: Impairs arsenite resistance."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 283
FT /note="C->A: Does not alter the arsenite/proton exchange
FT across the plasma membrane."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 290
FT /note="Y->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 316
FT /note="C->A: Results in moderate reduction of arsenite
FT transport capacities and sorting perturbations."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 318
FT /note="C->A: Results in moderate reduction of arsenite
FT transport capacities and sorting perturbations."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 333
FT /note="C->A: Results in moderate reduction of arsenite
FT transport capacities and sorting perturbations."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 344
FT /note="C->A: Results in moderate reduction of arsenite
FT transport capacities and sorting perturbations."
FT /evidence="ECO:0000269|PubMed:24291645"
FT MUTAGEN 345
FT /note="F->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 349
FT /note="S->A: Impairs arsenite resistance."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 351
FT /note="N->A: Leads to ER retention, protein unstability and
FT arsenite sensitivity."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 352
FT /note="F->A: Impairs arsenite resistance."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 353
FT /note="E->A: Impairs arsenite resistance."
FT /evidence="ECO:0000269|PubMed:26123064"
FT MUTAGEN 380
FT /note="E->A: Impairs arsenite resistance."
FT /evidence="ECO:0000269|PubMed:26123064"
SQ SEQUENCE 404 AA; 45848 MW; 1BE290E26772B4CA CRC64;
MSEDQKSENS VPSKVNMVNR TDILTTIKSL SWLDLMLPFT IILSIIIAVI ISVYVPSSRH
TFDAEGHPNL MGVSIPLTVG MIVMMIPPIC KVSWESIHKY FYRSYIRKQL ALSLFLNWVI
GPLLMTALAW MALFDYKEYR QGIIMIGVAR CIAMVLIWNQ IAGGDNDLCV VLVITNSLLQ
MVLYAPLQIF YCYVISHDHL NTSNRVLFEE VAKSVGVFLG IPLGIGIIIR LGSLTIAGKS
NYEKYILRFI SPWAMIGFHY TLFVIFISRG YQFIHEIGSA ILCFVPLVLY FFIAWFLTFA
LMRYLSISRS DTQRECSCDQ ELLLKRVWGR KSCEASFSIT MTQCFTMASN NFELSLAIAI
SLYGNNSKQA IAATFGPLLE VPILLILAIV ARILKPYYIW NNRN
