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Arsenical-resistance protein 3 (Arsenic compounds resistance protein 3) (As(III)/H( ) and Sb(III)/H( )antiporter)

 ARR3_YEAST              Reviewed;         404 AA.
Q06598; D6W4J9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 139.
RecName: Full=Arsenical-resistance protein 3 {ECO:0000305};
AltName: Full=Arsenic compounds resistance protein 3 {ECO:0000303|PubMed:9234670};
AltName: Full=As(III)/H(+) and Sb(III)/H(+)antiporter {ECO:0000305};
Name=ARR3 {ECO:0000312|SGD:S000006405};
Synonyms=ACR3 {ECO:0000303|PubMed:9234670};
OrderedLocusNames=YPR201W {ECO:0000312|SGD:S000006405};
ORFNames=P9677.2;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=9234670;
DOI=10.1002/(SICI)1097-0061(199707)13:9<819::AID-YEA142>3.0.CO;2-Y;
Bobrowicz P., Wysocki R., Owsianik G., Goffeau A., Ulaszewski S.;
"Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in
resistance to arsenic compounds in the yeast Saccharomyces
cerevisiae.";
Yeast 13:819-828(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169875;
Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V.,
Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M.,
Chung E., Churcher C.M., Coster F., Davis K., Davis R.W.,
Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A.,
Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A.,
Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W.,
Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K.,
Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J.,
Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D.,
Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V.,
Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W.,
Zollner A., Vo D.H., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
Nature 387:103-105(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=9374482; DOI=10.1074/jbc.272.48.30061;
Wysocki R., Bobrowicz P., Ulaszewski S.;
"The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane
protein involved in arsenite transport.";
J. Biol. Chem. 272:30061-30066(1997).
[5]
INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20655873; DOI=10.1016/j.bbamem.2010.07.017;
Maciaszczyk-Dziubinska E., Wawrzycka D., Sloma E., Migocka M.,
Wysocki R.;
"The yeast permease Acr3p is a dual arsenite and antimonite plasma
membrane transporter.";
Biochim. Biophys. Acta 1798:2170-2175(2010).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=21447319; DOI=10.1016/j.bbamem.2011.03.014;
Maciaszczyk-Dziubinska E., Migocka M., Wysocki R.;
"Acr3p is a plasma membrane antiporter that catalyzes As(III)/H(+) and
Sb(III)/H(+) exchange in Saccharomyces cerevisiae.";
Biochim. Biophys. Acta 1808:1855-1859(2011).
[7]
FUNCTION, AND BIOTECHNOLOGY.
PubMed=22380876; DOI=10.1111/j.1469-8137.2012.04092.x;
Ali W., Isner J.C., Isayenkov S.V., Liu W., Zhao F.J., Maathuis F.J.;
"Heterologous expression of the yeast arsenite efflux system ACR3
improves Arabidopsis thaliana tolerance to arsenic stress.";
New Phytol. 194:716-723(2012).
[8]
FUNCTION, AND BIOTECHNOLOGY.
PubMed=22107880; DOI=10.1093/pcp/pcr161;
Duan G., Kamiya T., Ishikawa S., Arao T., Fujiwara T.;
"Expressing ScACR3 in rice enhanced arsenite efflux and reduced
arsenic accumulation in rice grains.";
Plant Cell Physiol. 53:154-163(2012).
[9]
MUTAGENESIS OF CYS-90; CYS-151; CYS-169; CYS-192; CYS-283; CYS-316;
CYS-318; CYS-333 AND CYS-344, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=24291645; DOI=10.1016/j.bbamem.2013.11.013;
Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D., Markowska K.,
Wysocki R.;
"Multiple cysteine residues are necessary for sorting and transport
activity of the arsenite permease Acr3p from Saccharomyces
cerevisiae.";
Biochim. Biophys. Acta 1838:747-755(2014).
[10]
MUTAGENESIS OF ASN-117; ARG-150; TRP-158; ASN-176; ARG-230; PHE-266;
TYR-290; PHE-345; SER-349; ASN-351; PHE-352; GLU-353 AND GLU-380,
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=26123064; DOI=10.1111/mmi.13113;
Markowska K., Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D.,
Wysocki R.;
"Identification of critical residues for transport activity of Acr3p,
the Saccharomyces cerevisiae As(III)/H(+) antiporter.";
Mol. Microbiol. 98:162-174(2015).
-!- FUNCTION: Plasma membrane transporter that confers resistance to
toxic metalloids by mediating extrusion of arsenite (As(III)) and
antimonite (Sb(III)) out of cells. Displays low-affinity
As(III)/H(+) and Sb(III)/H(+) exchange activity.
{ECO:0000269|PubMed:20655873, ECO:0000269|PubMed:21447319,
ECO:0000269|PubMed:22107880, ECO:0000269|PubMed:22380876,
ECO:0000269|PubMed:24291645, ECO:0000269|PubMed:26123064,
ECO:0000269|PubMed:9234670, ECO:0000269|PubMed:9374482}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2 mM for arsenite export {ECO:0000269|PubMed:21447319};
KM=2 mM for antimonite export {ECO:0000269|PubMed:21447319};
Note=Vmax for arsenite is approximately 3 times higher than for
antimonite. {ECO:0000269|PubMed:21447319};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20655873,
ECO:0000269|PubMed:21447319, ECO:0000269|PubMed:24291645,
ECO:0000269|PubMed:26123064, ECO:0000305|PubMed:9374482}; Multi-
pass membrane protein {ECO:0000255, ECO:0000305|PubMed:9374482}.
-!- INDUCTION: Expression is highly induced by arsenite and
antimonite. {ECO:0000269|PubMed:20655873}.
-!- DISRUPTION PHENOTYPE: Leads to sensitivity to antimony, tellurite,
cadmium, and phenylarsine oxide. {ECO:0000269|PubMed:9374482}.
-!- BIOTECHNOLOGY: Heterologous expression endows plants with greater
arsenic resistance by enhancing arsenite efflux. Reduces arsenic
accumulation in rice grains (PubMed:22107880). Does not lower
significantly arsenic tissue levels in Arabidopsis
(PubMed:22380876). {ECO:0000269|PubMed:22107880,
ECO:0000269|PubMed:22380876}.
-!- SIMILARITY: Belongs to the arsenical resistance-3 (ACR3) (TC
2.A.59) family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U25841; AAB64629.1; -; Genomic_DNA.
EMBL; BK006949; DAA11615.1; -; Genomic_DNA.
PIR; S58830; S58830.
RefSeq; NP_015527.1; NM_001184298.1.
ProteinModelPortal; Q06598; -.
BioGrid; 36371; 90.
DIP; DIP-3797N; -.
IntAct; Q06598; 3.
MINT; MINT-560243; -.
STRING; 4932.YPR201W; -.
TCDB; 2.A.59.1.1; the arsenical resistance-3 (acr3) family.
EnsemblFungi; YPR201W; YPR201W; YPR201W.
GeneID; 856331; -.
KEGG; sce:YPR201W; -.
EuPathDB; FungiDB:YPR201W; -.
SGD; S000006405; ARR3.
InParanoid; Q06598; -.
KO; K03325; -.
OMA; CTAMVLM; -.
OrthoDB; EOG092C3QM8; -.
BioCyc; YEAST:G3O-34321-MONOMER; -.
PRO; PR:Q06598; -.
Proteomes; UP000002311; Chromosome XVI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0015104; F:antimonite transmembrane transporter activity; IMP:SGD.
GO; GO:0015297; F:antiporter activity; IMP:SGD.
GO; GO:0015105; F:arsenite transmembrane transporter activity; IDA:SGD.
GO; GO:0015699; P:antimonite transport; IMP:SGD.
GO; GO:0015700; P:arsenite transport; IMP:SGD.
GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW.
InterPro; IPR004706; Arsenical-R_Acr3.
InterPro; IPR002657; BilAc:Na_symport/Acr3.
PANTHER; PTHR43057; PTHR43057; 1.
Pfam; PF01758; SBF; 1.
PIRSF; PIRSF005508; Acr3; 1.
TIGRFAMs; TIGR00832; acr3; 1.
1: Evidence at protein level;
Antiport; Arsenical resistance; Cell membrane; Complete proteome;
Glycoprotein; Ion transport; Membrane; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 404 Arsenical-resistance protein 3.
/FTId=PRO_0000064440.
TOPO_DOM 1 34 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 35 55 Helical. {ECO:0000255}.
TOPO_DOM 56 69 Extracellular.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 70 90 Helical. {ECO:0000255}.
TOPO_DOM 91 113 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 114 134 Helical. {ECO:0000255}.
TOPO_DOM 135 141 Extracellular.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 142 162 Helical. {ECO:0000255}.
TOPO_DOM 163 169 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 170 190 Helical. {ECO:0000255}.
TOPO_DOM 191 216 Extracellular.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 217 237 Helical. {ECO:0000255}.
TOPO_DOM 238 245 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 246 266 Helical. {ECO:0000255}.
TOPO_DOM 267 280 Extracellular.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 281 301 Helical. {ECO:0000255}.
TOPO_DOM 302 343 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 344 364 Helical. {ECO:0000255}.
TOPO_DOM 365 369 Extracellular.
{ECO:0000305|PubMed:9374482}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 404 Cytoplasmic.
{ECO:0000305|PubMed:9374482}.
CARBOHYD 201 201 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
MUTAGEN 90 90 C->A: Leads to ER retention and arsenite
sensitivity.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 117 117 N->A: Impairs cell membrane localization,
and leads to arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 150 150 R->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 151 151 C->V: Leads to complete loss of metalloid
transport function.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 158 158 W->A: Impairs cell membrane localization,
and leads to arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 169 169 C->A: Greatly reduces arsenite efflux.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 176 176 N->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 192 192 C->A: Results in moderate reduction of
arsenite transport capacities and sorting
perturbations.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 230 230 R->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 266 266 F->A: Impairs arsenite resistance.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 283 283 C->A: Does not alter the arsenite/proton
exchange across the plasma membrane.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 290 290 Y->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 316 316 C->A: Results in moderate reduction of
arsenite transport capacities and sorting
perturbations.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 318 318 C->A: Results in moderate reduction of
arsenite transport capacities and sorting
perturbations.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 333 333 C->A: Results in moderate reduction of
arsenite transport capacities and sorting
perturbations.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 344 344 C->A: Results in moderate reduction of
arsenite transport capacities and sorting
perturbations.
{ECO:0000269|PubMed:24291645}.
MUTAGEN 345 345 F->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 349 349 S->A: Impairs arsenite resistance.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 351 351 N->A: Leads to ER retention, protein
unstability and arsenite sensitivity.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 352 352 F->A: Impairs arsenite resistance.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 353 353 E->A: Impairs arsenite resistance.
{ECO:0000269|PubMed:26123064}.
MUTAGEN 380 380 E->A: Impairs arsenite resistance.
{ECO:0000269|PubMed:26123064}.
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


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