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Protein

Arsenical-resistance protein 3

Gene

ARR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.8 Publications

Kineticsi

Vmax for arsenite is approximately 3 times higher than for antimonite.1 Publication

  1. KM=2 mM for arsenite export1 Publication
  2. KM=2 mM for antimonite export1 Publication

    GO - Molecular functioni

    • antimonite transmembrane transporter activity Source: SGD
    • antiporter activity Source: SGD
    • arsenite transmembrane transporter activity Source: SGD
    • organic acid transmembrane transporter activity Source: GO_Central

    GO - Biological processi

    • antimonite transport Source: SGD
    • arsenite transport Source: SGD
    • response to arsenic-containing substance Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Biological processi

    Antiport, Arsenical resistance, Ion transport, Transport

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34321-MONOMER.

    Protein family/group databases

    TCDBi2.A.59.1.1. the arsenical resistance-3 (acr3) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Arsenical-resistance protein 3Curated
    Alternative name(s):
    Arsenic compounds resistance protein 31 Publication
    As(III)/H(+) and Sb(III)/H(+)antiporterCurated
    Gene namesi
    Name:ARR3Imported
    Synonyms:ACR31 Publication
    Ordered Locus Names:YPR201WImported
    ORF Names:P9677.2
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    Proteomesi
    • UP000002311 Componenti: Chromosome XVI

    Organism-specific databases

    EuPathDBiFungiDB:YPR201W.
    SGDiS000006405. ARR3.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3434Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei35 – 5521HelicalSequence analysisAdd
    BLAST
    Topological domaini56 – 6914Extracellular1 PublicationAdd
    BLAST
    Transmembranei70 – 9021HelicalSequence analysisAdd
    BLAST
    Topological domaini91 – 11323Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei114 – 13421HelicalSequence analysisAdd
    BLAST
    Topological domaini135 – 1417Extracellular1 Publication
    Transmembranei142 – 16221HelicalSequence analysisAdd
    BLAST
    Topological domaini163 – 1697Cytoplasmic1 Publication
    Transmembranei170 – 19021HelicalSequence analysisAdd
    BLAST
    Topological domaini191 – 21626Extracellular1 PublicationAdd
    BLAST
    Transmembranei217 – 23721HelicalSequence analysisAdd
    BLAST
    Topological domaini238 – 2458Cytoplasmic1 Publication
    Transmembranei246 – 26621HelicalSequence analysisAdd
    BLAST
    Topological domaini267 – 28014Extracellular1 PublicationAdd
    BLAST
    Transmembranei281 – 30121HelicalSequence analysisAdd
    BLAST
    Topological domaini302 – 34342Cytoplasmic1 PublicationAdd
    BLAST
    Transmembranei344 – 36421HelicalSequence analysisAdd
    BLAST
    Topological domaini365 – 3695Extracellular1 Publication
    Transmembranei370 – 39021HelicalSequence analysisAdd
    BLAST
    Topological domaini391 – 40414Cytoplasmic1 PublicationAdd
    BLAST

    GO - Cellular componenti

    • integral component of plasma membrane Source: GO_Central
    • plasma membrane Source: SGD
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Biotechnological usei

    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).2 Publications

    Disruption phenotypei

    Leads to sensitivity to antimony, tellurite, cadmium, and phenylarsine oxide.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901C → A: Leads to ER retention and arsenite sensitivity. 1 Publication
    Mutagenesisi117 – 1171N → A: Impairs cell membrane localization, and leads to arsenite sensitivity. 1 Publication
    Mutagenesisi150 – 1501R → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi151 – 1511C → V: Leads to complete loss of metalloid transport function. 1 Publication
    Mutagenesisi158 – 1581W → A: Impairs cell membrane localization, and leads to arsenite sensitivity. 1 Publication
    Mutagenesisi169 – 1691C → A: Greatly reduces arsenite efflux. 1 Publication
    Mutagenesisi176 – 1761N → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi192 – 1921C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication
    Mutagenesisi230 – 2301R → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi266 – 2661F → A: Impairs arsenite resistance. 1 Publication
    Mutagenesisi283 – 2831C → A: Does not alter the arsenite/proton exchange across the plasma membrane. 1 Publication
    Mutagenesisi290 – 2901Y → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi316 – 3161C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication
    Mutagenesisi318 – 3181C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication
    Mutagenesisi333 – 3331C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication
    Mutagenesisi344 – 3441C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication
    Mutagenesisi345 – 3451F → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi349 – 3491S → A: Impairs arsenite resistance. 1 Publication
    Mutagenesisi351 – 3511N → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication
    Mutagenesisi352 – 3521F → A: Impairs arsenite resistance. 1 Publication
    Mutagenesisi353 – 3531E → A: Impairs arsenite resistance. 1 Publication
    Mutagenesisi380 – 3801E → A: Impairs arsenite resistance. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 404404Arsenical-resistance protein 3PRO_0000064440Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi201 – 2011N-linked (GlcNAc...)PROSITE-ProRule annotation
    Glycosylationi365 – 3651N-linked (GlcNAc...)PROSITE-ProRule annotation

    Keywords - PTMi

    Glycoprotein

    Expressioni

    Inductioni

    Expression is highly induced by arsenite and antimonite.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi36371. 21 interactions.
    DIPiDIP-3797N.
    IntActiQ06598. 3 interactions.
    MINTiMINT-560243.

    Structurei

    3D structure databases

    ProteinModelPortaliQ06598.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    InParanoidiQ06598.
    KOiK03325.
    OMAiTAFWFPR.
    OrthoDBiEOG7T1RN9.

    Family and domain databases

    InterProiIPR004706. Arsenical-R_Acr3.
    IPR002657. BilAc:Na_symport/Acr3.
    [Graphical view]
    PANTHERiPTHR10361. PTHR10361. 2 hits.
    PTHR10361:SF31. PTHR10361:SF31. 2 hits.
    PfamiPF01758. SBF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005508. Acr3. 1 hit.
    TIGRFAMsiTIGR00832. acr3. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q06598-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSEDQKSENS VPSKVNMVNR TDILTTIKSL SWLDLMLPFT IILSIIIAVI
    60 70 80 90 100
    ISVYVPSSRH TFDAEGHPNL MGVSIPLTVG MIVMMIPPIC KVSWESIHKY
    110 120 130 140 150
    FYRSYIRKQL ALSLFLNWVI GPLLMTALAW MALFDYKEYR QGIIMIGVAR
    160 170 180 190 200
    CIAMVLIWNQ IAGGDNDLCV VLVITNSLLQ MVLYAPLQIF YCYVISHDHL
    210 220 230 240 250
    NTSNRVLFEE VAKSVGVFLG IPLGIGIIIR LGSLTIAGKS NYEKYILRFI
    260 270 280 290 300
    SPWAMIGFHY TLFVIFISRG YQFIHEIGSA ILCFVPLVLY FFIAWFLTFA
    310 320 330 340 350
    LMRYLSISRS DTQRECSCDQ ELLLKRVWGR KSCEASFSIT MTQCFTMASN
    360 370 380 390 400
    NFELSLAIAI SLYGNNSKQA IAATFGPLLE VPILLILAIV ARILKPYYIW

    NNRN
    Length:404
    Mass (Da):45,848
    Last modified:November 1, 1996 - v1
    Checksum:i1BE290E26772B4CA
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U25841 Genomic DNA. Translation: AAB64629.1.
    BK006949 Genomic DNA. Translation: DAA11615.1.
    PIRiS58830.
    RefSeqiNP_015527.1. NM_001184298.1.

    Genome annotation databases

    EnsemblFungiiYPR201W; YPR201W; YPR201W.
    GeneIDi856331.
    KEGGisce:YPR201W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U25841 Genomic DNA. Translation: AAB64629.1.
    BK006949 Genomic DNA. Translation: DAA11615.1.
    PIRiS58830.
    RefSeqiNP_015527.1. NM_001184298.1.

    3D structure databases

    ProteinModelPortaliQ06598.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi36371. 21 interactions.
    DIPiDIP-3797N.
    IntActiQ06598. 3 interactions.
    MINTiMINT-560243.

    Protein family/group databases

    TCDBi2.A.59.1.1. the arsenical resistance-3 (acr3) family.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYPR201W; YPR201W; YPR201W.
    GeneIDi856331.
    KEGGisce:YPR201W.

    Organism-specific databases

    EuPathDBiFungiDB:YPR201W.
    SGDiS000006405. ARR3.

    Phylogenomic databases

    InParanoidiQ06598.
    KOiK03325.
    OMAiTAFWFPR.
    OrthoDBiEOG7T1RN9.

    Enzyme and pathway databases

    BioCyciYEAST:G3O-34321-MONOMER.

    Miscellaneous databases

    PROiQ06598.

    Family and domain databases

    InterProiIPR004706. Arsenical-R_Acr3.
    IPR002657. BilAc:Na_symport/Acr3.
    [Graphical view]
    PANTHERiPTHR10361. PTHR10361. 2 hits.
    PTHR10361:SF31. PTHR10361:SF31. 2 hits.
    PfamiPF01758. SBF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005508. Acr3. 1 hit.
    TIGRFAMsiTIGR00832. acr3. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Isolation of three contiguous genes, ACR1, ACR2 and ACR3, involved in resistance to arsenic compounds in the yeast Saccharomyces cerevisiae."
      Bobrowicz P., Wysocki R., Owsianik G., Goffeau A., Ulaszewski S.
      Yeast 13:819-828(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
      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.
      Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "The Saccharomyces cerevisiae ACR3 gene encodes a putative membrane protein involved in arsenite transport."
      Wysocki R., Bobrowicz P., Ulaszewski S.
      J. Biol. Chem. 272:30061-30066(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY.
    5. "The yeast permease Acr3p is a dual arsenite and antimonite plasma membrane transporter."
      Maciaszczyk-Dziubinska E., Wawrzycka D., Sloma E., Migocka M., Wysocki R.
      Biochim. Biophys. Acta 1798:2170-2175(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, FUNCTION, SUBCELLULAR LOCATION.
    6. "Acr3p is a plasma membrane antiporter that catalyzes As(III)/H(+) and Sb(III)/H(+) exchange in Saccharomyces cerevisiae."
      Maciaszczyk-Dziubinska E., Migocka M., Wysocki R.
      Biochim. Biophys. Acta 1808:1855-1859(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    7. "Heterologous expression of the yeast arsenite efflux system ACR3 improves Arabidopsis thaliana tolerance to arsenic stress."
      Ali W., Isner J.C., Isayenkov S.V., Liu W., Zhao F.J., Maathuis F.J.
      New Phytol. 194:716-723(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOTECHNOLOGY.
    8. "Expressing ScACR3 in rice enhanced arsenite efflux and reduced arsenic accumulation in rice grains."
      Duan G., Kamiya T., Ishikawa S., Arao T., Fujiwara T.
      Plant Cell Physiol. 53:154-163(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOTECHNOLOGY.
    9. "Multiple cysteine residues are necessary for sorting and transport activity of the arsenite permease Acr3p from Saccharomyces cerevisiae."
      Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D., Markowska K., Wysocki R.
      Biochim. Biophys. Acta 1838:747-755(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF CYS-90; CYS-151; CYS-169; CYS-192; CYS-283; CYS-316; CYS-318; CYS-333 AND CYS-344, SUBCELLULAR LOCATION, FUNCTION.
    10. "Identification of critical residues for transport activity of Acr3p, the Saccharomyces cerevisiae As(III)/H(+) antiporter."
      Markowska K., Maciaszczyk-Dziubinska E., Migocka M., Wawrzycka D., Wysocki R.
      Mol. Microbiol. 98:162-174(2015) [PubMed] [Europe PMC] [Abstract]
      Cited for: 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, FUNCTION.

    Entry informationi

    Entry nameiARR3_YEAST
    AccessioniPrimary (citable) accession number: Q06598
    Secondary accession number(s): D6W4J9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: July 6, 2016
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XVI
      Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.