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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: -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

    GO - Biological processi

    Keywordsi

    Biological processAntiport, 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

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Topology

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Topological domaini1 – 34Cytoplasmic1 PublicationAdd BLAST34
    Transmembranei35 – 55HelicalSequence analysisAdd BLAST21
    Topological domaini56 – 69Extracellular1 PublicationAdd BLAST14
    Transmembranei70 – 90HelicalSequence analysisAdd BLAST21
    Topological domaini91 – 113Cytoplasmic1 PublicationAdd BLAST23
    Transmembranei114 – 134HelicalSequence analysisAdd BLAST21
    Topological domaini135 – 141Extracellular1 Publication7
    Transmembranei142 – 162HelicalSequence analysisAdd BLAST21
    Topological domaini163 – 169Cytoplasmic1 Publication7
    Transmembranei170 – 190HelicalSequence analysisAdd BLAST21
    Topological domaini191 – 216Extracellular1 PublicationAdd BLAST26
    Transmembranei217 – 237HelicalSequence analysisAdd BLAST21
    Topological domaini238 – 245Cytoplasmic1 Publication8
    Transmembranei246 – 266HelicalSequence analysisAdd BLAST21
    Topological domaini267 – 280Extracellular1 PublicationAdd BLAST14
    Transmembranei281 – 301HelicalSequence analysisAdd BLAST21
    Topological domaini302 – 343Cytoplasmic1 PublicationAdd BLAST42
    Transmembranei344 – 364HelicalSequence analysisAdd BLAST21
    Topological domaini365 – 369Extracellular1 Publication5
    Transmembranei370 – 390HelicalSequence analysisAdd BLAST21
    Topological domaini391 – 404Cytoplasmic1 PublicationAdd BLAST14

    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)DescriptionActionsGraphical viewLength
    Mutagenesisi90C → A: Leads to ER retention and arsenite sensitivity. 1 Publication1
    Mutagenesisi117N → A: Impairs cell membrane localization, and leads to arsenite sensitivity. 1 Publication1
    Mutagenesisi150R → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi151C → V: Leads to complete loss of metalloid transport function. 1 Publication1
    Mutagenesisi158W → A: Impairs cell membrane localization, and leads to arsenite sensitivity. 1 Publication1
    Mutagenesisi169C → A: Greatly reduces arsenite efflux. 1 Publication1
    Mutagenesisi176N → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi192C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication1
    Mutagenesisi230R → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi266F → A: Impairs arsenite resistance. 1 Publication1
    Mutagenesisi283C → A: Does not alter the arsenite/proton exchange across the plasma membrane. 1 Publication1
    Mutagenesisi290Y → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi316C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication1
    Mutagenesisi318C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication1
    Mutagenesisi333C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication1
    Mutagenesisi344C → A: Results in moderate reduction of arsenite transport capacities and sorting perturbations. 1 Publication1
    Mutagenesisi345F → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi349S → A: Impairs arsenite resistance. 1 Publication1
    Mutagenesisi351N → A: Leads to ER retention, protein unstability and arsenite sensitivity. 1 Publication1
    Mutagenesisi352F → A: Impairs arsenite resistance. 1 Publication1
    Mutagenesisi353E → A: Impairs arsenite resistance. 1 Publication1
    Mutagenesisi380E → A: Impairs arsenite resistance. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000644401 – 404Arsenical-resistance protein 3Add BLAST404

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi201N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
    Glycosylationi365N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiQ06598

    Expressioni

    Inductioni

    Expression is highly induced by arsenite and antimonite.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi36371, 90 interactors
    DIPiDIP-3797N
    IntActiQ06598, 3 interactors
    MINTiQ06598
    STRINGi4932.YPR201W

    Structurei

    3D structure databases

    ProteinModelPortaliQ06598
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    InParanoidiQ06598
    KOiK03325
    OMAiCTAMVLM
    OrthoDBiEOG092C3QM8

    Family and domain databases

    InterProiView protein in InterPro
    IPR004706 Arsenical-R_Acr3
    IPR002657 BilAc:Na_symport/Acr3
    PANTHERiPTHR43057 PTHR43057, 1 hit
    PfamiView protein in Pfam
    PF01758 SBF, 1 hit
    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

    Similar proteinsi

    Entry informationi

    Entry nameiARR3_YEAST
    AccessioniPrimary (citable) accession number: Q06598
    Secondary accession number(s): D6W4J9
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: September 12, 2018
    This is version 145 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

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