位置:首页 > 蛋白库 > ARR3_YEAST
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024