ARR1_YEAST
ID ARR1_YEAST Reviewed; 294 AA.
AC Q06596; D6W4J7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Arsenical-resistance protein ARR1 {ECO:0000303|PubMed:11442837};
DE AltName: Full=AP-1-like transcription factor YAP8 {ECO:0000303|PubMed:9372930};
DE AltName: Full=Arsenic compound resistance protein 1 {ECO:0000303|PubMed:9234670};
GN Name=ARR1 {ECO:0000303|PubMed:11442837};
GN Synonyms=ACR1 {ECO:0000303|PubMed:9234670},
GN YAP8 {ECO:0000303|PubMed:9372930}; OrderedLocusNames=YPR199C;
GN ORFNames=P9677.15;
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], FUNCTION, AND DISRUPTION PHENOTYPE.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP IDENTIFICATION, AND DOMAIN.
RX PubMed=9372930; DOI=10.1128/mcb.17.12.6982;
RA Fernandes L., Rodrigues-Pousada C., Struhl K.;
RT "Yap, a novel family of eight bZIP proteins in Saccharomyces cerevisiae
RT with distinct biological functions.";
RL Mol. Cell. Biol. 17:6982-6993(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11527213; DOI=10.1139/o01-033;
RA Bouganim N., David J., Wysocki R., Ramotar D.;
RT "Yap1 overproduction restores arsenite resistance to the ABC transporter
RT deficient mutant ycf1 by activating ACR3 expression.";
RL Biochem. Cell Biol. 79:441-448(2001).
RN [7]
RP FUNCTION.
RX PubMed=11442837; DOI=10.1046/j.1365-2958.2001.02485.x;
RA Wysocki R., Chery C.C., Wawrzycka D., Van Hulle M., Cornelis R.,
RA Thevelein J.M., Tamas M.J.;
RT "The glycerol channel Fps1p mediates the uptake of arsenite and antimonite
RT in Saccharomyces cerevisiae.";
RL Mol. Microbiol. 40:1391-1401(2001).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF CYS-132; CYS-137 AND CYS-274.
RX PubMed=15147884; DOI=10.1016/j.febslet.2004.04.019;
RA Menezes R.A., Amaral C., Delaunay A., Toledano M., Rodrigues-Pousada C.;
RT "Yap8p activation in Saccharomyces cerevisiae under arsenic conditions.";
RL FEBS Lett. 566:141-146(2004).
RN [9]
RP FUNCTION, SUBUNIT, ACTIVITY REGULATION, AND MUTAGENESIS OF CYS-92; CYS-93;
RP CYS-121; CYS-132; CYS-137 AND CYS-274.
RX PubMed=17200139; DOI=10.1242/jcs.03346;
RA Di Y., Tamas M.J.;
RT "Regulation of the arsenic-responsive transcription factor Yap8p involves
RT the ubiquitin-proteasome pathway.";
RL J. Cell Sci. 120:256-264(2007).
RN [10]
RP FUNCTION, ARSENIC-BINDING, AND MUTAGENESIS OF CYS-132 AND CYS-274.
RX PubMed=26711267; DOI=10.1128/mcb.00842-15;
RA Kumar N.V., Yang J., Pillai J.K., Rawat S., Solano C., Kumar A.,
RA Groetli M., Stemmler T.L., Rosen B.P., Tamas M.J.;
RT "Arsenic directly binds to and activates the yeast AP-1-like transcription
RT factor Yap8.";
RL Mol. Cell. Biol. 36:913-922(2015).
RN [11]
RP PHOSPHORYLATION BY HOG1, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP FUNCTION, AND MUTAGENESIS OF SER-14; THR-16; THR-138; SER-141; SER-145;
RP SER-282 AND SER-292.
RX PubMed=31772124; DOI=10.1126/scisignal.aaw4956;
RA Guerra-Moreno A., Prado M.A., Ang J., Schnell H.M., Micoogullari Y.,
RA Paulo J.A., Finley D., Gygi S.P., Hanna J.;
RT "Thiol-based direct threat sensing by the stress-activated protein kinase
RT Hog1.";
RL Sci. Signal. 12:0-0(2019).
CC -!- FUNCTION: Transcription activator required for resistance to arsenic
CC compounds and for a regulated expression of ACR2, ACR3 and YCF1.
CC {ECO:0000269|PubMed:11442837, ECO:0000269|PubMed:11527213,
CC ECO:0000269|PubMed:15147884, ECO:0000269|PubMed:26711267,
CC ECO:0000269|PubMed:31772124, ECO:0000269|PubMed:9234670}.
CC -!- ACTIVITY REGULATION: Transcriptional activity is controled by regulated
CC degradation by the ubiquitin-proteasome pathway in absence of arsenic
CC (PubMed:17200139). Arsenic-exposure results in stabilization and
CC increased transcriptional activity (PubMed:15147884, PubMed:17200139).
CC {ECO:0000269|PubMed:15147884, ECO:0000269|PubMed:17200139}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17200139}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15147884}. Nucleus
CC {ECO:0000269|PubMed:15147884, ECO:0000269|PubMed:31772124}.
CC Note=Predominantly localized in the cytoplasm under non-stress
CC conditions and redistributed into the nucleus after HOG1
CC phosphorylation in the presence of arsenic (PubMed:15147884,
CC PubMed:31772124). The major karyopherinse CRM1 mediates nuclear export
CC which is also regulated by arsenic stress (PubMed:15147884).
CC {ECO:0000269|PubMed:15147884, ECO:0000269|PubMed:31772124}.
CC -!- PTM: Phosphorylation by HOG1 promotes nuclear localization in the
CC presence of arsenic. {ECO:0000269|PubMed:31772124}.
CC -!- DISRUPTION PHENOTYPE: Leads to hypersensitivity to arsenic
CC (PubMed:9234670). Impairs the arsenic-dependent induction of arsenate
CC reductase ARR2, arsenite transporter ARR3 and vacuolar transporter YCF1
CC (PubMed:11527213, PubMed:15147884). {ECO:0000269|PubMed:11527213,
CC ECO:0000269|PubMed:15147884, ECO:0000269|PubMed:9234670}.
CC -!- MISCELLANEOUS: One of 8 closely related fungi-specific YAP proteins
CC (YAP1 to YAP8), which all seem to be transcription activators of the
CC environmental stress response and metabolism control pathways and to
CC have similar but not identical DNA binding specificities.
CC {ECO:0000305|PubMed:11527213}.
CC -!- SIMILARITY: Belongs to the bZIP family. YAP subfamily. {ECO:0000305}.
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DR EMBL; U25841; AAB64627.1; -; Genomic_DNA.
DR EMBL; AY558064; AAS56390.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11613.1; -; Genomic_DNA.
DR PIR; S58828; S58828.
DR RefSeq; NP_015525.1; NM_001184296.1.
DR AlphaFoldDB; Q06596; -.
DR SMR; Q06596; -.
DR BioGRID; 36369; 74.
DR DIP; DIP-4388N; -.
DR STRING; 4932.YPR199C; -.
DR PaxDb; Q06596; -.
DR PRIDE; Q06596; -.
DR EnsemblFungi; YPR199C_mRNA; YPR199C; YPR199C.
DR GeneID; 856329; -.
DR KEGG; sce:YPR199C; -.
DR SGD; S000006403; ARR1.
DR VEuPathDB; FungiDB:YPR199C; -.
DR eggNOG; ENOG502SVNC; Eukaryota.
DR HOGENOM; CLU_947336_0_0_1; -.
DR InParanoid; Q06596; -.
DR OMA; YRERRIN; -.
DR BioCyc; YEAST:G3O-34319-MON; -.
DR PRO; PR:Q06596; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q06596; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central.
DR GO; GO:0061395; P:positive regulation of transcription from RNA polymerase II promoter in response to arsenic-containing substance; IMP:SGD.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR023167; Yap1_redox_dom_sf.
DR SUPFAM; SSF111430; SSF111430; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
PE 1: Evidence at protein level;
KW Activator; Arsenical resistance; Cytoplasm; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..294
FT /note="Arsenical-resistance protein ARR1"
FT /id="PRO_0000076528"
FT DOMAIN 22..72
FT /note="bZIP"
FT /evidence="ECO:0000305|PubMed:9372930"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 22..45
FT /note="Basic motif"
FT /evidence="ECO:0000305|PubMed:9372930"
FT REGION 44..72
FT /note="Leucine-zipper"
FT /evidence="ECO:0000305|PubMed:9372930"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26711267"
FT BINDING 137
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26711267"
FT BINDING 274
FT /ligand="arsenite"
FT /ligand_id="ChEBI:CHEBI:29242"
FT /note="covalent"
FT /evidence="ECO:0000269|PubMed:26711267"
FT MUTAGEN 14
FT /note="S->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-16, A-138, A-141, A-145, A-282 and A-
FT 292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 16
FT /note="T->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-138, A-141, A-145, A-282 and A-
FT 292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 92
FT /note="C->A: Retains about 60% of activity; when assocoated
FT with A-93."
FT /evidence="ECO:0000269|PubMed:17200139"
FT MUTAGEN 93
FT /note="C->A: Retains about 60% of activity; when assocoated
FT with A-92."
FT /evidence="ECO:0000269|PubMed:17200139"
FT MUTAGEN 121
FT /note="C->A: Retains about 60% of activity."
FT /evidence="ECO:0000269|PubMed:17200139"
FT MUTAGEN 132
FT /note="C->A: Impairs nuclear relocalization in response to
FT arsenic and transcriptional activity, and leads to arsenic
FT hypersensitivity. Loses most of the arsenic-binding
FT capacity; when assciated with A-274."
FT /evidence="ECO:0000269|PubMed:15147884,
FT ECO:0000269|PubMed:17200139, ECO:0000269|PubMed:26711267"
FT MUTAGEN 137
FT /note="C->A: Impairs nuclear relocalization in response to
FT arsenic and transcriptional activity, and leads to arsenic
FT hypersensitivity."
FT /evidence="ECO:0000269|PubMed:15147884,
FT ECO:0000269|PubMed:17200139"
FT MUTAGEN 138
FT /note="T->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-16, A-141, A-145, A-282 and A-292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 141
FT /note="S->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-16, A-138, A-145, A-282 and A-292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 145
FT /note="S->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-16, A-138, A-141, A-282 and A-292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 274
FT /note="C->A: Impairs nuclear relocalization in response to
FT arsenic and transcriptional activity, and leads to arsenic
FT hypersensitivity. Loses most of the arsenic-binding
FT capacity; when assciated with A-274."
FT /evidence="ECO:0000269|PubMed:15147884,
FT ECO:0000269|PubMed:17200139, ECO:0000269|PubMed:26711267"
FT MUTAGEN 282
FT /note="S->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-16, A-138, A-141, A-145 and A-292."
FT /evidence="ECO:0000269|PubMed:31772124"
FT MUTAGEN 292
FT /note="S->A: Impairs largely arsenic-induced
FT phosphorylation, shows strong sensitivity to arsenic
FT treatment and a strong, although not complete, reduction in
FT arsenite-induced expression of ARR2 and ARR3; when
FT associated with A-14, A-16, A-138, A-141, A-145 and A-282."
FT /evidence="ECO:0000269|PubMed:31772124"
SQ SEQUENCE 294 AA; 33227 MW; BDED49B5C0BF8CD3 CRC64;
MAKPRGRKGG RKPSLTPPKN KRAAQLRASQ NAFRKRKLER LEELEKKEAQ LTVTNDQIHI
LKKENELLHF MLRSLLTERN MPSDERNISK ACCEEKPPTC NTLDGSVVLS STYNSLEIQQ
CYVFFKQLLS VCVGKNCTVP SPLNSFDRSF YPIGCTNLSN DIPGYSFLND AMSEIHTFGD
FNGELDSTFL EFSGTEIKEP NNFITENTNA IETAAASMVI RQGFHPRQYY TVDAFGGDVL
LSAMDIWSFM KVHPKVNTFD LEILGTELKK SATCSNFDIL ISLKHFIKVF SSKL
