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ARR2_YEAST
ID   ARR2_YEAST              Reviewed;         130 AA.
AC   Q06597; D6W4J8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Arsenical-resistance protein 2;
GN   Name=ARR2; Synonyms=ACR2; OrderedLocusNames=YPR200C; ORFNames=P9677.16;
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   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).
CC   -!- FUNCTION: Involved in resistance to arsenic compounds.
CC       {ECO:0000269|PubMed:9234670}.
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DR   EMBL; U25841; AAB64628.1; -; Genomic_DNA.
DR   EMBL; AY558053; AAS56379.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11614.1; -; Genomic_DNA.
DR   PIR; S58829; S58829.
DR   RefSeq; NP_015526.1; NM_001184297.1.
DR   AlphaFoldDB; Q06597; -.
DR   SMR; Q06597; -.
DR   BioGRID; 36370; 26.
DR   IntAct; Q06597; 3.
DR   STRING; 4932.YPR200C; -.
DR   PaxDb; Q06597; -.
DR   PRIDE; Q06597; -.
DR   EnsemblFungi; YPR200C_mRNA; YPR200C; YPR200C.
DR   GeneID; 856330; -.
DR   KEGG; sce:YPR200C; -.
DR   SGD; S000006404; ARR2.
DR   VEuPathDB; FungiDB:YPR200C; -.
DR   eggNOG; KOG3772; Eukaryota.
DR   GeneTree; ENSGT00940000176483; -.
DR   HOGENOM; CLU_107716_1_1_1; -.
DR   InParanoid; Q06597; -.
DR   OMA; GHIKGAW; -.
DR   BioCyc; MetaCyc:G3O-34320-MON; -.
DR   BioCyc; YEAST:G3O-34320-MON; -.
DR   SABIO-RK; Q06597; -.
DR   PRO; PR:Q06597; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q06597; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0030611; F:arsenate reductase activity; IDA:SGD.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046685; P:response to arsenic-containing substance; TAS:SGD.
DR   Gene3D; 3.40.250.10; -; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR036873; Rhodanese-like_dom_sf.
DR   Pfam; PF00581; Rhodanese; 1.
DR   SMART; SM00450; RHOD; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
PE   4: Predicted;
KW   Arsenical resistance; Reference proteome.
FT   CHAIN           1..130
FT                   /note="Arsenical-resistance protein 2"
FT                   /id="PRO_0000064439"
FT   DOMAIN          17..124
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
SQ   SEQUENCE   130 AA;  14883 MW;  3B32697BD503330F CRC64;
     MVSFITSRQL KGLIENQRKD FQVVDLRRED FARDHITNAW HVPVTAQITE KQLNQLIKGL
     SDTFSSSQFV KVIFHCTGSK NRGPKVAAKF ETYLQEEDIT SKFESCILVG GFYAWETHCR
     ESNLKLIVSG
 
 
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