BSD2_YEAST
ID BSD2_YEAST Reviewed; 321 AA.
AC P38356; D6VQT5;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Metal homeostatis protein BSD2;
DE AltName: Full=Bypass SOD defects protein 2;
GN Name=BSD2; OrderedLocusNames=YBR290W; ORFNames=YBR2037;
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, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF PRO-149.
RX PubMed=7935419; DOI=10.1128/mcb.14.11.7037-7045.1994;
RA Liu X.F., Culotta V.C.;
RT "The requirement for yeast superoxide dismutase is bypassed through
RT mutations in BSD2, a novel metal homeostasis gene.";
RL Mol. Cell. Biol. 14:7037-7045(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091861; DOI=10.1002/yea.320100007;
RA Holmstroem K., Brandt T., Kallesoe T.;
RT "The sequence of a 32,420 bp segment located on the right arm of chromosome
RT II from Saccharomyces cerevisiae.";
RL Yeast 10:S47-S62(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=9115231; DOI=10.1074/jbc.272.18.11763;
RA Liu X.F., Supek F., Nelson N., Culotta V.C.;
RT "Negative control of heavy metal uptake by the Saccharomyces cerevisiae
RT BSD2 gene.";
RL J. Biol. Chem. 272:11763-11769(1997).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9988727; DOI=10.1074/jbc.274.8.4863;
RA Liu X.F., Culotta V.C.;
RT "Post-translation control of Nramp metal transport in yeast. Role of metal
RT ions and the BSD2 gene.";
RL J. Biol. Chem. 274:4863-4868(1999).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [10]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Required for homeostasis of heavy metal ions such as cadmium,
CC cobalt and copper. Controls metal ion transport and prevents metal
CC hyperaccumulation by negatively regulating the SMF1 and SMF2 metal
CC transport systems. Under manganese-replete conditions facilitates
CC trafficking of SMF1 and SMF2 metal transporters to the vacuole where
CC they are degraded. {ECO:0000269|PubMed:7935419,
CC ECO:0000269|PubMed:9115231, ECO:0000269|PubMed:9988727}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum. Vacuole. Membrane; Multi-
CC pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Increased accumulation of copper, cadmium and
CC cobalt ions and enhanced sensitivity to the toxic effects of copper and
CC cadmium. Exhibits no additional sensitivity to manganese. SMF1 fails to
CC enter the vacuole and is stabilized. Reverses the aerobic defects of
CC yeast strains lacking superoxide dismutase (SOD). Concomitant deletion
CC of SMF1 completely abolishes the ability of BSD2 deletion to suppress
CC SOD deficiency and reverses the increased sensitivity to cadmium and
CC copper. However cobalt ion hyperaccumulation is not suppressed.
CC {ECO:0000269|PubMed:7935419, ECO:0000269|PubMed:9115231,
CC ECO:0000269|PubMed:9988727}.
CC -!- MISCELLANEOUS: Present with 3070 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BSD2 family. {ECO:0000305}.
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DR EMBL; L33783; AAA65065.1; -; Genomic_DNA.
DR EMBL; X76053; CAA53653.1; -; Genomic_DNA.
DR EMBL; Z36159; CAA85255.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07405.1; -; Genomic_DNA.
DR PIR; S44552; S44552.
DR RefSeq; NP_009849.1; NM_001178638.1.
DR AlphaFoldDB; P38356; -.
DR SMR; P38356; -.
DR BioGRID; 32984; 211.
DR DIP; DIP-7753N; -.
DR IntAct; P38356; 39.
DR MINT; P38356; -.
DR STRING; 4932.YBR290W; -.
DR TCDB; 8.A.30.2.1; the nedd4-family interacting protein-2 (nedd4) family.
DR iPTMnet; P38356; -.
DR MaxQB; P38356; -.
DR PaxDb; P38356; -.
DR PRIDE; P38356; -.
DR EnsemblFungi; YBR290W_mRNA; YBR290W; YBR290W.
DR GeneID; 852593; -.
DR KEGG; sce:YBR290W; -.
DR SGD; S000000494; BSD2.
DR VEuPathDB; FungiDB:YBR290W; -.
DR eggNOG; KOG4812; Eukaryota.
DR GeneTree; ENSGT00390000012721; -.
DR HOGENOM; CLU_041193_2_0_1; -.
DR InParanoid; P38356; -.
DR OMA; YYNEICI; -.
DR BioCyc; YEAST:G3O-29209-MON; -.
DR PRO; PR:P38356; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38356; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IBA:GO_Central.
DR GO; GO:0030001; P:metal ion transport; IMP:SGD.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR InterPro; IPR019325; NEDD4/Bsd2.
DR PANTHER; PTHR13396; PTHR13396; 1.
DR Pfam; PF10176; DUF2370; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Isopeptide bond; Membrane; Reference proteome;
KW Stress response; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Vacuole.
FT CHAIN 1..321
FT /note="Metal homeostatis protein BSD2"
FT /id="PRO_0000064996"
FT TOPO_DOM 1..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..211
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 233..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 312
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 149
FT /note="P->S: Reverses the aerobic defects of yeast strains
FT lacking superoxide dismutase (SOD). Associated with
FT elevated copper ion accumulation and increased sensitivity
FT to the toxic effects of copper and cadmium. Exhibits no
FT additional sensitivity to manganese."
FT /evidence="ECO:0000269|PubMed:7935419"
SQ SEQUENCE 321 AA; 35764 MW; 1C212AED2A249850 CRC64;
MPEQELLIGQ EMNTLHAGSS TDGINVGNAG RTRDTQTGVE GETEIGSDEE DSIEDEGSSS
GGNSTTERLV PHQLREQAAR HIGKIGRHFN ILDRLFKKRT QQSSDIQQGA MFDGVFSNLS
AKPDTTETEG NNEQDIPPTY DEAAADMAPS YYGMDLNNSD IYYDEICIEG LPVGNIANLL
WNIIVSTSFQ FIGFLITYIL HTSHAAKQGS RFGLGLTFIG YGYSMIPNDV TSKVGKNKSL
NRMELEDPNE FDDVRLNSQS TTQDKFESHL NHGLDEEKQN IPWLAVFVAF LGLFITLKSI
YDYIQVKKLE KKYLNQSQNQ A
