ID   BRP1_YEAST              Reviewed;         125 AA.
AC   P53194; A0A1S0T082;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Uncharacterized protein BRP1;
GN   Name=BRP1; OrderedLocusNames=YGL007W;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(1997).
RN   [2]
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   [3]
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   [4]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=15855155; DOI=10.1074/jbc.m503071200;
RA   Aouida M., Leduc A., Poulin R., Ramotar D.;
RT   "AGP2 encodes the major permease for high affinity polyamine import in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 280:24267-24276(2005).
RN   [5]
RP   REVISION OF FUNCTION.
RX   PubMed=16374585; DOI=10.1007/s00018-005-5341-7;
RA   Porat Z., Wender N., Erez O., Kahana C.;
RT   "Mechanism of polyamine tolerance in yeast: novel regulators and
RT   insights.";
RL   Cell. Mol. Life Sci. 62:3106-3116(2005).
CC   -!- DISRUPTION PHENOTYPE: Causes resistance to toxic polyamine
CC       concentrations (PubMed:15855155). Present in the 5'-UTR of plasma
CC       membrane ATPase 1 (PMA1), the ORF spans two upstream activating
CC       sequences (UAS) that are important for the expression of PMA1, and the
CC       deletion phenoytpe is attributed to down-regulation of PMA1
CC       (PubMed:16374585). {ECO:0000269|PubMed:15855155,
CC       ECO:0000305|PubMed:16374585}.
CC   -!- CAUTION: Was originally (PubMed:15855155) thought to function in
CC       polyamine resistance, hence the name BRP1, but this phenotype was later
CC       (PubMed:16374585) attributed to down-regulation of PMA1.
CC       {ECO:0000305|PubMed:15855155, ECO:0000305|PubMed:16374585}.
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DR   EMBL; Z72529; CAA96707.1; -; Genomic_DNA.
DR   EMBL; AY693239; AAT93258.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA80299.1; -; Genomic_DNA.
DR   PIR; S64009; S64009.
DR   AlphaFoldDB; P53194; -.
DR   STRING; 4932.YGL007W; -.
DR   PaxDb; P53194; -.
DR   PRIDE; P53194; -.
DR   EnsemblFungi; YGL007W_mRNA; YGL007W; YGL007W.
DR   SGD; S000002975; BRP1.
DR   HOGENOM; CLU_2147307_0_0_1; -.
DR   PRO; PR:P53194; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53194; protein.
PE   4: Predicted;
KW   Reference proteome.
FT   CHAIN           1..125
FT                   /note="Uncharacterized protein BRP1"
FT                   /id="PRO_0000202777"
SQ   SEQUENCE   125 AA;  13790 MW;  66F6E7A5C6DE3247 CRC64;
     MMEKEGKKPE RHMDNILKMS IPVKSMSEVS RPGSAALGNT DAMRASLRNS RRSFSGHVRL
     VLRLVYGFIS AVIIAGSPLR DRVCFQITGK GQAKQSDVWV IPAMPVYVSP FQEACFVFSP
     SAMVT