ID   BOR1_YEAST              Reviewed;         576 AA.
AC   P53838; D6W0R9;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   04-NOV-2026, entry version 159.
DE   RecName: Full=Boron transporter 1;
GN   Name=BOR1; OrderedLocusNames=YNL275W; ORFNames=N0626;
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=9169873; DOI=10.1038/387s093;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(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   FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=11401825; DOI=10.1152/ajpcell.2001.281.1.c33;
RA   Zhao R., Reithmeier R.A.F.;
RT   "Expression and characterization of the anion transporter homologue YNL275w
RT   in Saccharomyces cerevisiae.";
RL   Am. J. Physiol. 281:C33-C45(2001).
RN   [4]
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   [5]
RP   FUNCTION.
RX   PubMed=16923078; DOI=10.1111/j.1574-6968.2006.00395.x;
RA   Nozawa A., Takano J., Kobayashi M., von Wiren N., Fujiwara T.;
RT   "Roles of BOR1, DUR3, and FPS1 in boron transport and tolerance in
RT   Saccharomyces cerevisiae.";
RL   FEMS Microbiol. Lett. 262:216-222(2006).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16565073; DOI=10.1074/jbc.m600911200;
RA   Decker B.L., Wickner W.T.;
RT   "Enolase activates homotypic vacuole fusion and protein transport to the
RT   vacuole in yeast.";
RL   J. Biol. Chem. 281:14523-14528(2006).
RN   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=17459946; DOI=10.1152/ajpcell.00286.2005;
RA   Jennings M.L., Howren T.R., Cui J., Winters M., Hannigan R.;
RT   "Transport and regulatory characteristics of the yeast bicarbonate
RT   transporter homolog Bor1p.";
RL   Am. J. Physiol. 293:C468-C476(2007).
RN   [9]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17166224; DOI=10.1111/j.1574-6968.2006.00556.x;
RA   Takano J., Kobayashi M., Noda Y., Fujiwara T.;
RT   "Saccharomyces cerevisiae Bor1p is a boron exporter and a key determinant
RT   of boron tolerance.";
RL   FEMS Microbiol. Lett. 267:230-235(2007).
CC   -!- FUNCTION: Functions in boric acid/borate export across the plasma
CC       membrane, and thereby protects yeast cells from boron toxicity.
CC       Involved in the trafficking of proteins to the vacuole.
CC       {ECO:0000269|PubMed:11401825, ECO:0000269|PubMed:16565073,
CC       ECO:0000269|PubMed:16923078, ECO:0000269|PubMed:17166224,
CC       ECO:0000269|PubMed:17459946}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC       Vacuole membrane; Multi-pass membrane protein.
CC   -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC       {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; Z71551; CAA96183.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10285.1; -; Genomic_DNA.
DR   PIR; S63249; S63249.
DR   RefSeq; NP_014124.1; NM_001183113.1.
DR   AlphaFoldDB; P53838; -.
DR   SMR; P53838; -.
DR   BioGRID; 35565; 29.
DR   DIP; DIP-8001N; -.
DR   FunCoup; P53838; 501.
DR   STRING; 4932.YNL275W; -.
DR   TCDB; 2.A.31.3.2; the anion exchanger (ae) family.
DR   iPTMnet; P53838; -.
DR   PaxDb; 4932-YNL275W; -.
DR   PeptideAtlas; P53838; -.
DR   DNASU; 855446; -.
DR   EnsemblFungi; YNL275W_mRNA; YNL275W; YNL275W.
DR   GeneID; 855446; -.
DR   KEGG; sce:YNL275W; -.
DR   AGR; SGD:S000005219; -.
DR   SGD; S000005219; BOR1.
DR   VEuPathDB; FungiDB:YNL275W; -.
DR   eggNOG; KOG1172; Eukaryota.
DR   HOGENOM; CLU_002289_7_2_1; -.
DR   InParanoid; P53838; -.
DR   OMA; AAFHWDT; -.
DR   OrthoDB; 1735926at2759; -.
DR   BioCyc; YEAST:G3O-33269-MONOMER; -.
DR   BioGRID-ORCS; 855446; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P53838; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P53838; protein.
DR   GO; GO:0071944; C:cell periphery; HDA:SGD.
DR   GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR   GO; GO:0016020; C:membrane; ISM:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0080139; F:borate efflux transmembrane transporter activity; IDA:SGD.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; IEA:InterPro.
DR   GO; GO:0046713; P:borate transport; IDA:SGD.
DR   GO; GO:0006820; P:monoatomic anion transport; IEA:InterPro.
DR   GO; GO:0050801; P:monoatomic ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   FunFam; 1.10.287.570:FF:000003; Anion exchange family protein; 1.
DR   Gene3D; 1.10.287.570; Helical hairpin bin; 1.
DR   InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR   InterPro; IPR003020; HCO3_transpt_euk.
DR   PANTHER; PTHR11453; ANION EXCHANGE PROTEIN; 1.
DR   PANTHER; PTHR11453:SF82; BORON TRANSPORTER 1; 1.
DR   Pfam; PF00955; HCO3_cotransp; 2.
PE   1: Evidence at protein level;
KW   Anion exchange; Cell membrane; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Vacuole.
FT   CHAIN           1..576
FT                   /note="Boron transporter 1"
FT                   /id="PRO_0000079243"
FT   TOPO_DOM        1..84
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..116
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        135..140
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        141..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161..165
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        187..192
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        214..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..274
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..329
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        330..350
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..373
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        395..438
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        439..459
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        460..495
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        517..518
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        519..539
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        540..576
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          19..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   576 AA;  65028 MW;  4EA3FFC89F66307A CRC64;
     MSNESTRVTV SRGCTASDEC AQALERTNDE LDRESSVSES RSDEESHEKL SRRRFPTLGI
     GIWLDLKDRI PYYKSDWVDA FNYRVIPSIV DTYFNNLLPA IAFAQDMFDR TDNSYGVNEV
     LLSSAMAGIV FGVLGGQPLC IVGVTGPISI FNYTVYEIIK PLNTSYFGFM FWICMWSMIF
     HLVLAFTNAV CLLQYVTTFP CDIFGLFINV VYIQKGIQIL TRQFSAKSGE KSVQDGFASV
     VVALVMTAFG LFFKLFHYYP LFSHRIRTFI SDYSTALSVL FWSSFTHFGG YLHDVKFKKL
     PITKAFFPTS KVNRPQNTWL AYEPIPVKDV FIALPFGIFL TILFYFDHNV SSLMAQRHQY
     KLKKPSSFHY DFALLGLTTC ISGVLGIPAP NGLIPQAPLH TETLLVRDSN QKVISCVEQR
     FTNTFQGLMI LGTMTRPLLV CLGEIPQAVL SGLFFIMGIN GLMTNSIIQR LVFLFSDPNR
     RDNTSPLMKV SKKSMLIFLS FSLTGFAGEF AITNTIAAIG FPLVLLLSVL VSFSFAYIFP
     TEELKILDTN VAQKFTIKNL LLENIRDAKF CDKHED
//