BOR1_YEAST
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 03-AUG-2022, entry version 144.
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;
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}.
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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; 28.
DR DIP; DIP-8001N; -.
DR STRING; 4932.YNL275W; -.
DR TCDB; 2.A.31.3.2; the anion exchanger (ae) family.
DR iPTMnet; P53838; -.
DR MaxQB; P53838; -.
DR PaxDb; P53838; -.
DR PRIDE; P53838; -.
DR DNASU; 855446; -.
DR EnsemblFungi; YNL275W_mRNA; YNL275W; YNL275W.
DR GeneID; 855446; -.
DR KEGG; sce:YNL275W; -.
DR SGD; S000005219; BOR1.
DR VEuPathDB; FungiDB:YNL275W; -.
DR eggNOG; KOG1172; Eukaryota.
DR HOGENOM; CLU_002289_7_2_1; -.
DR InParanoid; P53838; -.
DR OMA; AWDYRVI; -.
DR BioCyc; YEAST:G3O-33269-MON; -.
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:0016021; C:integral component of 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:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0080139; F:borate efflux transmembrane transporter activity; IDA:SGD.
DR GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046713; P:borate transport; IDA:SGD.
DR GO; GO:0050801; P: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 InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR PANTHER; PTHR11453; PTHR11453; 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 23..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
