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Boron transporter 1

 BOR1_YEAST              Reviewed;         576 AA.
P53838; D6W0R9;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-JUL-2017, entry version 121.
RecName: Full=Boron transporter 1;
Name=BOR1; OrderedLocusNames=YNL275W; ORFNames=N0626;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169873;
Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F.,
Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M.,
Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N.,
Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D.,
Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A.,
Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A.,
Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C.,
Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M.,
Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J.,
Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L.,
Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M.,
Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P.,
Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A.,
Wambutt R., Wedler H., Zollner A., Hani J.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV
and its evolutionary implications.";
Nature 387:93-98(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=11401825;
Zhao R., Reithmeier R.A.F.;
"Expression and characterization of the anion transporter homologue
YNL275w in Saccharomyces cerevisiae.";
Am. J. Physiol. 281:C33-C45(2001).
[4]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[5]
FUNCTION.
PubMed=16923078; DOI=10.1111/j.1574-6968.2006.00395.x;
Nozawa A., Takano J., Kobayashi M., von Wiren N., Fujiwara T.;
"Roles of BOR1, DUR3, and FPS1 in boron transport and tolerance in
Saccharomyces cerevisiae.";
FEMS Microbiol. Lett. 262:216-222(2006).
[6]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16565073; DOI=10.1074/jbc.M600911200;
Decker B.L., Wickner W.T.;
"Enolase activates homotypic vacuole fusion and protein transport to
the vacuole in yeast.";
J. Biol. Chem. 281:14523-14528(2006).
[7]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 208353 / W303-1A;
PubMed=16847258; DOI=10.1073/pnas.0604075103;
Kim H., Melen K., Oesterberg M., von Heijne G.;
"A global topology map of the Saccharomyces cerevisiae membrane
proteome.";
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
[8]
FUNCTION.
PubMed=17459946; DOI=10.1152/ajpcell.00286.2005;
Jennings M.L., Howren T.R., Cui J., Winters M., Hannigan R.;
"Transport and regulatory characteristics of the yeast bicarbonate
transporter homolog Bor1p.";
Am. J. Physiol. 293:C468-C476(2007).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17166224; DOI=10.1111/j.1574-6968.2006.00556.x;
Takano J., Kobayashi M., Noda Y., Fujiwara T.;
"Saccharomyces cerevisiae Bor1p is a boron exporter and a key
determinant of boron tolerance.";
FEMS Microbiol. Lett. 267:230-235(2007).
-!- FUNCTION: Functions in boric acid/borate export across the plasma
membrane, and thereby protects yeast cells from boron toxicity.
Involved in the trafficking of proteins to the vacuole.
{ECO:0000269|PubMed:11401825, ECO:0000269|PubMed:16565073,
ECO:0000269|PubMed:16923078, ECO:0000269|PubMed:17166224,
ECO:0000269|PubMed:17459946}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
Vacuole membrane; Multi-pass membrane protein.
-!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
{ECO:0000305}.
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EMBL; Z71551; CAA96183.1; -; Genomic_DNA.
EMBL; BK006947; DAA10285.1; -; Genomic_DNA.
PIR; S63249; S63249.
RefSeq; NP_014124.1; NM_001183113.1.
ProteinModelPortal; P53838; -.
BioGrid; 35565; 21.
DIP; DIP-8001N; -.
STRING; 4932.YNL275W; -.
TCDB; 2.A.31.3.2; the anion exchanger (ae) family.
iPTMnet; P53838; -.
MaxQB; P53838; -.
PRIDE; P53838; -.
EnsemblFungi; YNL275W; YNL275W; YNL275W.
GeneID; 855446; -.
KEGG; sce:YNL275W; -.
EuPathDB; FungiDB:YNL275W; -.
SGD; S000005219; BOR1.
GeneTree; ENSGT00760000119021; -.
HOGENOM; HOG000197283; -.
InParanoid; P53838; -.
OMA; HWILAIT; -.
OrthoDB; EOG092C2JUS; -.
BioCyc; YEAST:G3O-33269-MONOMER; -.
Reactome; R-SCE-1237044; Erythrocytes take up carbon dioxide and release oxygen.
Reactome; R-SCE-1247673; Erythrocytes take up oxygen and release carbon dioxide.
Reactome; R-SCE-425381; Bicarbonate transporters.
PRO; PR:P53838; -.
Proteomes; UP000002311; Chromosome XIV.
GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
GO; GO:0016021; C:integral component of membrane; ISM:SGD.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IDA:SGD.
GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
GO; GO:0080139; F:borate efflux transmembrane transporter activity; IDA:SGD.
GO; GO:0005452; F:inorganic anion exchanger activity; IEA:InterPro.
GO; GO:0046713; P:borate transport; IDA:SGD.
GO; GO:0006623; P:protein targeting to vacuole; IMP:SGD.
GO; GO:0051453; P:regulation of intracellular pH; IBA:GO_Central.
InterPro; IPR011531; HCO3_transpt_C.
InterPro; IPR003020; HCO3_transpt_euk.
PANTHER; PTHR11453; PTHR11453; 1.
Pfam; PF00955; HCO3_cotransp; 2.
1: Evidence at protein level;
Anion exchange; Cell membrane; Complete proteome; Ion transport;
Membrane; Reference proteome; Transmembrane; Transmembrane helix;
Transport; Vacuole.
CHAIN 1 576 Boron transporter 1.
/FTId=PRO_0000079243.
TOPO_DOM 1 84 Cytoplasmic. {ECO:0000255}.
TRANSMEM 85 105 Helical. {ECO:0000255}.
TOPO_DOM 106 116 Extracellular. {ECO:0000255}.
TRANSMEM 117 134 Helical. {ECO:0000255}.
TOPO_DOM 135 140 Cytoplasmic. {ECO:0000255}.
TRANSMEM 141 160 Helical. {ECO:0000255}.
TOPO_DOM 161 165 Extracellular. {ECO:0000255}.
TRANSMEM 166 186 Helical. {ECO:0000255}.
TOPO_DOM 187 192 Cytoplasmic. {ECO:0000255}.
TRANSMEM 193 213 Helical. {ECO:0000255}.
TOPO_DOM 214 235 Extracellular. {ECO:0000255}.
TRANSMEM 236 256 Helical. {ECO:0000255}.
TOPO_DOM 257 274 Cytoplasmic. {ECO:0000255}.
TRANSMEM 275 295 Helical. {ECO:0000255}.
TOPO_DOM 296 329 Extracellular. {ECO:0000255}.
TRANSMEM 330 350 Helical. {ECO:0000255}.
TOPO_DOM 351 373 Cytoplasmic. {ECO:0000255}.
TRANSMEM 374 394 Helical. {ECO:0000255}.
TOPO_DOM 395 438 Extracellular. {ECO:0000255}.
TRANSMEM 439 459 Helical. {ECO:0000255}.
TOPO_DOM 460 495 Cytoplasmic. {ECO:0000255}.
TRANSMEM 496 516 Helical. {ECO:0000255}.
TOPO_DOM 517 518 Extracellular. {ECO:0000255}.
TRANSMEM 519 539 Helical. {ECO:0000255}.
TOPO_DOM 540 576 Cytoplasmic. {ECO:0000255}.
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


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