BTN1_YEAST
ID BTN1_YEAST Reviewed; 408 AA.
AC P47040; D6VWC3; O60004; Q6B1E1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein BTN1;
DE Flags: Precursor;
GN Name=YHC3; Synonyms=BTN1; OrderedLocusNames=YJL059W; ORFNames=J1139;
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], SUBCELLULAR LOCATION, AND VARIANTS
RP PHE-181 AND ARG-328.
RC STRAIN=K289-3A;
RX PubMed=9753630; DOI=10.1006/bbrc.1998.9272;
RA Croopnick J.B., Choi H.C., Mueller D.M.;
RT "The subcellular location of the yeast Saccharomyces homologue of the
RT protein defective in the juvenile form of Batten disease.";
RL Biochem. Biophys. Res. Commun. 250:335-341(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=9219333;
RX DOI=10.1002/(sici)1097-0061(19970630)13:8<691::aid-yea123>3.0.co;2-d;
RA Pearce D.A., Sherman F.;
RT "BTN1, a yeast gene corresponding to the human gene responsible for
RT Batten's disease, is not essential for viability, mitochondrial function,
RT or degradation of mitochondrial ATP synthase.";
RL Yeast 13:691-697(1997).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10319861; DOI=10.1038/8861;
RA Pearce D.A., Ferea T., Nosel S.A., Das B., Sherman F.;
RT "Action of BTN1, the yeast orthologue of the gene mutated in Batten
RT disease.";
RL Nat. Genet. 22:55-58(1999).
RN [7]
RP FUNCTION.
RX PubMed=11053386; DOI=10.1128/jb.182.22.6418-6423.2000;
RA Chattopadhyay S., Muzaffar N.E., Sherman F., Pearce D.A.;
RT "The yeast model for Batten disease: mutations in BTN1, BTN2, and HSP30
RT alter pH homeostasis.";
RL J. Bacteriol. 182:6418-6423(2000).
RN [8]
RP FUNCTION.
RX PubMed=14660799; DOI=10.1073/pnas.2136651100;
RA Kim Y., Ramirez-Montealegre D., Pearce D.A.;
RT "A role in vacuolar arginine transport for yeast Btn1p and for human CLN3,
RT the protein defective in Batten disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:15458-15462(2003).
RN [9]
RP FUNCTION.
RX PubMed=15701790; DOI=10.1128/ec.4.2.281-288.2005;
RA Kim Y., Chattopadhyay S., Locke S., Pearce D.A.;
RT "Interaction among Btn1p, Btn2p, and Ist2p reveals potential interplay
RT among the vacuole, amino acid levels, and ion homeostasis in the yeast
RT Saccharomyces cerevisiae.";
RL Eukaryot. Cell 4:281-288(2005).
CC -!- FUNCTION: Plays a role in vacuolar arginine transport. Involved in pH
CC homeostasis. May be involved in ion homeostasis together with IST2. Not
CC necessary for mitochondrial function or ATP synthase degradation.
CC {ECO:0000269|PubMed:10319861, ECO:0000269|PubMed:11053386,
CC ECO:0000269|PubMed:14660799, ECO:0000269|PubMed:15701790,
CC ECO:0000269|PubMed:9219333}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:10319861,
CC ECO:0000269|PubMed:9753630}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10319861, ECO:0000269|PubMed:9753630}.
CC -!- SIMILARITY: Belongs to the battenin family. {ECO:0000305}.
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DR EMBL; AF058447; AAC61258.1; -; Genomic_DNA.
DR EMBL; Z49334; CAA89350.1; -; Genomic_DNA.
DR EMBL; AY693139; AAT93158.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08739.1; -; Genomic_DNA.
DR PIR; S56831; S56831.
DR RefSeq; NP_012476.1; NM_001181492.1.
DR AlphaFoldDB; P47040; -.
DR SMR; P47040; -.
DR BioGRID; 33695; 60.
DR DIP; DIP-4761N; -.
DR IntAct; P47040; 1.
DR MINT; P47040; -.
DR STRING; 4932.YJL059W; -.
DR TCDB; 2.A.57.5.2; the equilibrative nucleoside transporter (ent) family.
DR PaxDb; P47040; -.
DR PRIDE; P47040; -.
DR EnsemblFungi; YJL059W_mRNA; YJL059W; YJL059W.
DR GeneID; 853387; -.
DR KEGG; sce:YJL059W; -.
DR SGD; S000003595; YHC3.
DR VEuPathDB; FungiDB:YJL059W; -.
DR eggNOG; KOG3880; Eukaryota.
DR GeneTree; ENSGT00390000003249; -.
DR HOGENOM; CLU_029663_1_2_1; -.
DR InParanoid; P47040; -.
DR OMA; WLCNWQV; -.
DR BioCyc; YEAST:G3O-31522-MON; -.
DR PRO; PR:P47040; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47040; protein.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IBA:GO_Central.
DR GO; GO:1903826; P:L-arginine transmembrane transport; IMP:SGD.
DR GO; GO:0015819; P:lysine transport; IMP:SGD.
DR GO; GO:0051453; P:regulation of intracellular pH; IMP:SGD.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR003492; Battenin_disease_Cln3.
DR InterPro; IPR018460; Battenin_disease_Cln3_subgr.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR10981; PTHR10981; 1.
DR Pfam; PF02487; CLN3; 1.
DR PIRSF; PIRSF015974; CLN3_BTN1; 1.
DR PRINTS; PR01315; BATTENIN.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 3: Inferred from homology;
KW Amino-acid transport; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix; Transport; Vacuole.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..408
FT /note="Protein BTN1"
FT /id="PRO_0000020836"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 323..343
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 181
FT /note="Y -> F (in strain: K289-3A)"
FT /evidence="ECO:0000269|PubMed:9753630"
FT VARIANT 328
FT /note="H -> R (in strain: K289-3A)"
FT /evidence="ECO:0000269|PubMed:9753630"
FT CONFLICT 162
FT /note="L -> P (in Ref. 4; AAT93158)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 408 AA; 46383 MW; BAB6891F676E80EE CRC64;
MSDKSHQIYC YFWLFGLINN VLYVVILSAA VDIVGPTLPK SLVLLADIFP SLAIKLCSPF
FIDRIKYSYR IWSLITMSCL GMFLVSFKNL FVCLLGISFA SISSGFGEVT FLQLTHYYKQ
ISLNGWSSGT GGAGIIGGAS YMFLTSIFKV PVKLTLLVFS LLPFAFLFYF KLESNDTNLT
YQSLQQIDEA EDDQLVPFPV AFTHTNASQS LYSTRQHILQ TVKRLRRLVF PYMVPLTTVY
LFEYLINQAV APTLLFPING DERSKSMPFF FHKYRDIYVT YGTLYQLGVF ISRSFGHLMR
MRSLYILAFL QGVNLCITVL QSWFYVTHSP WAVMILIFYE GFLGGASYVN TFLNILEQED
PDETEFAMGA VSIADSFGVF LAALLGLGLE PKLCRHQIAD DRPWCRME