BTN2_YEAST
ID BTN2_YEAST Reviewed; 410 AA.
AC P53286; D6VUS2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein BTN2;
DE AltName: Full=Batten disease protein 2;
GN Name=BTN2; OrderedLocusNames=YGR142W;
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 FUNCTION, AND SUBCELLULAR LOCATION.
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 [4]
RP FUNCTION, INTERACTION WITH RHB1, AND SUBCELLULAR LOCATION.
RX PubMed=12456008; DOI=10.1128/ec.1.4.606-612.2002;
RA Chattopadhyay S., Pearce D.A.;
RT "Interaction with Btn2p is required for localization of Rsglp: Btn2p-
RT mediated changes in arginine uptake in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 1:606-612(2002).
RN [5]
RP INTERACTION WITH YIF1.
RX PubMed=12615067; DOI=10.1016/s0006-291x(03)00209-2;
RA Chattopadhyay S., Roberts P.M., Pearce D.A.;
RT "The yeast model for Batten disease: a role for Btn2p in the trafficking of
RT the Golgi-associated vesicular targeting protein, Yif1p.";
RL Biochem. Biophys. Res. Commun. 302:534-538(2003).
RN [6]
RP FUNCTION, AND INTERACTION WITH IST2.
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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TDA3.
RX PubMed=21441304; DOI=10.1091/mbc.e10-11-0878;
RA Kanneganti V., Kama R., Gerst J.E.;
RT "Btn3 is a negative regulator of Btn2-mediated endosomal protein
RT trafficking and prion curing in yeast.";
RL Mol. Biol. Cell 22:1648-1663(2011).
CC -!- FUNCTION: V-SNARE binding protein that facilitates specific protein
CC retrieval from a late endosome to the Golgi. Modulates the rate of
CC arginine uptake. Involved in pH homeostasis. Required for the correct
CC localization of IST2. May be involved in ion homeostasis together with
CC IST2. {ECO:0000269|PubMed:11053386, ECO:0000269|PubMed:12456008,
CC ECO:0000269|PubMed:15701790, ECO:0000269|PubMed:21441304}.
CC -!- SUBUNIT: Interacts with RHB1, IST2, TDA3 and YIF1.
CC {ECO:0000269|PubMed:12456008, ECO:0000269|PubMed:12615067,
CC ECO:0000269|PubMed:15701790, ECO:0000269|PubMed:21441304}.
CC -!- INTERACTION:
CC P53286; P38250: IST2; NbExp=2; IntAct=EBI-3796, EBI-21520;
CC P53286; P25378: RHB1; NbExp=2; IntAct=EBI-3796, EBI-15113;
CC P53286; P53845: YIF1; NbExp=2; IntAct=EBI-3796, EBI-28230;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Late endosome.
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DR EMBL; Z72927; CAA97155.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08233.1; -; Genomic_DNA.
DR PIR; S64451; S64451.
DR RefSeq; NP_011658.3; NM_001181271.3.
DR AlphaFoldDB; P53286; -.
DR BioGRID; 33388; 98.
DR DIP; DIP-5534N; -.
DR IntAct; P53286; 12.
DR MINT; P53286; -.
DR STRING; 4932.YGR142W; -.
DR iPTMnet; P53286; -.
DR PaxDb; P53286; -.
DR PRIDE; P53286; -.
DR EnsemblFungi; YGR142W_mRNA; YGR142W; YGR142W.
DR GeneID; 853043; -.
DR KEGG; sce:YGR142W; -.
DR SGD; S000003374; BTN2.
DR VEuPathDB; FungiDB:YGR142W; -.
DR eggNOG; ENOG502S308; Eukaryota.
DR HOGENOM; CLU_055876_0_0_1; -.
DR InParanoid; P53286; -.
DR OMA; MACANEL; -.
DR BioCyc; YEAST:G3O-30846-MON; -.
DR PRO; PR:P53286; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53286; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005770; C:late endosome; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:SGD.
DR GO; GO:0051087; F:chaperone binding; IPI:SGD.
DR GO; GO:0140311; F:protein sequestering activity; IMP:SGD.
DR GO; GO:0000149; F:SNARE binding; IDA:SGD.
DR GO; GO:0006865; P:amino acid transport; IMP:SGD.
DR GO; GO:0006886; P:intracellular protein transport; IMP:SGD.
DR GO; GO:0030307; P:positive regulation of cell growth; IMP:SGD.
DR GO; GO:0006457; P:protein folding; IMP:SGD.
DR GO; GO:0034504; P:protein localization to nucleus; IMP:SGD.
DR GO; GO:0006885; P:regulation of pH; IMP:SGD.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:SGD.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Endosome; Reference proteome.
FT CHAIN 1..410
FT /note="Protein BTN2"
FT /id="PRO_0000065007"
FT REGION 223..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 243..330
FT /evidence="ECO:0000255"
FT COMPBIAS 230..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..375
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 410 AA; 47168 MW; E7AE1EB1E3612F3E CRC64;
MFSIFNSPCV FEQLPSFSQP LHSRYFDCSS PVSYYPECKR RKAIKANLRA PKKSDANCSE
PLRYALAETP NGYTLSLSKR IPYELFSKYV NEKLGELKEN HYRPTYHVVQ DFFGNQYYVE
DEADEDALLR SALKDLDFRA IGKKIAKDLF QDYEIELNHR GDELSILSKK DKIFKEFSLD
QVFEDVFVIG CGVENIDDGS REKYALLKIG LVKHEEEISE GGINEPKMPI IESKIDESHD
DVNMSESLKE EEAEKAKEPL TKEDQIKKWI EEERLMQEES RKSEQEKAAK EDEERQKKEK
EARLKARKES LINKQKTKRS QQKKLQNSKS LPISEIEASN KNNNSNSGSA ESDNESINSD
SDTTLDFSVS GNTLKKHASP LLEDVEDEEV DRYNESLSRS PKGNSIIEEI
