BAP2_YEAST
ID BAP2_YEAST Reviewed; 609 AA.
AC P38084; D6VQ67;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Leu/Val/Ile amino-acid permease;
DE AltName: Full=Branched-chain amino-acid permease 2;
GN Name=BAP2; OrderedLocusNames=YBR068C; ORFNames=YBR0629;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 139 AND 203.
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 CHARACTERIZATION.
RX PubMed=7495881; DOI=10.1016/0167-4889(95)00138-8;
RA Grauslund M., Didion T., Kielland-Brandt M.C., Andersen H.A.;
RT "BAP2, a gene encoding a permease for branched-chain amino acids in
RT Saccharomyces cerevisiae.";
RL Biochim. Biophys. Acta 1269:275-280(1995).
RN [4]
RP FUNCTION IN L-CYSTEINE UPTAKE.
RX PubMed=10467005; DOI=10.1007/s002940050459;
RA During-Olsen L., Regenberg B., Gjermansen C., Kielland-Brandt M.C.,
RA Hansen J.;
RT "Cysteine uptake by Saccharomyces cerevisiae is accomplished by multiple
RT permeases.";
RL Curr. Genet. 35:609-617(1999).
RN [5]
RP FUNCTION.
RX PubMed=10654085; DOI=10.1007/s002940050506;
RA Regenberg B., During-Olsen L., Kielland-Brandt M.C., Holmberg S.;
RT "Substrate specificity and gene expression of the amino-acid permeases in
RT Saccharomyces cerevisiae.";
RL Curr. Genet. 36:317-328(1999).
RN [6]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-24, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-16; SER-19; SER-21;
RP SER-24; SER-76 AND SER-84, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Permease for leucine, valine and isoleucine. Also transports
CC cysteine, methionine, phenyalanine, tyrosine and tryptophan.
CC {ECO:0000269|PubMed:10467005, ECO:0000269|PubMed:10654085}.
CC -!- INTERACTION:
CC P38084; Q02774: SHR3; NbExp=3; IntAct=EBI-3414, EBI-17099;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14562095};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8660 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. YAT (TC 2.A.3.10) family. {ECO:0000305}.
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DR EMBL; Z35937; CAA85012.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07187.2; -; Genomic_DNA.
DR PIR; S45930; S45930.
DR RefSeq; NP_009624.4; NM_001178416.4.
DR AlphaFoldDB; P38084; -.
DR SMR; P38084; -.
DR BioGRID; 32771; 101.
DR DIP; DIP-4910N; -.
DR IntAct; P38084; 14.
DR MINT; P38084; -.
DR STRING; 4932.YBR068C; -.
DR TCDB; 2.A.3.10.6; the amino acid-polyamine-organocation (apc) family.
DR iPTMnet; P38084; -.
DR SwissPalm; P38084; -.
DR MaxQB; P38084; -.
DR PaxDb; P38084; -.
DR PRIDE; P38084; -.
DR EnsemblFungi; YBR068C_mRNA; YBR068C; YBR068C.
DR GeneID; 852360; -.
DR KEGG; sce:YBR068C; -.
DR SGD; S000000272; BAP2.
DR VEuPathDB; FungiDB:YBR068C; -.
DR eggNOG; KOG1286; Eukaryota.
DR GeneTree; ENSGT00940000176401; -.
DR HOGENOM; CLU_007946_12_0_1; -.
DR InParanoid; P38084; -.
DR OMA; PKFLDYV; -.
DR BioCyc; YEAST:G3O-29037-MON; -.
DR PRO; PR:P38084; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38084; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; IDA:SGD.
DR GO; GO:0015192; F:L-phenylalanine transmembrane transporter activity; IMP:CACAO.
DR GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR GO; GO:0006865; P:amino acid transport; IDA:SGD.
DR GO; GO:0098713; P:leucine import across plasma membrane; IMP:CACAO.
DR GO; GO:0055085; P:transmembrane transport; IDA:SGD.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004762; Amino_acid_permease_fungi.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR00913; 2A0310; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..609
FT /note="Leu/Val/Ile amino-acid permease"
FT /id="PRO_0000054146"
FT TOPO_DOM 1..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..123
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..173
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..289
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 290..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 501..521
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 15
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 84
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 139
FT /note="V -> E (in Ref. 1; CAA85012)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="W -> G (in Ref. 1; CAA85012)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 609 AA; 67769 MW; B87FD6A7464E07F5 CRC64;
MLSSEDFGSS GKKETSPDSI SIRSFSAGNN FQSSSSEKTY SKQKSGSDKL IHRFADSFKR
AEGSTTRTKQ INENTSDLED GVESITSDSK LKKSMKSRHV VMMSLGTGIG TGLLVANAKG
LHYGGPAALI IGYILVSFVT YFMIQAAGEM AVTYPTLPAN FNAYSSIFIS KSFGFATVWL
YCFQWLTVLP LELITASMTI QFWNDKINPD IYILIFYVFL VFIHFFGVKA YGETEFIFNC
CKILMIAGFI ILSIVINCGG AGNDGYIGAT YWHNPGAFAG DTSIGRFKNV CYILVTAYFS
FGGMELFALS VQEQSNPRKS TPVAAKRSIY RIVVIYLLTM ILIGFNVPYN DDQLMGAGGS
ATHASPYVLA ASIHGVKIVP HIINAVILIS VVSVANSSLY AGPRLICSLA QQGYAPKFLD
YVDREGRPLR ALIVCCVFGV IAFVAASSKE EIVFTWLAAI AGLSELFTWT SIMLSHLRFR
QAMKVQGRSL DELGYKATTG IWGSIYGVFF NILVFVAQFW VALAPLGNGG KCDAESFFQN
YLAFPIWLAF YFGYMVYNRD FTLLNPLDKI DLDFHRRIYD PELMRQEDEE NKEKLRNMSL
MRKAYHFWC
