YBT1_YEAST
ID YBT1_YEAST Reviewed; 1661 AA.
AC P32386; D6VXW0; Q07882;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=ATP-dependent bile acid permease;
GN Name=YBT1; Synonyms=BAT1; OrderedLocusNames=YLL048C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-378.
RX PubMed=8139928; DOI=10.1093/nar/22.5.869;
RA Cusick M.E.;
RT "RNP1, a new ribonucleoprotein gene of the yeast Saccharomyces
RT cerevisiae.";
RL Nucleic Acids Res. 22:869-877(1994).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9182565; DOI=10.1074/jbc.272.24.15358;
RA Ortiz D.F., St Pierre M.V., Abdulmessih A., Arias I.M.;
RT "A yeast ATP-binding cassette-type protein mediating ATP-dependent bile
RT acid transport.";
RL J. Biol. Chem. 272:15358-15365(1997).
RN [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-936, AND IDENTIFICATION BY
RP 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-940 AND SER-955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE 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).
RN [10]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=21649806; DOI=10.1111/j.1600-0854.2011.01228.x;
RA Gulshan K., Moye-Rowley W.S.;
RT "Vacuolar import of phosphatidylcholine requires the ATP-binding cassette
RT transporter Ybt1.";
RL Traffic 12:1257-1268(2011).
RN [11]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=22970809; DOI=10.1042/bj20120847;
RA Sasser T.L., Padolina M., Fratti R.A.;
RT "The Yeast vacuolar ABC transporter Ybt1p regulates membrane fusion through
RT Ca2+ transport modulation.";
RL Biochem. J. 448:365-372(2012).
CC -!- FUNCTION: Vacuolar class C ABC transporter which regulates the
CC translocation of phosphatidylcholine to the vacuole lumen, the release
CC of lumenal calcium stores, and acts as a negative regulator of vacuole
CC fusion. Exhibits ATP-dependent bile acid transport.
CC {ECO:0000269|PubMed:21649806, ECO:0000269|PubMed:22970809}.
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:21649806,
CC ECO:0000269|PubMed:22970809}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:21649806,
CC ECO:0000269|PubMed:22970809}.
CC -!- MISCELLANEOUS: Present with 3000 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; Z73153; CAA97500.1; -; Genomic_DNA.
DR EMBL; M88608; AAA20992.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09276.1; -; Genomic_DNA.
DR PIR; S64800; S64800.
DR RefSeq; NP_013052.1; NM_001181868.1.
DR AlphaFoldDB; P32386; -.
DR SMR; P32386; -.
DR BioGRID; 31267; 86.
DR DIP; DIP-6474N; -.
DR IntAct; P32386; 15.
DR MINT; P32386; -.
DR STRING; 4932.YLL048C; -.
DR TCDB; 3.A.1.208.12; the atp-binding cassette (abc) superfamily.
DR iPTMnet; P32386; -.
DR MaxQB; P32386; -.
DR PaxDb; P32386; -.
DR PRIDE; P32386; -.
DR EnsemblFungi; YLL048C_mRNA; YLL048C; YLL048C.
DR GeneID; 850678; -.
DR KEGG; sce:YLL048C; -.
DR SGD; S000003971; YBT1.
DR VEuPathDB; FungiDB:YLL048C; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000176323; -.
DR HOGENOM; CLU_000604_27_6_1; -.
DR InParanoid; P32386; -.
DR OMA; ICMATPV; -.
DR BioCyc; MetaCyc:G3O-32147-MON; -.
DR BioCyc; YEAST:G3O-32147-MON; -.
DR Reactome; R-SCE-189483; Heme degradation.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR Reactome; R-SCE-9749641; Aspirin ADME.
DR Reactome; R-SCE-9753281; Paracetamol ADME.
DR Reactome; R-SCE-9754706; Atorvastatin ADME.
DR PRO; PR:P32386; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P32386; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; IDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033285; F:ATPase-coupled monocarboxylic acid transmembrane transporter activity; IMP:SGD.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0015718; P:monocarboxylic acid transport; IMP:SGD.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Calcium; Calcium transport; Glycoprotein; Ion transport;
KW Membrane; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Transmembrane; Transmembrane helix; Transport; Vacuole.
FT CHAIN 1..1661
FT /note="ATP-dependent bile acid permease"
FT /id="PRO_0000093447"
FT TOPO_DOM 1..33
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 96..133
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..154
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..166
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 167..187
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 188..205
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 206..226
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 227..345
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 346..366
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 367..393
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 394..414
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 415..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 496..516
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 517..519
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 520..540
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 541..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 603..623
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 624..644
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 645..665
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 666..1053
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1054..1074
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1075..1114
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1115..1135
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1136..1178
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1179..1199
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1200
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1201..1221
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1222..1292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1293..1313
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1314..1315
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 1316..1336
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1337..1661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 354..662
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 694..935
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 1026..1345
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1381..1636
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 445..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 729..736
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1415..1422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 936
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 940
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 172..174
FT /note="TIT -> QIH (in Ref. 3; AAA20992)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="LR -> FS (in Ref. 3; AAA20992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1661 AA; 189162 MW; E71D3D57A3013C38 CRC64;
MHHVLNSTRP DHRFWFYDDV TQYGRTKYLN YYTPLVLLIF TVLFITYNIW KHYYYYDVLH
LKQKNPIDEL LYSSTDEDEQ SPLINNNTIT TNYVDNNCTK DALKNRHFSL EKLKSVKVNG
EPHGTPEIVR RGFIEKSRII LEFFLVLSQV IIHSFILLHY VNKNPEFTQQ GTITGLVEWC
ALFIIVSLRL ANVNQNFKFI NKYPGNLWSV SFINYLALFI SMILPFRSIF IHHINSPISR
KYYISQISIN LALFLLLFFA RIRNNFAIIY KTDSWITPSP EPVTSIAGFI CWAWLDSFVW
KAHKVSIKVK DIWGLMMQDY SFFVVKKFRY FVDHKVKRKR IFSLNLFFFF SNYLVLQCFW
AFLGSVLSFI PTVLLKRILE YVEDQSSAPS NLAWFYVTVM FVGRILVAIC QAQALFFGRR
VCIRMKSIII SEIYTKALRR KISTNKTKPS NEDPQEINDQ KSINGDEEST SSANLGAIIN
LMAIDAFKVS EICGYLHSFL EAFVMTVVAL ALLYRLLGFA AIVGVLIIVA MLPLNYKLAK
YIGDLQKKNL AVTDNRIQKL NEAFQAIRII KYFSWEENFE KDINTIRENE LSLLLMRSIV
WSISSFLWFV TPTIVTAASF AYYIYVQGEV LTTPVAFTAL SLFTLLRDPL DRLSDMLSFV
VQSKVSLDRV QDFLNENDTK KYDQLTIDPN GNRFAFENST ISWDKDNQDF KLKDLNIEFK
TGKLNVVIGP TGSGKTSLLM ALLGEMYLLN GKVVVPALEP RQELIVDANG TTNSIAYCSQ
AAWLLNDTVK NNILFNSPFN EARYKAVVEA CGLKRDFEIL KAGDLTEIGE KGITLSGGQK
QRVSLARALY SNARHVLLDD CLSAVDSHTA SWIYDNCITG PLMEDRTCIL VSHNIALTLR
NAELVVLLED GRVKDQGDPI DMLQKGLFGE DELVKSSILS RANSSANLAA KSSTSLSNLP
AVKEQQVSVN NNSSHFEAKK LQKSLRTEAE RTEDGKLIKE ETKEEGVVGL DVYKWYLKIF
GGWKIVSFLA SLFLIAQLLY IGQSWWVRAW ASHNVIAKII PRAQRAIAFI SKKASHLIDW
RGSSQISMAS AENQPSSGHS TMYYLVLYLI IGFAQALLGA GKTILNFVAG INASRKIFNM
ILNKVLHSKI RFFDATPTGR IMNRFSKDIE AIDQELTPYI QGAFYSLIEC LSTVILITFI
TPQFLSVAIV VSILYYFVGY FYMAGSRELK RFESISRSPI YQHFSETLVG VTTIRAFGDE
GRFMQENLHK IDENNKPFFY LWVANRWLAF RIDMIGSLVI FGAGLFILFN INNLDSGMAG
ISLTYAISFT EGALWLVRLY SEVEMNMNSV ERVKEYMEIE QEPYNEHKEI PPPQWPQDGK
IEVNDLSLRY APNLPRVIKN VSFSVDAQSK IGIVGRTGAG KSTIITALFR FLEPETGHIK
IDNIDISGVD LQRLRRSITI IPQDPTLFSG TIKTNLDPYD EFSDRQIFEA LKRVNLISEE
QLQQGATRET SNEASSTNSE NVNKFLDLSS EISEGGSNLS QGQRQLMCLA RSLLRSPKII
LLDEATASID YSSDAKIQET IRKEFQGSTI LTIAHRLRSV IDYDKILVMD AGEVKEYDHP
YSLLLNKQSA FYSMCEHSGE LDILIELAKK AFVEKLNSKK D
