YO075_YEAST
ID YO075_YEAST Reviewed; 1294 AA.
AC Q08234; D6W1Z3; Q08233;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein/permease YOL075C;
GN OrderedLocusNames=YOL075C; ORFNames=YOL074C;
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].
RX PubMed=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 1164.
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 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 [5]
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).
CC -!- INTERACTION:
CC Q08234; P48558: BXI1; NbExp=2; IntAct=EBI-29278, EBI-28349;
CC Q08234; P33302: PDR5; NbExp=3; IntAct=EBI-29278, EBI-13038;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC PDR (TC 3.A.1.205) subfamily. {ECO:0000305}.
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DR EMBL; Z74817; CAA99085.1; -; Genomic_DNA.
DR EMBL; Z74816; CAA99084.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10709.2; -; Genomic_DNA.
DR PIR; S77690; S77690.
DR RefSeq; NP_014567.2; NM_001183329.2.
DR AlphaFoldDB; Q08234; -.
DR SMR; Q08234; -.
DR BioGRID; 34327; 49.
DR DIP; DIP-8021N; -.
DR IntAct; Q08234; 21.
DR MINT; Q08234; -.
DR STRING; 4932.YOL075C; -.
DR CarbonylDB; Q08234; -.
DR iPTMnet; Q08234; -.
DR PaxDb; Q08234; -.
DR PRIDE; Q08234; -.
DR EnsemblFungi; YOL075C_mRNA; YOL075C; YOL075C.
DR GeneID; 854080; -.
DR KEGG; sce:YOL075C; -.
DR SGD; S000005435; YOL075C.
DR VEuPathDB; FungiDB:YOL075C; -.
DR eggNOG; KOG0065; Eukaryota.
DR GeneTree; ENSGT00940000159739; -.
DR HOGENOM; CLU_000604_57_4_1; -.
DR InParanoid; Q08234; -.
DR OMA; ACGYFVQ; -.
DR BioCyc; YEAST:G3O-33479-MON; -.
DR PRO; PR:Q08234; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08234; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0000329; C:fungal-type vacuole membrane; IDA:SGD.
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:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013525; ABC_2_trans.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR043926; ABCG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01061; ABC2_membrane; 2.
DR Pfam; PF19055; ABC2_membrane_7; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1294
FT /note="Uncharacterized ABC transporter ATP-binding
FT protein/permease YOL075C"
FT /id="PRO_0000093467"
FT TOPO_DOM 1..375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..495
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..530
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..604
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..1038
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1039..1059
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1060..1120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 1121..1141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1142..1266
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1267..1287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1288..1294
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..287
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 679..941
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 727..734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 528
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 1164
FT /note="A -> R (in Ref. 1 and 2; CAA99085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1294 AA; 145072 MW; D2CA5E455C39284E CRC64;
MSQQENGDVA TELIENRLSF SRIPRISLHV RDLSIVASKT NTTLVNTFSM DLPSGSVMAV
MGGSGSGKTT LLNVLASKIS GGLTHNGSIR YVLEDTGSEP NETEPKRAHL DGQDHPIQKH
VIMAYLPQQD VLSPRLTCRE TLKFAADLKL NSSERTKKLM VEQLIEELGL KDCADTLVGD
NSHRGLSGGE KRRLSIGTQM ISNPSIMFLD EPTTGLDAYS AFLVIKTLKK LAKEDGRTFI
MSIHQPRSDI LFLLDQVCIL SKGNVVYCDK MDNTIPYFES IGYHVPQLVN PADYFIDLSS
VDSRSDKEEA ATQSRLNSLI DHWHDYERTH LQLQAESYIS NATEIQIQNM TTRLPFWKQV
TVLTRRNFKL NFSDYVTLIS TFAEPLIIGT VCGWIYYKPD KSSIGGLRTT TACLYASTIL
QCYLYLLFDT YRLCEQDIAL YDRERAEGSV TPLAFIVARK ISLFLSDDFA MTMIFVSITY
FMFGLEADAR KFFYQFAVVF LCQLSCSGLS MLSVAVSRDF SKASLVGNMT FTVLSMGCGF
FVNAKVMPVY VRWIKYIAFT WYSFGTLMSS TFTNSYCTTD NLDECLGNQI LEVYGFPRNW
ITVPAVVLLC WSVGYFVVGA IILYLHKIDI TLQNEVKSKQ KKIKKKSPTG MKPEIQLLDD
VYHQKDLEAE KGKNIHITIK LEDIDLRVIF SAPFSNWKEG NFHHETKEIL QSVNAIFKPG
MINAIMGPSG SGKSSLLNLI SGRLKSSVFA KFDTSGSIMF NDIQVSELMF KNVCSYVSQD
DDHLLAALTV KETLKYAAAL RLHHLTEAER MERTDNLIRS LGLKHCENNI IGNEFVKGIS
GGEKRRVTMG VQLLNDPPIL LLDEPTSGLD SFTSATILEI LEKLCREQGK TIIITIHQPR
SELFKRFGNV LLLAKSGRTA FNGSPDEMIA YFTELGYNCP SFTNVADFFL DLISVNTQNE
QNEISSRARV EKILSAWKAN MDNESLSPTP ISEKQQYSQE SFFTEYSEFV RKPANLVLAY
IVNVKRQFTT TRRSFDSLMA RIAQIPGLGV IFALFFAPVK HNYTSISNRL GLAQESTALY
FVGMLGNLAC YPTERDYFYE EYNDNVYGIA PFFLAYMTLE LPLSALASVL YAVFTVLACG
LPRTAGNFFA TVYCSFIVTC CGEALGIMTN TFFERPGFVV NCISIILSIG TQMSGLMSLG
MSRVLKGFNY LNPVGYTSMI IINFAFPGNL KLTCEDGGKN SDGTCEFANG HDVLVSYGLV
RNTQKYLGII VCVAIIYRLI AFFILKAKLE WIKW
