ID YOR1_YEAST Reviewed; 1477 AA.
AC P53049; D6VV58;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 27-MAR-2024, entry version 209.
DE RecName: Full=Oligomycin resistance ATP-dependent permease YOR1 {ECO:0000305};
DE AltName: Full=ABC transporter YOR1;
DE AltName: Full=ABC-type Cd(2+) transporter;
DE EC=7.2.2.2 {ECO:0000269|PubMed:16814918};
DE AltName: Full=ABC-type glutathione-S-conjugate transporter;
DE EC=7.6.2.3 {ECO:0000269|PubMed:16814918};
DE AltName: Full=Yeast oligomycin resistance protein 1 {ECO:0000303|PubMed:8524254};
GN Name=YOR1 {ECO:0000303|PubMed:8524254};
GN Synonyms=YRS1 {ECO:0000303|PubMed:8663018}; OrderedLocusNames=YGR281W;
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], AND FUNCTION.
RX PubMed=8524254; DOI=10.1128/mcb.15.12.6875;
RA Katzmann D.J., Hallstrom T.C., Voet M., Wysock W., Golin J., Volckaert G.,
RA Moye-Rowley W.S.;
RT "Expression of an ATP-binding cassette transporter-encoding gene (YOR1) is
RT required for oligomycin resistance in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 15:6875-6883(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=9090054;
RX DOI=10.1002/(sici)1097-0061(19970315)13:3<251::aid-yea63>3.0.co;2-r;
RA Volckaert G., Voet M., Robben J.;
RT "Sequence analysis of a near-subtelomeric 35.4 kb DNA segment on the right
RT arm of chromosome VII from Saccharomyces cerevisiae carrying the MAL1 locus
RT reveals 15 complete open reading frames, including ZUO1, BGL2 and BIO2
RT genes and an ABC transporter gene.";
RL Yeast 13:251-259(1997).
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=8663018; DOI=10.1074/jbc.271.25.14712;
RA Cui Z., Hirata D., Tsuchiya E., Osada H., Miyakawa T.;
RT "The multidrug resistance-associated protein (MRP) subfamily (Yrs1/Yor1) of
RT Saccharomyces cerevisiae is important for the tolerance to a broad range of
RT organic anions.";
RL J. Biol. Chem. 271:14712-14716(1996).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=9575223; DOI=10.1074/jbc.273.20.12612;
RA Decottignies A., Grant A.M., Nichols J.W., de Wet H., McIntosh D.B.,
RA Goffeau A.;
RT "ATPase and multidrug transport activities of the overexpressed yeast ABC
RT protein Yor1p.";
RL J. Biol. Chem. 273:12612-12622(1998).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PHE-670.
RX PubMed=10082567; DOI=10.1128/mcb.19.4.2998;
RA Katzmann D.J., Epping E.A., Moye-Rowley W.S.;
RT "Mutational disruption of plasma membrane trafficking of Saccharomyces
RT cerevisiae Yor1p, a homologue of mammalian multidrug resistance protein.";
RL Mol. Cell. Biol. 19:2998-3009(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-71; GLU-73 AND
RP 1472-ASP--GLU-1474.
RX PubMed=12107161; DOI=10.1074/jbc.m202987200;
RA Epping E.A., Moye-Rowley W.S.;
RT "Identification of interdependent signals required for anterograde traffic
RT of the ATP-binding cassette transporter protein Yor1p.";
RL J. Biol. Chem. 277:34860-34869(2002).
RN [9]
RP INDUCTION.
RX PubMed=12529331; DOI=10.1074/jbc.m208549200;
RA Hikkel I., Lucau-Danila A., Delaveau T., Marc P., Devaux F., Jacq C.;
RT "A general strategy to uncover transcription factor properties identifies a
RT new regulator of drug resistance in yeast.";
RL J. Biol. Chem. 278:11427-11432(2003).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16814918; DOI=10.1016/j.biochi.2006.05.014;
RA Nagy Z., Montigny C., Leverrier P., Yeh S., Goffeau A., Garrigos M.,
RA Falson P.;
RT "Role of the yeast ABC transporter Yor1p in cadmium detoxification.";
RL Biochimie 88:1665-1671(2006).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-24, 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 [15]
RP DOMAIN.
RX PubMed=17615300; DOI=10.1091/mbc.e07-01-0046;
RA Pagant S., Kung L., Dorrington M., Lee M.C., Miller E.A.;
RT "Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded
RT Yor1p does not permit ER export despite the presence of a diacidic sorting
RT signal.";
RL Mol. Biol. Cell 18:3398-3413(2007).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-53, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [17]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLU-1392 AND
RP HIS-1423.
RX PubMed=17950691; DOI=10.1016/j.bbamem.2007.08.035;
RA Grigoras I., Lazard M., Plateau P., Blanquet S.;
RT "Functional characterization of the Saccharomyces cerevisiae ABC-
RT transporter Yor1p overexpressed in plasma membranes.";
RL Biochim. Biophys. Acta 1778:68-78(2008).
RN [18]
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 -!- FUNCTION: Functions as a pleiotropic drug pump at the plasma membrane
CC to clear toxic substances from the cytosol. Organic anion transporter
CC involved in the detoxification of a wide range of toxic environmental
CC organic anions that contain carboxyl groups (PubMed:8663018). Required
CC for tolerance to reveromycin A, tautomycin and leptomycin B
CC (PubMed:8663018). Required for oligomycin resistance (PubMed:8524254,
CC PubMed:10082567). Required for rhodamine B resistance. Mediates the
CC ATP-dependent efflux of rhodamine B (PubMed:9575223). Involved in
CC cadmium detoxification. Displays an energy-dependent efflux of cadmium
CC and glutathione, suggesting that YOR1 transports both compounds as a
CC bis-glutathionato-cadmium Cd-(GS)(2) complex (PubMed:16814918). Confers
CC resistance to rhodamine 6G and to doxorubicin (PubMed:17950691).
CC {ECO:0000269|PubMed:10082567, ECO:0000269|PubMed:16814918,
CC ECO:0000269|PubMed:17950691, ECO:0000269|PubMed:8524254,
CC ECO:0000269|PubMed:8663018, ECO:0000269|PubMed:9575223}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ATP + H2O
CC = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:36439, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64612, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:9575223};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36441;
CC Evidence={ECO:0000305|PubMed:9575223};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.2;
CC Evidence={ECO:0000269|PubMed:16814918};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12133;
CC Evidence={ECO:0000305|PubMed:16814918};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000269|PubMed:16814918};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000305|PubMed:16814918};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50 uM for ATP {ECO:0000269|PubMed:17950691};
CC Vmax=290 nmol/min/mg enzyme {ECO:0000269|PubMed:17950691};
CC -!- INTERACTION:
CC P53049; Q04322: GYL1; NbExp=2; IntAct=EBI-29324, EBI-27427;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10082567,
CC ECO:0000269|PubMed:12107161, ECO:0000269|PubMed:9575223}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Transcriptionally regulated by PDR8.
CC {ECO:0000269|PubMed:12529331}.
CC -!- MISCELLANEOUS: Present with 3610 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; Z73066; CAA97312.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08369.1; -; Genomic_DNA.
DR PIR; S64616; S64616.
DR RefSeq; NP_011797.3; NM_001181410.3.
DR AlphaFoldDB; P53049; -.
DR SMR; P53049; -.
DR BioGRID; 33531; 492.
DR DIP; DIP-6796N; -.
DR IntAct; P53049; 53.
DR MINT; P53049; -.
DR STRING; 4932.YGR281W; -.
DR SwissLipids; SLP:000000522; -.
DR TCDB; 3.A.1.208.3; the atp-binding cassette (abc) superfamily.
DR GlyCosmos; P53049; 3 sites, No reported glycans.
DR GlyGen; P53049; 3 sites.
DR iPTMnet; P53049; -.
DR MaxQB; P53049; -.
DR PaxDb; 4932-YGR281W; -.
DR PeptideAtlas; P53049; -.
DR EnsemblFungi; YGR281W_mRNA; YGR281W; YGR281W.
DR GeneID; 853198; -.
DR KEGG; sce:YGR281W; -.
DR AGR; SGD:S000003513; -.
DR SGD; S000003513; YOR1.
DR VEuPathDB; FungiDB:YGR281W; -.
DR eggNOG; KOG0054; Eukaryota.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; P53049; -.
DR OMA; QVTDAWT; -.
DR OrthoDB; 3295317at2759; -.
DR BioCyc; YEAST:G3O-30944-MONOMER; -.
DR Reactome; R-SCE-382556; ABC-family proteins mediated transport.
DR BioGRID-ORCS; 853198; 0 hits in 10 CRISPR screens.
DR PRO; PR:P53049; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53049; Protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0015434; F:ABC-type cadmium transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; IEA:UniProtKB-EC.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042908; P:xenobiotic transport; IDA:SGD.
DR CDD; cd18597; ABC_6TM_YOR1_D1_like; 1.
DR CDD; cd18606; ABC_6TM_YOR1_D2_like; 1.
DR CDD; cd03250; ABCC_MRP_domain1; 1.
DR CDD; cd03244; ABCC_MRP_domain2; 1.
DR Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR24223; ATP-BINDING CASSETTE SUB-FAMILY C; 1.
DR PANTHER; PTHR24223:SF443; MULTIDRUG-RESISTANCE LIKE PROTEIN 1, ISOFORM I; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1477
FT /note="Oligomycin resistance ATP-dependent permease YOR1"
FT /id="PRO_0000093450"
FT TOPO_DOM 1..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 228..249
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 271..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 350..357
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 358..370
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 371..433
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 455..478
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 500..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 616..636
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 637..892
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 893..913
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 914..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 941..961
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 962..1027
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1028..1048
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1049..1117
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1118..1138
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1139..1141
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:16847258"
FT TRANSMEM 1142..1162
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1163..1477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT DOMAIN 207..493
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 581..808
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 897..1175
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1213..1464
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 71..73
FT /note="Diacidic ER export motif DxE"
FT /evidence="ECO:0000269|PubMed:17615300"
FT COMPBIAS 1..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 621..628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1247..1254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 53
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CARBOHYD 661
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 759
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 799
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 71
FT /note="D->A: Causes the protein to be retained in the
FT endoplasmic reticulum (ER) and degraded via ER-associated
FT degradation."
FT /evidence="ECO:0000269|PubMed:12107161"
FT MUTAGEN 73
FT /note="E->A: Causes the protein to be retained in the
FT endoplasmic reticulum (ER) and degraded via ER-associated
FT degradation."
FT /evidence="ECO:0000269|PubMed:12107161"
FT MUTAGEN 670
FT /note="Missing: Causes the protein to be retained in the
FT endoplasmic reticulum (ER) and degraded via ER-associated
FT degradation."
FT /evidence="ECO:0000269|PubMed:10082567"
FT MUTAGEN 1392
FT /note="E->Q: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:17950691"
FT MUTAGEN 1423
FT /note="H->R: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:17950691"
FT MUTAGEN 1472..1474
FT /note="DFE->AFA: Causes partial retention of the protein in
FT the endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:12107161"
SQ SEQUENCE 1477 AA; 166728 MW; 40C5D36CA9B6A8C5 CRC64;
MTITVGDAVS ETELENKSQN VVLSPKASAS SDISTDVDKD TSSSWDDKSL LPTGEYIVDR
NKPQTYLNSD DIEKVTESDI FPQKRLFSFL HSKKIPEVPQ TDDERKIYPL FHTNIISNMF
FWWVLPILRV GYKRTIQPND LFKMDPRMSI ETLYDDFEKN MIYYFEKTRK KYRKRHPEAT
EEEVMENAKL PKHTVLRALL FTFKKQYFMS IVFAILANCT SGFNPMITKR LIEFVEEKAI
FHSMHVNKGI GYAIGACLMM FVNGLTFNHF FHTSQLTGVQ AKSILTKAAM KKMFNASNYA
RHCFPNGKVT SFVTTDLARI EFALSFQPFL AGFPAILAIC IVLLIVNLGP IALVGIGIFF
GGFFISLFAF KLILGFRIAA NIFTDARVTM MREVLNNIKM IKYYTWEDAY EKNIQDIRTK
EISKVRKMQL SRNFLIAMAM SLPSIASLVT FLAMYKVNKG GRQPGNIFAS LSLFQVLSLQ
MFFLPIAIGT GIDMIIGLGR LQSLLEAPED DPNQMIEMKP SPGFDPKLAL KMTHCSFEWE
DYELNDAIEE AKGEAKDEGK KNKKKRKDTW GKPSASTNKA KRLDNMLKDR DGPEDLEKTS
FRGFKDLNFD IKKGEFIMIT GPIGTGKSSL LNAMAGSMRK TDGKVEVNGD LLMCGYPWIQ
NASVRDNIIF GSPFNKEKYD EVVRVCSLKA DLDILPAGDM TEIGERGITL SGGQKARINL
ARSVYKKKDI YLFDDVLSAV DSRVGKHIMD ECLTGMLANK TRILATHQLS LIERASRVIV
LGTDGQVDIG TVDELKARNQ TLINLLQFSS QNSEKEDEEQ EAVVAGELGQ LKYESEVKEL
TELKKKATEM SQTANSGKIV ADGHTSSKEE RAVNSISLKI YREYIKAAVG KWGFIALPLY
AILVVGTTFC SLFSSVWLSY WTENKFKNRP PSFYMGLYSF FVFAAFIFMN GQFTILCAMG
IMASKWLNLR AVKRILHTPM SYIDTTPLGR ILNRFTKDTD SLDNELTESL RLMTSQFANI
VGVCVMCIVY LPWFAIAIPF LLVIFVLIAD HYQSSGREIK RLEAVQRSFV YNNLNEVLGG
MDTIKAYRSQ ERFLAKSDFL INKMNEAGYL VVVLQRWVGI FLDMVAIAFA LIITLLCVTR
AFPISAASVG VLLTYVLQLP GLLNTILRAM TQTENDMNSA ERLVTYATEL PLEASYRKPE
MTPPESWPSM GEIIFENVDF AYRPGLPIVL KNLNLNIKSG EKIGICGRTG AGKSTIMSAL
YRLNELTAGK ILIDNVDISQ LGLFDLRRKL AIIPQDPVLF RGTIRKNLDP FNERTDDELW
DALVRGGAIA KDDLPEVKLQ KPDENGTHGK MHKFHLDQAV EEEGSNFSLG ERQLLALTRA
LVRQSKILIL DEATSSVDYE TDGKIQTRIV EEFGDCTILC IAHRLKTIVN YDRILVLEKG
EVAEFDTPWT LFSQEDSIFR SMCSRSGIVE NDFENRS
//
