ID   ADP1_YEAST              Reviewed;        1049 AA.
AC   P25371; D6VR20;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   27-MAR-2024, entry version 210.
DE   RecName: Full=Probable ATP-dependent permease;
DE   Flags: Precursor;
GN   Name=ADP1; OrderedLocusNames=YCR011C; ORFNames=YCR105, YCR11C;
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=1789009; DOI=10.1002/yea.320070813;
RA   Purnelle B., Skala J., Goffeau A.;
RT   "The product of the YCR105 gene located on the chromosome III from
RT   Saccharomyces cerevisiae presents homologies to ATP-dependent permeases.";
RL   Yeast 7:867-872(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1626432; DOI=10.1002/yea.320080508;
RA   Skala J., Purnelle B., Goffeau A.;
RT   "The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm
RT   of chromosome III from Saccharomyces cerevisiae reveals seven open reading
RT   frames including the RVS161, ADP1 and PGK genes.";
RL   Yeast 8:409-417(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=1574125; DOI=10.1038/357038a0;
RA   Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M.,
RA   Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G.,
RA   Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A.,
RA   Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C.,
RA   Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M.,
RA   Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C.,
RA   Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F.,
RA   Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C.,
RA   Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E.,
RA   Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P.,
RA   Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J.,
RA   Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P.,
RA   Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M.,
RA   Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P.,
RA   Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G.,
RA   Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E.,
RA   Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F.,
RA   Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L.,
RA   Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J.,
RA   Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M.,
RA   Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A.,
RA   Richterich P., Roberts A.B., Rodriguez F., Sanz E.,
RA   Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J.,
RA   Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I.,
RA   Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M.,
RA   Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M.,
RA   Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D.,
RA   Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K.,
RA   Sgouros J.G.;
RT   "The complete DNA sequence of yeast chromosome III.";
RL   Nature 357:38-46(1992).
RN   [4]
RP   SEQUENCE REVISION TO 29.
RA   Valles G., Volckaerts G.;
RL   Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [7]
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   [8]
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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-659 AND SER-702, AND
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-659 AND SER-702, 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).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCG family.
CC       Eye pigment precursor importer (TC 3.A.1.204) subfamily. {ECO:0000305}.
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DR   EMBL; X59720; CAA42328.2; -; Genomic_DNA.
DR   EMBL; AY693056; AAT93075.1; -; Genomic_DNA.
DR   EMBL; BK006937; DAA07489.1; -; Genomic_DNA.
DR   PIR; S19421; S19421.
DR   RefSeq; NP_009937.2; NM_001178724.1.
DR   AlphaFoldDB; P25371; -.
DR   SMR; P25371; -.
DR   BioGRID; 30990; 81.
DR   DIP; DIP-1775N; -.
DR   IntAct; P25371; 14.
DR   MINT; P25371; -.
DR   STRING; 4932.YCR011C; -.
DR   TCDB; 3.A.1.204.9; the atp-binding cassette (abc) superfamily.
DR   GlyCosmos; P25371; 5 sites, No reported glycans.
DR   GlyGen; P25371; 5 sites.
DR   iPTMnet; P25371; -.
DR   MaxQB; P25371; -.
DR   PaxDb; 4932-YCR011C; -.
DR   PeptideAtlas; P25371; -.
DR   EnsemblFungi; YCR011C_mRNA; YCR011C; YCR011C.
DR   GeneID; 850369; -.
DR   KEGG; sce:YCR011C; -.
DR   AGR; SGD:S000000604; -.
DR   SGD; S000000604; ADP1.
DR   VEuPathDB; FungiDB:YCR011C; -.
DR   eggNOG; KOG0061; Eukaryota.
DR   GeneTree; ENSGT00940000165949; -.
DR   HOGENOM; CLU_000604_57_1_1; -.
DR   InParanoid; P25371; -.
DR   OMA; NCQLDAF; -.
DR   OrthoDB; 359054at2759; -.
DR   BioCyc; YEAST:G3O-29328-MONOMER; -.
DR   BioGRID-ORCS; 850369; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P25371; -.
DR   Proteomes; UP000002311; Chromosome III.
DR   RNAct; P25371; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; HDA:SGD.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; ISS:SGD.
DR   GO; GO:0055085; P:transmembrane transport; ISS:SGD.
DR   CDD; cd03213; ABCG_EPDR; 1.
DR   CDD; cd00055; EGF_Lam; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR043926; ABCG_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR48041; ABC TRANSPORTER G FAMILY MEMBER 28; 1.
DR   PANTHER; PTHR48041:SF139; PROTEIN SCARLET; 1.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   Pfam; PF19055; ABC2_membrane_7; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Endoplasmic reticulum; Glycoprotein; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..1049
FT                   /note="Probable ATP-dependent permease"
FT                   /id="PRO_0000000257"
FT   TOPO_DOM        26..324
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        346..463
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        464..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        482..793
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        794..814
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        815..828
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        829..849
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        850..877
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        878..898
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        899..909
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        910..930
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        931..937
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        938..958
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        959..1000
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1001..1021
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1022..1024
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1025..1045
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1046..1049
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          384..631
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          793..1044
FT                   /note="ABC transmembrane type-2"
FT   BINDING         423..430
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MOD_RES         659
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         702
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   CARBOHYD        50
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        114
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        221
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        935
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        29
FT                   /note="K -> E (in Ref. 1; no nucleotide entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1049 AA;  117231 MW;  A3E9CE54BC28407B CRC64;
     MGSHRRYLYY SILSFLLLSC SVVLAKQDKT PFFEGTSSKN SRLTAQDKGN DTCPPCFNCM
     LPIFECKQFS ECNSYTGRCE CIEGFAGDDC SLPLCGGLSP DESGNKDRPI RAQNDTCHCD
     NGWGGINCDV CQEDFVCDAF MPDPSIKGTC YKNGMIVDKV FSGCNVTNEK ILQILNGKIP
     QITFACDKPN QECNFQFWID QLESFYCGLS DCAFEYDLEQ NTSHYKCNDV QCKCVPDTVL
     CGAKGSIDIS DFLTETIKGP GDFSCDLETR QCKFSEPSMN DLILTVFGDP YITLKCESGE
     CVHYSEIPGY KSPSKDPTVS WQGKLVLALT AVMVLALFTF ATFYISKSPL FRNGLGSSKS
     PIRLPDEDAV NNFLQNEDDT LATLSFENIT YSVPSINSDG VEETVLNEIS GIVKPGQILA
     IMGGSGAGKT TLLDILAMKR KTGHVSGSIK VNGISMDRKS FSKIIGFVDQ DDFLLPTLTV
     FETVLNSALL RLPKALSFEA KKARVYKVLE ELRIIDIKDR IIGNEFDRGI SGGEKRRVSI
     ACELVTSPLV LFLDEPTSGL DASNANNVIE CLVRLSSDYN RTLVLSIHQP RSNIFYLFDK
     LVLLSKGEMV YSGNAKKVSE FLRNEGYICP DNYNIADYLI DITFEAGPQG KRRRIRNISD
     LEAGTDTNDI DNTIHQTTFT SSDGTTQREW AHLAAHRDEI RSLLRDEEDV EGTDGRRGAT
     EIDLNTKLLH DKYKDSVYYA ELSQEIEEVL SEGDEESNVL NGDLPTGQQS AGFLQQLSIL
     NSRSFKNMYR NPKLLLGNYL LTILLSLFLG TLYYNVSNDI SGFQNRMGLF FFILTYFGFV
     TFTGLSSFAL ERIIFIKERS NNYYSPLAYY ISKIMSEVVP LRVVPPILLS LIVYPMTGLN
     MKDNAFFKCI GILILFNLGI SLEILTIGII FEDLNNSIIL SVLVLLGSLL FSGLFINTKN
     ITNVAFKYLK NFSVFYYAYE SLLINEVKTL MLKERKYGLN IEVPGATILS TFGFVVQNLV
     FDIKILALFN VVFLIMGYLA LKWIVVEQK
//