ADP1_YEAST
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 03-AUG-2022, entry version 204.
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; 52.
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 iPTMnet; P25371; -.
DR MaxQB; P25371; -.
DR PaxDb; P25371; -.
DR PRIDE; P25371; -.
DR EnsemblFungi; YCR011C_mRNA; YCR011C; YCR011C.
DR GeneID; 850369; -.
DR KEGG; sce:YCR011C; -.
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; IDHKYGL; -.
DR BioCyc; YEAST:G3O-29328-MON; -.
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: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; ISS:SGD.
DR GO; GO:0055085; P:transmembrane transport; ISS:SGD.
DR CDD; cd00055; EGF_Lam; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR002049; LE_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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; SSF52540; 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
