ROD1_YEAST
ID ROD1_YEAST Reviewed; 837 AA.
AC Q02805; D6W284; Q12475;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein ROD1;
DE AltName: Full=Resistance to o-dinitrobenzene protein 1;
GN Name=ROD1; OrderedLocusNames=YOR018W; ORFNames=OR26.08;
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8621680; DOI=10.1074/jbc.271.6.2914;
RA Wu A.L., Hallstrom T.C., Moye-Rowley W.S.;
RT "ROD1, a novel gene conferring multiple resistance phenotypes in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 271:2914-2920(1996).
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.
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 FUNCTION, DOMAIN, INTERACTION WITH RSP5, AND MUTAGENESIS OF 487-PRO-PRO-488
RP AND 656-PRO-PRO-657.
RX PubMed=12163175; DOI=10.1016/s0014-5793(02)03104-6;
RA Andoh T., Hirata Y., Kikuchi A.;
RT "PY motifs of Rod1 are required for binding to Rsp5 and for drug
RT resistance.";
RL FEBS Lett. 525:131-134(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-436 AND SER-720, AND
RP IDENTIFICATION BY 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; SER-536 AND SER-720, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-141; SER-436;
RP SER-720 AND SER-725, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-401, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Mediates resistance to o-dinitrobenzene, calcium and zinc.
CC {ECO:0000269|PubMed:12163175, ECO:0000269|PubMed:8621680}.
CC -!- SUBUNIT: Interacts with RSP5 via its 2 PY-motifs.
CC {ECO:0000269|PubMed:12163175}.
CC -!- INTERACTION:
CC Q02805; P39940: RSP5; NbExp=3; IntAct=EBI-15679, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8621680}; Peripheral
CC membrane protein {ECO:0000269|PubMed:8621680}. Note=Membrane-associated
CC or associated to a complex that cofractionates with plasma membrane.
CC -!- DOMAIN: The PY-motifs are required for the interaction with RSP5
CC ubiquitin-ligase and important for resistance to o-dinitrobenzene.
CC {ECO:0000269|PubMed:12163175}.
CC -!- MISCELLANEOUS: Present with 386 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the arrestin family. {ECO:0000305}.
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DR EMBL; U40561; AAB03678.1; -; Genomic_DNA.
DR EMBL; X87331; CAA60767.1; -; Genomic_DNA.
DR EMBL; Z74926; CAA99208.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10800.1; -; Genomic_DNA.
DR PIR; S54624; S54624.
DR RefSeq; NP_014661.1; NM_001183437.1.
DR AlphaFoldDB; Q02805; -.
DR BioGRID; 34422; 128.
DR DIP; DIP-4189N; -.
DR IntAct; Q02805; 7.
DR MINT; Q02805; -.
DR STRING; 4932.YOR018W; -.
DR iPTMnet; Q02805; -.
DR MaxQB; Q02805; -.
DR PaxDb; Q02805; -.
DR PRIDE; Q02805; -.
DR EnsemblFungi; YOR018W_mRNA; YOR018W; YOR018W.
DR GeneID; 854183; -.
DR KEGG; sce:YOR018W; -.
DR SGD; S000005544; ROD1.
DR VEuPathDB; FungiDB:YOR018W; -.
DR eggNOG; KOG3780; Eukaryota.
DR GeneTree; ENSGT00940000176571; -.
DR HOGENOM; CLU_018982_1_1_1; -.
DR InParanoid; Q02805; -.
DR OMA; IAVDNTW; -.
DR BioCyc; YEAST:G3O-33566-MON; -.
DR PRO; PR:Q02805; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q02805; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:SGD.
DR GO; GO:0000754; P:adaptation of signaling pathway by response to pheromone involved in conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IDA:SGD.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IGI:SGD.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:SGD.
DR GO; GO:0070086; P:ubiquitin-dependent endocytosis; IMP:SGD.
DR Gene3D; 2.60.40.640; -; 1.
DR InterPro; IPR014752; Arrestin-like_C.
DR InterPro; IPR011021; Arrestin-like_N.
DR InterPro; IPR011022; Arrestin_C-like.
DR Pfam; PF02752; Arrestin_C; 1.
DR Pfam; PF00339; Arrestin_N; 1.
DR SMART; SM01017; Arrestin_C; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Membrane; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..837
FT /note="Protein ROD1"
FT /id="PRO_0000097396"
FT REGION 675..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..837
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 487..490
FT /note="PY-motif"
FT MOTIF 656..659
FT /note="PY-motif"
FT COMPBIAS 681..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 725
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT MUTAGEN 487..488
FT /note="PP->QA: Reduced binding to RSP5."
FT /evidence="ECO:0000269|PubMed:12163175"
FT MUTAGEN 656..657
FT /note="PP->QA: Reduced binding to RSP5."
FT /evidence="ECO:0000269|PubMed:12163175"
FT CONFLICT 618
FT /note="Y -> D (in Ref. 1; AAB03678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 837 AA; 92349 MW; FD9A64174B1DC443 CRC64;
MFSSSSRPSK EPLLFDIRLR NLDNDVLLIK GPPDEASSVL LSGTIVLSIT EPIQIKSLAL
RLFGRLRLNI PTVLQTVHGP HKRYSKFERN IYSHFWDDFN IKSYFQNLYD NHNNGKITIS
SKSSTNLAAL PKRKRALSTA SLISSNGQTS ASKNYHTLVK GNYEFPFSAI IPGSLVESVE
GLPNAAVTYA LEATIERPKQ PDLICKKHLR VIRTLAIDAV ELSETVSVDN SWPEKVDYTI
SIPTKAIAIG SSTMINILIV PILKGLKLGP VRISLVENSQ YCGSYGGVIN QERMVAKLKL
KDPLKHVAQI KKKRSLNEAA DEGVDTDTGE FQDKWEVRAL LNIPASLTKC SQDCRILSNI
KVRHKIKFTI SLLNPDGHIS ELRAALPVQL FISPFVPVNV KTSDVIERTL KTFGPSYQVT
SQHDNSFSSK NFVDDSEEDV IFQRSASALQ LSSMPTIVSG STLNINSTDA EATAVADTTM
VTSLMVPPNY GNHVYDRVYG EVTNEDETSA SASSSAVESQ AIHNIQNLYI SDSNNSNNPI
LAPNPQIKIE DDSLNNCDSR GDSVNNSNLN LVNSNLTISE NWNNNSPSAN RYNNIINAGL
NSPSLTPSFA HLSRRNSYSR QTSSTSLKND LELTDLSRVP SYDKAMKSDM IGEDLPPAYP
EEELGVQENK KIELERPQIL HHKSTSSLLP LPGSSKSSNN LKRSSSRTHL SHSPLPRNNS
GSSVSLQQLA RNNTDSSFNL NLSFTSAKSS TGSRHFPFNM TTSFTSNSSS KNNSHFDKTD
STSDANKPRE EENYTSATHN RRSRSSSVRS NNSNSPLRQG TGSFANLMEM FTKRDRS
