ETP1_YEAST
ID ETP1_YEAST Reviewed; 585 AA.
AC P38748; D3DKQ3; Q6Q5F9;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=RING finger protein ETP1;
DE AltName: Full=BRAP2 homolog;
DE AltName: Full=Ethanol tolerance protein 1;
GN Name=ETP1; OrderedLocusNames=YHL010C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091229; DOI=10.1126/science.8091229;
RA Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA Waterston R., Wilson R., Vaudin M.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT VIII.";
RL Science 265:2077-2082(1994).
RN [2]
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 [3]
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 [4]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-369 AND LYS-410, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [5]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-410, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=14557538; DOI=10.1073/pnas.2135500100;
RA Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
RT "A subset of membrane-associated proteins is ubiquitinated in response to
RT mutations in the endoplasmic reticulum degradation machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
RN [6]
RP FUNCTION.
RX PubMed=19416103; DOI=10.1111/j.1567-1364.2009.00497.x;
RA Snowdon C., Schierholtz R., Poliszczuk P., Hughes S., van der Merwe G.;
RT "ETP1/YHL010c is a novel gene needed for the adaptation of Saccharomyces
RT cerevisiae to ethanol.";
RL FEMS Yeast Res. 9:372-380(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION BY
RP 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).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-369 AND LYS-450, AND
RP IDENTIFICATION BY 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: May act as a cytoplasmic retention protein with a role in
CC regulating nuclear transport. Binds nuclear localization sequences in
CC vitro. Needed to adapt efficiently to ethanol, either as sole carbon
CC source or as cell stressor. Involved in ethanol-dependent
CC transcriptional activation of several genes and ethanol-induced protein
CC turnover of some proteins. {ECO:0000269|PubMed:19416103}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; U11582; AAB65064.1; -; Genomic_DNA.
DR EMBL; AY558115; AAS56441.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06676.1; -; Genomic_DNA.
DR PIR; S46825; S46825.
DR RefSeq; NP_011853.1; NM_001179090.1.
DR AlphaFoldDB; P38748; -.
DR SMR; P38748; -.
DR BioGRID; 36413; 79.
DR DIP; DIP-2987N; -.
DR IntAct; P38748; 4.
DR MINT; P38748; -.
DR STRING; 4932.YHL010C; -.
DR iPTMnet; P38748; -.
DR MaxQB; P38748; -.
DR PaxDb; P38748; -.
DR PRIDE; P38748; -.
DR EnsemblFungi; YHL010C_mRNA; YHL010C; YHL010C.
DR GeneID; 856376; -.
DR KEGG; sce:YHL010C; -.
DR SGD; S000001002; ETP1.
DR VEuPathDB; FungiDB:YHL010C; -.
DR eggNOG; KOG0804; Eukaryota.
DR GeneTree; ENSGT00500000044909; -.
DR HOGENOM; CLU_009969_0_1_1; -.
DR InParanoid; P38748; -.
DR OMA; GIIHLYK; -.
DR BioCyc; YEAST:G3O-31032-MON; -.
DR PRO; PR:P38748; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38748; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:0045471; P:response to ethanol; IMP:SGD.
DR CDD; cd12717; RRM_ETP1; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR011422; BRAP2.
DR InterPro; IPR034931; ETP1_RRM.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF07576; BRAP2; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Metal-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..585
FT /note="RING finger protein ETP1"
FT /id="PRO_0000056337"
FT ZN_FING 240..280
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 277..377
FT /note="UBP-type; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 372..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..585
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 313
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 332
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 338
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 369
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 410
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131,
FT ECO:0000269|PubMed:14557538"
FT CROSSLNK 450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 558
FT /note="T -> I (in Ref. 3; AAS56441)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 67503 MW; 88FF670CC73A1263 CRC64;
MDQFEYIITL EFGNQNQVES AYQIFKSIPK KLKAKSIGEE SIKSNNQDWQ DWRVCDLEID
MITDFKNQTS KEEESDLITS QYLGHGIIRL FKLSNANNTL NEKEILTIPG DDTMICILFV
PTYFTVHDLL HFYIGDDIVN KQVSNFRILR NQQKGMGFNF TVLIKFRNAL DAKNFKEEFN
GKSFSRMDPE TCHVISVKEI VFQKKLFQRP AANEDFPYLL TDPFTVKKKK ELVKVELPTC
PVCLERMDSE TTGLVTIPCQ HTFHCQCLNK WKNSRCPVCR HSSLRLSRES LLKQAGDSAH
CATCGSTDNL WICLICGNVG CGRYNSKHAI KHYEETLHCF AMDIRTQRVW DYAGDNYVHR
LVQNEVDGKL VEVGGSGDDD NNDIGNSDEL QNVVYGNRSK NGEKSNSNKK DGELAANFLR
HREYHLEYVQ VLISQLESQR EYYELKLQEK DQTASDSSNV ESLKKSMEDL KLQFQVTQKE
WQKREMAQKS KLEEDMLVIE GLQANLDHLS KKQEQLEREN KALEESKQDL EEQVKDLMFY
LDSQEKFKDA DESVKEGTIL IQQPHGAAQA SKSKKKRNKN KKAGK
