EFR3_YEAST
ID EFR3_YEAST Reviewed; 782 AA.
AC Q03653; D6W037;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein EFR3;
GN Name=EFR3; OrderedLocusNames=YMR212C; ORFNames=YM8261.06C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
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 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 [4]
RP IDENTIFICATION BY 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643; THR-687; THR-690;
RP SER-735 AND SER-771, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=17761666; DOI=10.1074/mcp.m700098-mcp200;
RA Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,
RA van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
RT "Profiling phosphoproteins of yeast mitochondria reveals a role of
RT phosphorylation in assembly of the ATP synthase.";
RL Mol. Cell. Proteomics 6:1896-1906(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227; THR-231 AND SER-675, AND
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-564 AND SER-771, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-625; SER-632; THR-690;
RP SER-771 AND SER-774, 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).
CC -!- MISCELLANEOUS: Present with 1670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the EFR3 family. {ECO:0000305}.
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DR EMBL; Z49809; CAA89927.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10111.1; -; Genomic_DNA.
DR PIR; S55094; S55094.
DR RefSeq; NP_013939.1; NM_001182719.1.
DR PDB; 4N5A; X-ray; 3.20 A; A=8-562.
DR PDBsum; 4N5A; -.
DR AlphaFoldDB; Q03653; -.
DR SMR; Q03653; -.
DR BioGRID; 35390; 35.
DR DIP; DIP-5686N; -.
DR IntAct; Q03653; 8.
DR MINT; Q03653; -.
DR STRING; 4932.YMR212C; -.
DR iPTMnet; Q03653; -.
DR MaxQB; Q03653; -.
DR PaxDb; Q03653; -.
DR PRIDE; Q03653; -.
DR EnsemblFungi; YMR212C_mRNA; YMR212C; YMR212C.
DR GeneID; 855252; -.
DR KEGG; sce:YMR212C; -.
DR SGD; S000004825; EFR3.
DR VEuPathDB; FungiDB:YMR212C; -.
DR eggNOG; KOG1877; Eukaryota.
DR GeneTree; ENSGT00390000002143; -.
DR HOGENOM; CLU_371806_0_0_1; -.
DR InParanoid; Q03653; -.
DR OMA; LLYYVNS; -.
DR BioCyc; YEAST:G3O-32895-MON; -.
DR PRO; PR:Q03653; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03653; protein.
DR GO; GO:0071944; C:cell periphery; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:SGD.
DR DisProt; DP02751; -.
DR InterPro; IPR039786; EFR3.
DR PANTHER; PTHR47766; PTHR47766; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..782
FT /note="Protein EFR3"
FT /id="PRO_0000203332"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 564
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 687
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 690
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 47..66
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 70..86
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 88..93
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 95..106
FT /evidence="ECO:0007829|PDB:4N5A"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 115..129
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 134..138
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 141..158
FT /evidence="ECO:0007829|PDB:4N5A"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 165..177
FT /evidence="ECO:0007829|PDB:4N5A"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 188..200
FT /evidence="ECO:0007829|PDB:4N5A"
FT TURN 201..204
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:4N5A"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 296..307
FT /evidence="ECO:0007829|PDB:4N5A"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 315..327
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 337..350
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 396..412
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 420..429
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 448..459
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 464..477
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 479..493
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 499..512
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 515..526
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 533..537
FT /evidence="ECO:0007829|PDB:4N5A"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:4N5A"
FT HELIX 549..557
FT /evidence="ECO:0007829|PDB:4N5A"
SQ SEQUENCE 782 AA; 89191 MW; FE54FB221CB48F77 CRC64;
MQLSMRMMFT PKHQKLVNQC YPTGRTTDKK PKSSETSYLL YYVNSRRSKL EKVSTYLIKR
STSDLNHRRI GNIAVTLDLM NKIVLHCKEN LNVFVKDFLY IMNKVLSNNN FNNDVSVVEL
IELAFSSICQ NLDDVLCNGD MEFVQLYQNF VDLFFKIVTE RIHNDDMLLK CCIDISNTNS
VSSNPQLNHF VSKSVAYTIS KFQERNPKFK TLSLEAALES NLGKRLSRTQ TRTIGLDKAA
EDNHDLSVKA LQSYFNTTET DKLNLSIRTL LRCLQSTPNK ELLEFVCNGI PVQLRYIVIL
LLVRQLSDKD KNVNPIVSLK LMSSLLVSDV SIVGLSVLDI MRKLLNFQLK NATNKEVVAQ
SCITMTDLNH KTYYAEQTSD MLYELLLKLK SDTVKDVEKN AVVEDIDFLV EHITQPSISL
ELFIDLAHYM KNHIICLFNI VETEVPSSIL FSKLYSLLRE LDSHGVQKEM MEEIFDKYGK
MALLSGLNYF LENVSEPEYT YYSYHLQAAN FLKLNDYKSQ TEYKMQTRTL FTKEDLLSYY
SDTGSNKYSK KGAQILLSRD NQISTSDLLS DSQVRTTPLE YKNVPNAIFS NGKAVYDNND
FAAKQNKFDN SIDDNIEEAN DTVISDANAK GSIYRFVAED ARSWKTMRAT APKVSDLKKT
MNEKNIPNNM KRDGSFRGSQ SVKSRVTNIT FLLNELKTFS DDANKIKDPD EENIVGLDKI
DVARSNSLRL APISSLSDRS SIGNRKSFLQ KTATGENQND DFKDANEDLH SLSSRGKIFS
ST
