MLF3_YEAST
ID MLF3_YEAST Reviewed; 452 AA.
AC P32047; D6W1A5;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein MLF3;
DE AltName: Full=Multicopy suppressor of leflunomide sensitivity 3;
GN Name=MLF3; Synonyms=YMK1; OrderedLocusNames=YNL074C; ORFNames=N2359;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8701611;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<391::aid-yea921>3.0.co;2-n;
RA Poehlmann R., Philippsen P.;
RT "Sequencing a cosmid clone of Saccharomyces cerevisiae chromosome XIV
RT reveals 12 new open reading frames (ORFs) and an ancient duplication of six
RT ORFs.";
RL Yeast 12:391-402(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(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 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
RX PubMed=2016746; DOI=10.1016/0022-2836(91)90701-7;
RA Gatti D., Tzagoloff A.;
RT "Structure and evolution of a group of related aminoacyl-tRNA
RT synthetases.";
RL J. Mol. Biol. 218:557-568(1991).
RN [6]
RP INVOLVEMENT IN LEFLUNOMIDE RESISTANCE.
RX PubMed=9805003; DOI=10.1016/s0167-4781(98)00190-0;
RA Fujimura H.A.;
RT "Saccharomyces cerevisiae MLF3/YNL074C gene, encoding a serine-rich protein
RT of unknown function, determines the level of resistance to the novel
RT immunosuppressive drug leflunomide.";
RL Biochim. Biophys. Acta 1442:415-418(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8 AND SER-171, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-227, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-56; SER-74;
RP SER-189; TYR-295; SER-297 AND SER-439, AND IDENTIFICATION BY MASS
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-74; SER-79;
RP THR-121; SER-145; SER-156; SER-160; THR-169; THR-173; SER-183; SER-189;
RP TYR-227; SER-228; SER-257; SER-265; TYR-295; SER-297; SER-320; SER-353 AND
RP SER-439, AND 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: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Disruption of the MLF3 gene causes increased sensitivity
CC to the immunosuppressant leflunomide.
CC -!- SIMILARITY: To yeast VHS2. {ECO:0000305}.
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DR EMBL; X86470; CAA60186.1; -; Genomic_DNA.
DR EMBL; Z71350; CAA95948.1; -; Genomic_DNA.
DR EMBL; AY692774; AAT92793.1; -; Genomic_DNA.
DR EMBL; X57360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006947; DAA10471.1; -; Genomic_DNA.
DR PIR; S53906; S53906.
DR RefSeq; NP_014325.3; NM_001182912.3.
DR AlphaFoldDB; P32047; -.
DR BioGRID; 35749; 62.
DR IntAct; P32047; 5.
DR MINT; P32047; -.
DR STRING; 4932.YNL074C; -.
DR iPTMnet; P32047; -.
DR SwissPalm; P32047; -.
DR MaxQB; P32047; -.
DR PaxDb; P32047; -.
DR PRIDE; P32047; -.
DR TopDownProteomics; P32047; -.
DR EnsemblFungi; YNL074C_mRNA; YNL074C; YNL074C.
DR GeneID; 855650; -.
DR KEGG; sce:YNL074C; -.
DR SGD; S000005018; MLF3.
DR VEuPathDB; FungiDB:YNL074C; -.
DR eggNOG; ENOG502S4KQ; Eukaryota.
DR GeneTree; ENSGT00940000176806; -.
DR HOGENOM; CLU_061868_0_0_1; -.
DR InParanoid; P32047; -.
DR OMA; NINNTGM; -.
DR BioCyc; YEAST:G3O-33103-MON; -.
DR PRO; PR:P32047; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P32047; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IGI:SGD.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..452
FT /note="Protein MLF3"
FT /id="PRO_0000096499"
FT REGION 61..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 121
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 169
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15665377"
FT MOD_RES 173
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 295
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 452 AA; 49210 MW; 9C4FB02D38D6963E CRC64;
MCVYKSNSNN SNPSFIFERT VQEASSNDLF LQPPVSASNT SHSSRSNSFY NLQTISPIPI
SGSEVRTPSL RKNSNNVSSP LDNVIPTSRS ASNSTTSSLA HQEYILNPIC NMQNHHHRRR
TLENSVAPAL DASCSIVNDE NTDLSDVDMV YSRRPSSAVS LNMALLARTN SATLPSSESS
PASPDLKLSR SHSHSAATRP TLNNINNTGM TTTTSNGEPN SRILRFYSYV DMLNDEKLAQ
ANNTPTSRPP MKSQAYSCPF ILKRSPPQAY SSSSATTTFS NPFIKTTELP ATSPYVSPQQ
SARQYSNNAN NNAKSPKNRS SSILFQRQSI LSNVDPVANM HKNPKFQIES SDSEEEDLTM
DMLDPSFPLS SSLRSSANLA SNPELATQTP LSTSSSYTAI GKPMPLSTDP SYVSSSNTLS
SEHELRVEKV SEVLKKKVSN GGFSTEFNSC DT