FRM2_YEAST
ID FRM2_YEAST Reviewed; 193 AA.
AC P37261; D6VQZ0; Q8NIM8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Fatty acid repression mutant protein 2;
GN Name=FRM2; OrderedLocusNames=YCL026C-A; ORFNames=YCLX08C, YCLX8C;
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=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 [2]
RP SEQUENCE REVISION TO 105-115.
RA Valles G., Volckaerts G.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
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 IDENTIFICATION, AND SIMILARITY.
RX PubMed=8313894; DOI=10.1002/j.1460-2075.1994.tb06287.x;
RA Koonin E.V., Bork P., Sander C.;
RT "Yeast chromosome III: new gene functions.";
RL EMBO J. 13:493-503(1994).
RN [5]
RP FUNCTION.
RX PubMed=8701605;
RX DOI=10.1002/(sici)1097-0061(19960330)12:4<319::aid-yea914>3.0.co;2-#;
RA McHale M.W., Kroening K.D., Bernlohr D.A.;
RT "Identification of a class of Saccharomyces cerevisiae mutants defective in
RT fatty acid repression of gene transcription and analysis of the frm2
RT gene.";
RL Yeast 12:319-331(1996).
RN [6]
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 [7]
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).
CC -!- FUNCTION: Involved in negative regulation of fatty acid metabolism.
CC {ECO:0000269|PubMed:8701605}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
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DR EMBL; X59720; CAC42960.1; -; Genomic_DNA.
DR EMBL; BK006937; DAA07459.1; -; Genomic_DNA.
DR PIR; S53591; S53591.
DR RefSeq; NP_009904.2; NM_001178713.1.
DR PDB; 4URP; X-ray; 2.99 A; A/B=1-193.
DR PDBsum; 4URP; -.
DR AlphaFoldDB; P37261; -.
DR SMR; P37261; -.
DR BioGRID; 30958; 85.
DR DIP; DIP-3881N; -.
DR IntAct; P37261; 2.
DR MINT; P37261; -.
DR STRING; 4932.YCL026C-A; -.
DR iPTMnet; P37261; -.
DR PaxDb; P37261; -.
DR PRIDE; P37261; -.
DR EnsemblFungi; YCL026C-A_mRNA; YCL026C-A; YCL026C-A.
DR GeneID; 850332; -.
DR KEGG; sce:YCL026C-A; -.
DR SGD; S000000589; FRM2.
DR VEuPathDB; FungiDB:YCL026C-A; -.
DR eggNOG; ENOG502RYI9; Eukaryota.
DR HOGENOM; CLU_073125_1_0_1; -.
DR InParanoid; P37261; -.
DR OMA; LQHYNPM; -.
DR BioCyc; YEAST:G3O-29320-MON; -.
DR PRO; PR:P37261; -.
DR Proteomes; UP000002311; Chromosome III.
DR RNAct; P37261; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0016657; F:oxidoreductase activity, acting on NAD(P)H, nitrogenous group as acceptor; IDA:SGD.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IMP:SGD.
DR CDD; cd02140; Frm2-like; 1.
DR Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR033877; Frm2/Hbn1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR PANTHER; PTHR43035; PTHR43035; 1.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid metabolism; Lipid metabolism; Nucleus;
KW Reference proteome.
FT CHAIN 1..193
FT /note="Fatty acid repression mutant protein 2"
FT /id="PRO_0000087340"
FT HELIX 7..12
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 31..41
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:4URP"
FT TURN 81..86
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 91..99
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 100..109
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 117..139
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:4URP"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 164..173
FT /evidence="ECO:0007829|PDB:4URP"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:4URP"
SQ SEQUENCE 193 AA; 21232 MW; 2F555CE7D9DBCE15 CRC64;
MSPTGNYLNA ITNRRTIYNL KPELPQGVGL DDVKRTVHVI LKNTPTAFNS QVNRAVIIVG
DTHKRIWDAV ASAMPTAEAK KRPESCRDEA YGSVIFFTDE GPTEKLQRDF PALAAAFPTC
AAHTTGAVQI QSWTALELLG LGANLQHYND YVKSALPQDV PIAWTVQSQL VFGVPTALPE
EKTFINNVIN VYH
