HMDH2_YEAST
ID HMDH2_YEAST Reviewed; 1045 AA.
AC P12684; D6VZ84; E9P8X3;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase 2 {ECO:0000303|PubMed:3526336};
DE Short=HMG-CoA reductase 2 {ECO:0000303|PubMed:3526336};
DE EC=1.1.1.34 {ECO:0000269|PubMed:3526336};
GN Name=HMG2 {ECO:0000303|PubMed:3526336}; OrderedLocusNames=YLR450W;
GN ORFNames=L9324.2;
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 PATHWAY.
RX PubMed=3065625; DOI=10.1128/mcb.8.9.3797-3808.1988;
RA Basson M.E., Thorsness M., Finer-Moore J., Stroud R.M., Rine J.;
RT "Structural and functional conservation between yeast and human 3-hydroxy-
RT 3-methylglutaryl coenzyme A reductases, the rate-limiting enzyme of sterol
RT biosynthesis.";
RL Mol. Cell. Biol. 8:3797-3808(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 772-961, FUNCTION, CATALYTIC ACTIVITY,
RP DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=3526336; DOI=10.1073/pnas.83.15.5563;
RA Basson M.E., Thorsness M., Rine J.;
RT "Saccharomyces cerevisiae contains two functional genes encoding 3-hydroxy-
RT 3-methylglutaryl-coenzyme A reductase.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:5563-5567(1986).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=8744950; DOI=10.1091/mbc.7.5.769;
RA Koning A.J., Roberts C.J., Wright R.L.;
RT "Different subcellular localization of Saccharomyces cerevisiae HMG-CoA
RT reductase isozymes at elevated levels corresponds to distinct endoplasmic
RT reticulum membrane proliferations.";
RL Mol. Biol. Cell 7:769-789(1996).
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 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 [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-565, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-565, AND IDENTIFICATION BY
RP 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 [12]
RP DOMAIN, ENZYME STABILITY, AND MUTAGENESIS OF ASP-188; ILE-191; ILE-192;
RP 202-THR--CYS-205; SER-215; PHE-217; LEU-219; LEU-231; PRO-256; PHE-257;
RP ILE-262; LEU-328; ASP-342; LEU-345; TYR-350; LEU-354 AND GLU-359.
RX PubMed=21628456; DOI=10.1074/jbc.m111.244798;
RA Theesfeld C.L., Pourmand D., Davis T., Garza R.M., Hampton R.Y.;
RT "The sterol-sensing domain (SSD) directly mediates signal-regulated
RT endoplasmic reticulum-associated degradation (ERAD) of 3-hydroxy-3-
RT methylglutaryl (HMG)-CoA reductase isozyme Hmg2.";
RL J. Biol. Chem. 286:26298-26307(2011).
RN [13]
RP REVIEW ON ERGOSTEROL BIOSYNTHESIS.
RX PubMed=32679672; DOI=10.3390/genes11070795;
RA Jorda T., Puig S.;
RT "Regulation of ergosterol biosynthesis in Saccharomyces cerevisiae.";
RL Genes (Basel) 11:0-0(2020).
CC -!- FUNCTION: HMG-CoA reductase; part of the first module of ergosterol
CC biosynthesis pathway constitutes by the early steps of the pathway,
CC conserved across all eukaryotes, and which results in the formation of
CC mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:3065625,
CC PubMed:3526336). HMG1 and HMG2 catalyze the reduction of
CC hydroxymethylglutaryl-CoA (HMG-CoA) to mevalonate that is the rate-
CC limiting step within the first mosule (PubMed:3526336). The first
CC module starts with the action of the cytosolic acetyl-CoA
CC acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-
CC CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses
CC acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step
CC of the early module is the reduction to mevalonate by the 3-hydroxy-3-
CC methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are
CC derived from a single ancestral HMGR gene by gene duplication
CC (PubMed:32679672). {ECO:0000269|PubMed:3065625,
CC ECO:0000269|PubMed:3526336, ECO:0000303|PubMed:32679672}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-
CC methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10003,
CC ECO:0000269|PubMed:3526336};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:15991;
CC Evidence={ECO:0000269|PubMed:3526336};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate
CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3.
CC {ECO:0000269|PubMed:3065625, ECO:0000269|PubMed:3526336}.
CC -!- INTERACTION:
CC P12684; P12683: HMG1; NbExp=5; IntAct=EBI-8384, EBI-8377;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8744950}; Multi-pass
CC membrane protein {ECO:0000255}. Nucleus envelope
CC {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The sterol-sensing domain (SSD) is required for sterol pathway
CC signals to stimulate hmg2 ER-associated degradation and detects both
CC geranylgeranyl pyrophosphate and a secondary oxysterol signal.
CC {ECO:0000269|PubMed:21628456}.
CC -!- DISRUPTION PHENOTYPE: When both HMG1 and HMG2 are deleted, cells are
CC unable to undergo spore germination and vegetative growth.
CC {ECO:0000269|PubMed:3526336}.
CC -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. {ECO:0000305}.
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DR EMBL; M22255; AAA34677.1; -; Genomic_DNA.
DR EMBL; U22382; AAB67527.1; -; Genomic_DNA.
DR EMBL; AY692800; AAT92819.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09750.1; -; Genomic_DNA.
DR PIR; B30239; B30239.
DR RefSeq; NP_013555.1; NM_001182338.1.
DR AlphaFoldDB; P12684; -.
DR SMR; P12684; -.
DR BioGRID; 31708; 133.
DR DIP; DIP-6277N; -.
DR IntAct; P12684; 33.
DR MINT; P12684; -.
DR STRING; 4932.YLR450W; -.
DR iPTMnet; P12684; -.
DR MaxQB; P12684; -.
DR PaxDb; P12684; -.
DR PRIDE; P12684; -.
DR EnsemblFungi; YLR450W_mRNA; YLR450W; YLR450W.
DR GeneID; 851171; -.
DR KEGG; sce:YLR450W; -.
DR SGD; S000004442; HMG2.
DR VEuPathDB; FungiDB:YLR450W; -.
DR eggNOG; KOG2480; Eukaryota.
DR GeneTree; ENSGT00940000155305; -.
DR HOGENOM; CLU_001734_0_0_1; -.
DR InParanoid; P12684; -.
DR OMA; WPRADGK; -.
DR BioCyc; MetaCyc:YLR450W-MON; -.
DR BioCyc; YEAST:YLR450W-MON; -.
DR UniPathway; UPA00058; UER00103.
DR PRO; PR:P12684; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; P12684; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IDA:SGD.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005778; C:peroxisomal membrane; IBA:GO_Central.
DR GO; GO:0000502; C:proteasome complex; IPI:SGD.
DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IGI:SGD.
DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro.
DR GO; GO:0006696; P:ergosterol biosynthetic process; ISA:SGD.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central.
DR CDD; cd00643; HMG-CoA_reductase_classI; 1.
DR Gene3D; 1.10.3270.10; -; 1.
DR Gene3D; 3.30.70.420; -; 1.
DR Gene3D; 3.90.770.10; -; 1.
DR InterPro; IPR025583; HMG-CoA_N_dom.
DR InterPro; IPR002202; HMG_CoA_Rdtase.
DR InterPro; IPR023074; HMG_CoA_Rdtase_cat_sf.
DR InterPro; IPR023076; HMG_CoA_Rdtase_CS.
DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc.
DR InterPro; IPR023282; HMG_CoA_Rdtase_N.
DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_sf.
DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom_sf.
DR InterPro; IPR000731; SSD.
DR PANTHER; PTHR10572; PTHR10572; 1.
DR Pfam; PF00368; HMG-CoA_red; 1.
DR Pfam; PF13323; HPIH; 1.
DR Pfam; PF12349; Sterol-sensing; 1.
DR PRINTS; PR00071; HMGCOARDTASE.
DR SUPFAM; SSF55035; SSF55035; 1.
DR SUPFAM; SSF56542; SSF56542; 1.
DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1.
DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1.
DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1.
DR PROSITE; PS01192; HMG_COA_REDUCTASE_3; 1.
DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1.
DR PROSITE; PS50156; SSD; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Membrane; NADP; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..1045
FT /note="3-hydroxy-3-methylglutaryl-coenzyme A reductase 2"
FT /id="PRO_0000114457"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..186
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..243
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 244..264
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 265..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..324
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 346..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..497
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:16847258"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..1045
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:16847258"
FT DOMAIN 188..356
FT /note="SSD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00199"
FT REGION 1018..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1038
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 710
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 844
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 920
FT /note="Charge relay system"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT ACT_SITE 1016
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10003"
FT BINDING 716..722
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT BINDING 777..779
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT BINDING 804..812
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT BINDING 873..875
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT BINDING 1015..1016
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT BINDING 1020..1021
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P04035"
FT MOD_RES 565
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 188
FT /note="D->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 191
FT /note="I->A: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 192
FT /note="I->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 202..205
FT /note="TLCC->AAAA: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 215
FT /note="S->A,T: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 217
FT /note="F->L: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 219
FT /note="L->F: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 231
FT /note="L->A: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 256
FT /note="P->A: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 257
FT /note="F->L: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 262
FT /note="I->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 328
FT /note="L->A: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 342
FT /note="D->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 345
FT /note="L->A: Leads to normal response to the FPP-derived
FT signal but no response to the oxysterol signal."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 350
FT /note="Y->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 354
FT /note="L->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT MUTAGEN 359
FT /note="E->A: Leads to increased stability and reduced
FT response to degradation signals."
FT /evidence="ECO:0000269|PubMed:21628456"
FT CONFLICT 29
FT /note="V -> A (in Ref. 4; AAT92819)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 115692 MW; 1FD9DCD3AC01B15E CRC64;
MSLPLKTIVH LVKPFACTAR FSARYPIHVI VVAVLLSAAA YLSVTQSYLN EWKLDSNQYS
TYLSIKPDEL FEKCTHYYRS PVSDTWKLLS SKEAADIYTP FHYYLSTISF QSKDNSTTLP
SLDDVIYSVD HTRYLLSEEP KIPTELVSEN GTKWRLRNNS NFILDLHNIY RNMVKQFSNK
TSEFDQFDLF IILAAYLTLF YTLCCLFNDM RKIGSKFWLS FSALSNSACA LYLSLYTTHS
LLKKPASLLS LVIGLPFIVV IIGFKHKVRL AAFSLQKFHR ISIDKKITVS NIIYEAMFQE
GAYLIRDYLF YISSFIGCAI YARHLPGLVN FCILSTFMLV FDLLLSATFY SAILSMKLEI
NIIHRSTVIR QTLEEDGVVP TTADIIYKDE TASEPHFLRS NVAIILGKAS VIGLLLLINL
YVFTDKLNAT ILNTVYFDST IYSLPNFINY KDIGNLSNQV IISVLPKQYY TPLKKYHQIE
DSVLLIIDSV SNAIRDQFIS KLLFFAFAVS ISINVYLLNA AKIHTGYMNF QPQSNKIDDL
VVQQKSATIE FSETRSMPAS SGLETPVTAK DIIISEEIQN NECVYALSSQ DEPIRPLSNL
VELMEKEQLK NMNNTEVSNL VVNGKLPLYS LEKKLEDTTR AVLVRRKALS TLAESPILVS
EKLPFRNYDY DRVFGACCEN VIGYMPIPVG VIGPLIIDGT SYHIPMATTE GCLVASAMRG
CKAINAGGGA TTVLTKDGMT RGPVVRFPTL IRSGACKIWL DSEEGQNSIK KAFNSTSRFA
RLQHIQTCLA GDLLFMRFRT TTGDAMGMNM ISKGVEYSLK QMVEEYGWED MEVVSVSGNY
CTDKKPAAIN WIEGRGKSVV AEATIPGDVV KSVLKSDVSA LVELNISKNL VGSAMAGSVG
GFNAHAANLV TALFLALGQD PAQNVESSNC ITLMKEVDGD LRISVSMPSI EVGTIGGGTV
LEPQGAMLDL LGVRGPHPTE PGANARQLAR IIACAVLAGE LSLCSALAAG HLVQSHMTHN
RKTNKANELP QPSNKGPPCK TSALL
