ERG29_YEAST
ID ERG29_YEAST Reviewed; 237 AA.
AC P40207; D6VZV7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Ergosterol biosynthesis protein 29 {ECO:0000303|PubMed:23892078};
GN Name=ERG29 {ECO:0000303|PubMed:23892078}; OrderedLocusNames=YMR134W;
GN ORFNames=YM9375.03;
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 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 FUNCTION.
RX PubMed=9180083; DOI=10.1126/science.276.5319.1709;
RA Babcock M., de Silva D., Oaks R., Davis-Kaplan S., Jiralerspong S.,
RA Montermini L., Pandolfo M., Kaplan J.;
RT "Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog
RT of frataxin.";
RL Science 276:1709-1712(1997).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=16135527; DOI=10.1091/mbc.e05-07-0678;
RA Altmann K., Westermann B.;
RT "Role of essential genes in mitochondrial morphogenesis in Saccharomyces
RT cerevisiae.";
RL Mol. Biol. Cell 16:5410-5417(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16630279; DOI=10.1111/j.1567-1364.2005.00007.x;
RA Snoek I.S., Steensma H.Y.;
RT "Why does Kluyveromyces lactis not grow under anaerobic conditions?
RT Comparison of essential anaerobic genes of Saccharomyces cerevisiae with
RT the Kluyveromyces lactis genome.";
RL FEMS Yeast Res. 6:393-403(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23892078; DOI=10.1016/j.febslet.2013.07.024;
RA Moretti-Almeida G., Netto L.E., Monteiro G.;
RT "The essential gene YMR134W from Saccharomyces cerevisiae is important for
RT appropriate mitochondrial iron utilization and the ergosterol biosynthetic
RT pathway.";
RL FEBS Lett. 587:3008-3013(2013).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=29773647; DOI=10.1074/jbc.ra118.001781;
RA Ward D.M., Chen O.S., Li L., Kaplan J., Bhuiyan S.A., Natarajan S.K.,
RA Bard M., Cox J.E.;
RT "Altered sterol metabolism in budding yeast affects mitochondrial iron-
RT sulfur (Fe-S) cluster synthesis.";
RL J. Biol. Chem. 293:10782-10795(2018).
RN [11]
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: Part of the third module of ergosterol biosynthesis pathway
CC that includes the late steps of the pathway (PubMed:23892078). ERG29
CC regulates the activity of the iron-containing C4-methylsterol oxidase
CC ERG25 (PubMed:23892078). The third module or late pathway involves the
CC ergosterol synthesis itself through consecutive reactions that mainly
CC occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene
CC synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate
CC moieties to form squalene, which is the precursor of all steroids.
CC Squalene synthase is crucial for balancing the incorporation of
CC farnesyl diphosphate (FPP) into sterol and nonsterol isoprene
CC synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the
CC stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is
CC considered to be a rate-limiting enzyme in steroid biosynthesis. Then,
CC the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3
CC oxidosqualene to lanosterol, a reaction that forms the sterol core. In
CC the next steps, lanosterol is transformed to zymosterol through a
CC complex process involving various demethylation, reduction and
CC desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also
CC known as CYP51) catalyzes C14-demethylation of lanosterol to produce
CC 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for
CC ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15
CC double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-
CC dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is
CC substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which
CC ERG25 catalyzes the three-step monooxygenation required for the
CC demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes
CC the oxidative decarboxylation that results in a reduction of the 3-
CC beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is
CC responsible for the reduction of the keto group on the C-3. ERG28 has a
CC role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the
CC endoplasmic reticulum and ERG29 regulates the activity of the iron-
CC containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-
CC methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-
CC methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol
CC isomerase ERG2 catalyzes the reaction which results in unsaturation at
CC C-7 in the B ring of sterols and thus converts fecosterol to episterol.
CC The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5
CC double bond in the B ring to produce 5-dehydroepisterol. The C-22
CC sterol desaturase ERG5 further converts 5-dehydroepisterol into
CC ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double
CC bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-
CC 3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce
CC ergosterol (PubMed:32679672). {ECO:0000269|PubMed:23892078,
CC ECO:0000303|PubMed:32679672}.
CC -!- FUNCTION: Plays a role in maintaining mitochondrial and plasma membrane
CC integrity and consequently impacting the iron homeostasis, respiratory
CC metabolism and antioxidant response (PubMed:9180083, PubMed:16135527,
CC PubMed:16630279, PubMed:23892078, PubMed:29773647).
CC {ECO:0000269|PubMed:16135527, ECO:0000269|PubMed:16630279,
CC ECO:0000269|PubMed:23892078, ECO:0000269|PubMed:29773647,
CC ECO:0000269|PubMed:9180083}.
CC -!- INTERACTION:
CC P40207; P46956: PHO86; NbExp=3; IntAct=EBI-27272, EBI-13337;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:29773647}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Causes lethality under aerobic growth conditions
CC (PubMed:16630279, PubMed:29773647). Affects the methyl sterol oxidase
CC reaction performed by the C4-methylsterol monooxygenase ERG25 and leads
CC to an increase in intermediate sterols and a corresponding decrease in
CC zymosterol and ergosterol production (PubMed:29773647). Impairs Fe-S
CC cluster synthesis via increased degradation of YFH1 (PubMed:29773647).
CC Leads to increased mitochondrial oxidants (PubMed:29773647). Leads to
CC an increased accumulation of iron from the culture media
CC (PubMed:23892078). {ECO:0000269|PubMed:16630279,
CC ECO:0000269|PubMed:23892078, ECO:0000269|PubMed:29773647}.
CC -!- MISCELLANEOUS: Present with 2950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z47071; CAA87348.1; -; Genomic_DNA.
DR EMBL; AY558410; AAS56736.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10031.1; -; Genomic_DNA.
DR PIR; S50390; S50390.
DR RefSeq; NP_013853.1; NM_001182635.1.
DR AlphaFoldDB; P40207; -.
DR BioGRID; 35311; 20.
DR DIP; DIP-4433N; -.
DR IntAct; P40207; 2.
DR MINT; P40207; -.
DR STRING; 4932.YMR134W; -.
DR MaxQB; P40207; -.
DR PaxDb; P40207; -.
DR PRIDE; P40207; -.
DR EnsemblFungi; YMR134W_mRNA; YMR134W; YMR134W.
DR GeneID; 855164; -.
DR KEGG; sce:YMR134W; -.
DR SGD; S000004741; ERG29.
DR VEuPathDB; FungiDB:YMR134W; -.
DR eggNOG; ENOG502QRC6; Eukaryota.
DR HOGENOM; CLU_101860_0_0_1; -.
DR InParanoid; P40207; -.
DR OMA; FEDRDKF; -.
DR BioCyc; YEAST:G3O-32827-MON; -.
DR PRO; PR:P40207; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P40207; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; HDA:SGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; IMP:SGD.
DR GO; GO:0006696; P:ergosterol biosynthetic process; IMP:SGD.
DR GO; GO:0007005; P:mitochondrion organization; IMP:SGD.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Reference proteome; Steroid biosynthesis; Steroid metabolism;
KW Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix.
FT CHAIN 1..237
FT /note="Ergosterol biosynthesis protein 29"
FT /id="PRO_0000203302"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 237 AA; 27921 MW; 9DCF3CED15B4A622 CRC64;
MSLKDRYLNL ELKLINKLQE LPYVHQFIHD RISGRITLFL IVVGTLAFFN ELYITIEMSL
LQKNTSEELE RGRIDESLKL HRMLVSDEYH GKEYKDEKSG IVIEEFEDRD KFFAKPVFVS
ELDVECNVIV DGKELLSTPL KFHVEFSPED YENEKRPEFG TTLRVLRLRL YHYFKDCEIY
RDIIKNEGGE GARKFTISNG VKIYNHKDEL LPLNIDDVQL CFLKIDTGNT IKCEFIL
