PGA3_YEAST
ID PGA3_YEAST Reviewed; 312 AA.
AC Q12746; D6W0G0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Plasma membrane-associated coenzyme Q6 reductase PGA3;
DE EC=1.6.2.2;
DE AltName: Full=Processing of GAS1 and ALP protein 3;
GN Name=PGA3; Synonyms=NQR1; OrderedLocusNames=YML125C;
GN ORFNames=YM4987.10C, YM7056.01C;
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 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 [4]
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 [5]
RP FUNCTION.
RX PubMed=16943325; DOI=10.1091/mbc.e06-04-0368;
RA Yu L., Pena Castillo L., Mnaimneh S., Hughes T.R., Brown G.W.;
RT "A survey of essential gene function in the yeast cell division cycle.";
RL Mol. Biol. Cell 17:4736-4747(2006).
RN [6]
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 [7]
RP INDUCTION, SUBCELLULAR LOCATION, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY
RP REGULATION.
RX PubMed=19239415; DOI=10.1111/j.1474-9726.2009.00461.x;
RA Jimenez-Hidalgo M., Santos-Ocana C., Padilla S., Villalba J.M.,
RA Lopez-Lluch G., Martin-Montalvo A., Minor R.K., Sinclair D.A., de Cabo R.,
RA Navas P.;
RT "NQR1 controls lifespan by regulating the promotion of respiratory
RT metabolism in yeast.";
RL Aging Cell 8:140-151(2009).
CC -!- FUNCTION: NADH-dependent cytochrome b5 reductase that reduces coenzyme
CC Q6 at the plasma membrane and mediates lifespan extension by calorie
CC restriction by shifting fermentative to respiratory metabolism,
CC probably through modulating the NAD(+)/NADH ratio.
CC {ECO:0000269|PubMed:16943325, ECO:0000269|PubMed:19239415}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome b5] + NADH = 2 Fe(II)-[cytochrome b5] +
CC H(+) + NAD(+); Xref=Rhea:RHEA:46680, Rhea:RHEA-COMP:10438, Rhea:RHEA-
CC COMP:10439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.6.2.2;
CC Evidence={ECO:0000269|PubMed:19239415};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by diphenylene iodonium (DPI).
CC {ECO:0000269|PubMed:19239415}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Endoplasmic reticulum membrane; Multi-pass membrane protein.
CC -!- INDUCTION: By calorie restriction. {ECO:0000269|PubMed:19239415}.
CC -!- MISCELLANEOUS: Present with 29000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the flavoprotein pyridine nucleotide cytochrome
CC reductase family. {ECO:0000305}.
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DR EMBL; Z49218; CAA89155.1; -; Genomic_DNA.
DR EMBL; Z50178; CAA90558.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09774.1; -; Genomic_DNA.
DR PIR; S54059; S54059.
DR RefSeq; NP_013581.1; NM_001182488.1.
DR AlphaFoldDB; Q12746; -.
DR SMR; Q12746; -.
DR BioGRID; 35080; 311.
DR DIP; DIP-4519N; -.
DR IntAct; Q12746; 2.
DR STRING; 4932.YML125C; -.
DR iPTMnet; Q12746; -.
DR MaxQB; Q12746; -.
DR PaxDb; Q12746; -.
DR PRIDE; Q12746; -.
DR EnsemblFungi; YML125C_mRNA; YML125C; YML125C.
DR GeneID; 854914; -.
DR KEGG; sce:YML125C; -.
DR SGD; S000004594; PGA3.
DR VEuPathDB; FungiDB:YML125C; -.
DR eggNOG; KOG0534; Eukaryota.
DR GeneTree; ENSGT00940000176475; -.
DR HOGENOM; CLU_003827_9_0_1; -.
DR InParanoid; Q12746; -.
DR OMA; HAKERCF; -.
DR BioCyc; YEAST:G3O-32704-MON; -.
DR PRO; PR:Q12746; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q12746; protein.
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:0005886; C:plasma membrane; IDA:SGD.
DR GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IMP:SGD.
DR GO; GO:0015031; P:protein transport; IMP:SGD.
DR Gene3D; 3.40.50.80; -; 1.
DR InterPro; IPR001834; CBR-like.
DR InterPro; IPR008333; Cbr1-like_FAD-bd_dom.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19370; PTHR19370; 1.
DR Pfam; PF00970; FAD_binding_6; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Endoplasmic reticulum; FAD; Flavoprotein; Membrane; NAD;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..312
FT /note="Plasma membrane-associated coenzyme Q6 reductase
FT PGA3"
FT /id="PRO_0000167628"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..179
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 180..200
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 201..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 70..173
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 153..168
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 179..211
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 312 AA; 35287 MW; 84C77D091F2FCA9B CRC64;
MSKEDIEGTN ILDEPVHGIY IPAALFVVGV AITTYMSGEL KILWSLPILF MIIFVRAYSA
YKRRRSLYPD RWTSLELEDQ TIISKNTALY RFKLKTRLES LDIPAGHHVA VRVPIDGKQE
VRYYNPISSK LESGYLDLVV KAYVDGKVSK YFAGLNSGDT VDFKGPIGTL NYEPNSSKHL
GIVAGGSGIT PVLQILNEII TVPEDLTKVS LLYANETEND ILLKDELDEM AEKYPHFQVH
YVVHYPSDRW TGDVGYITKD QMNRYLPEYS EDNRLLICGP DGMNNLALQY AKELGWKVNS
TRSSGDDQVF VF
