GCN20_YEAST
ID GCN20_YEAST Reviewed; 752 AA.
AC P43535; D6VTN9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Protein GCN20 {ECO:0000303|PubMed:7621831};
DE AltName: Full=General control non-derepressible protein 20 {ECO:0000312|SGD:S000001905};
GN Name=GCN20 {ECO:0000312|SGD:S000001905}; OrderedLocusNames=YFR009W;
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, INTERACTION WITH GCN1, AND
RP ASSOCIATION WITH RIBOSOMES.
RX PubMed=7621831;
RA Vazquez de Aldana C.R., Marton M.J., Hinnebusch A.G.;
RT "GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex
RT that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-
RT starved cells.";
RL EMBO J. 14:3184-3199(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7670463; DOI=10.1038/ng0795-261;
RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA Eki T.;
RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT cerevisiae.";
RL Nat. Genet. 10:261-268(1995).
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 FUNCTION, INTERACTION WITH GCN1, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=9234705; DOI=10.1128/mcb.17.8.4474;
RA Marton M.J., Vazquez de Aldana C.R., Qiu H., Chakraburtty K.,
RA Hinnebusch A.G.;
RT "Evidence that GCN1 and GCN20, translational regulators of GCN4, function
RT on elongating ribosomes in activation of eIF2alpha kinase GCN2.";
RL Mol. Cell. Biol. 17:4474-4489(1997).
RN [6]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH GCN1 AND GCN2.
RX PubMed=10775272; DOI=10.1093/emboj/19.8.1887;
RA Garcia-Barrio M., Dong J., Ufano S., Hinnebusch A.G.;
RT "Association of GCN1-GCN20 regulatory complex with the N-terminus of
RT eIF2alpha kinase GCN2 is required for GCN2 activation.";
RL EMBO J. 19:1887-1899(2000).
RN [7]
RP INTERACTION WITH GCN1.
RX PubMed=11101534; DOI=10.1093/emboj/19.23.6622;
RA Sattlegger E., Hinnebusch A.G.;
RT "Separate domains in GCN1 for binding protein kinase GCN2 and ribosomes are
RT required for GCN2 activation in amino acid-starved cells.";
RL EMBO J. 19:6622-6633(2000).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10733573; DOI=10.1128/mcb.20.8.2706-2717.2000;
RA Yang R., Wek S.A., Wek R.C.;
RT "Glucose limitation induces GCN4 translation by activation of Gcn2 protein
RT kinase.";
RL Mol. Cell. Biol. 20:2706-2717(2000).
RN [9]
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 [10]
RP FUNCTION, INTERACTION WITH GCN1, AND ASSOCIATION WITH RIBOSOMES.
RX PubMed=15722345; DOI=10.1074/jbc.m414566200;
RA Sattlegger E., Hinnebusch A.G.;
RT "Polyribosome binding by GCN1 is required for full activation of eukaryotic
RT translation initiation factor 2{alpha} kinase GCN2 during amino acid
RT starvation.";
RL J. Biol. Chem. 280:16514-16521(2005).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Acts as a positive activator of the GCN2 protein kinase
CC activity in response to in response to low amino acid, carbon, or
CC purine availability (PubMed:7621831, PubMed:10733573). Component of the
CC GCN1-GCN20 complex that forms a complex with GCN2 on translating
CC ribosomes; during this process, GCN20 helps GCN1 to act as a chaperone
CC to facilitate delivery of uncharged tRNAs that enter the A site of
CC ribosomes to the tRNA-binding domain of GCN2, and hence stimulating
CC GCN2 kinase activity (PubMed:7621831, PubMed:9234705, PubMed:10775272,
CC PubMed:15722345). Participates in gene-specific mRNA translation
CC activation, such as the transcriptional activator GCN4, by promoting
CC the GCN2-mediated phosphorylation of eukaryotic translation initiation
CC factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing GCN4-
CC mediated reprogramming of amino acid biosynthetic gene expression to
CC alleviate nutrient depletion (PubMed:15722345).
CC {ECO:0000269|PubMed:10733573, ECO:0000269|PubMed:10775272,
CC ECO:0000269|PubMed:15722345, ECO:0000269|PubMed:7621831,
CC ECO:0000269|PubMed:9234705}.
CC -!- SUBUNIT: Interacts (via N-terminus) with GCN1 (via C-terminus); this
CC interaction stimulates GCN2 kinase activity in response to amino acid
CC starvation (PubMed:7621831, PubMed:9234705, PubMed:11101534,
CC PubMed:15722345). The GCN1-GCN20 complex interacts with GCN2 on
CC translating ribosomes in amino acid-starved cells; this association
CC stimulates GCN2 kinase activation by uncharged tRNAs, and hence
CC allowing GCN4 translational activation and derepression of amino acid
CC biosynthetic genes (PubMed:7621831, PubMed:9234705, PubMed:10775272,
CC PubMed:11101534). Associates with ribosomes (PubMed:7621831,
CC PubMed:9234705, PubMed:15722345). {ECO:0000269|PubMed:10775272,
CC ECO:0000269|PubMed:11101534, ECO:0000269|PubMed:15722345,
CC ECO:0000269|PubMed:7621831, ECO:0000269|PubMed:9234705}.
CC -!- INTERACTION:
CC P43535; P33892: GCN1; NbExp=3; IntAct=EBI-7423, EBI-7442;
CC -!- DISRUPTION PHENOTYPE: Inhibits GCN4 derepression in amino acid or
CC purine-starved cells (PubMed:10733573). Attenuates GCN4 derepression in
CC glucose-starved cells (PubMed:10733573). {ECO:0000269|PubMed:10733573}.
CC -!- MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC EF3 subfamily. {ECO:0000305}.
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DR EMBL; U19971; AAA75444.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09248.1; -; Genomic_DNA.
DR EMBL; AY723804; AAU09721.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12449.1; -; Genomic_DNA.
DR PIR; S56146; S56146.
DR RefSeq; NP_116664.1; NM_001179974.1.
DR AlphaFoldDB; P43535; -.
DR SMR; P43535; -.
DR BioGRID; 31159; 353.
DR ComplexPortal; CPX-1808; GCN1-GCN20 complex.
DR DIP; DIP-2345N; -.
DR IntAct; P43535; 54.
DR MINT; P43535; -.
DR STRING; 4932.YFR009W; -.
DR iPTMnet; P43535; -.
DR MaxQB; P43535; -.
DR PaxDb; P43535; -.
DR PRIDE; P43535; -.
DR EnsemblFungi; YFR009W_mRNA; YFR009W; YFR009W.
DR GeneID; 850561; -.
DR KEGG; sce:YFR009W; -.
DR SGD; S000001905; GCN20.
DR VEuPathDB; FungiDB:YFR009W; -.
DR eggNOG; KOG0062; Eukaryota.
DR GeneTree; ENSGT00940000155604; -.
DR HOGENOM; CLU_000604_36_6_1; -.
DR InParanoid; P43535; -.
DR OMA; CTHIADI; -.
DR BioCyc; YEAST:G3O-30462-MON; -.
DR PRO; PR:P43535; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43535; protein.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:SGD.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0031369; F:translation initiation factor binding; IPI:UniProtKB.
DR GO; GO:0071232; P:cellular response to histidine; IDA:UniProtKB.
DR GO; GO:0042327; P:positive regulation of phosphorylation; IMP:UniProtKB.
DR GO; GO:0071264; P:positive regulation of translational initiation in response to starvation; IDA:UniProtKB.
DR GO; GO:0006448; P:regulation of translational elongation; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Nucleotide-binding;
KW Reference proteome; Repeat; Stress response; Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..752
FT /note="Protein GCN20"
FT /id="PRO_0000093461"
FT DOMAIN 199..464
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 532..748
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 232..239
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 565..572
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 752 AA; 85027 MW; 486FED10305A572E CRC64;
MASIGSQVRK AASSIDPIVT DYAVGYFNHL SGITFDAVQS KQVDLSTEVQ FVSDLLIDAG
ASKAKVKELS ESILKQLTTQ LKENEAKLEL TGDTSKRLLD INVLKSHNSK SDINVSLSML
GVNGDIEHTG RKMETRVDLK KLAKAEQKIA KKVAKRNNKF VKYEASKLIN DQKEEDYDSF
FLQINPLEFG SSAGKSKDIH IDTFDLYVGD GQRILSNAQL TLSFGHRYGL VGQNGIGKST
LLRALSRREL NVPKHVSILH VEQELRGDDT KALQSVLDAD VWRKQLLSEE AKINERLKEM
DVLRQEFEED SLEVKKLDNE REDLDNHLIQ ISDKLVDMES DKAEARAASI LYGLGFSTEA
QQQPTNSFSG GWRMRLSLAR ALFCQPDLLL LDEPSNMLDV PSIAYLAEYL KTYPNTVLTV
SHDRAFLNEV ATDIIYQHNE RLDYYRGQDF DTFYTTKEER RKNAQREYDN QMVYRKHLQE
FIDKYRYNAA KSQEAQSRIK KLEKLPVLEP PEQDKTIDFK FPECDKLSPP IIQLQDVSFG
YDENNLLLKD VNLDVQMDSR IALVGANGCG KTTLLKIMME QLRPLKGFVS RNPRLRIGYF
TQHHVDSMDL TTSAVDWMSK SFPGKTDEEY RRHLGSFGIT GTLGLQKMQL LSGGQKSRVA
FAALCLNNPH ILVLDEPSNH LDTTGLDALV EALKNFNGGV LMVSHDISVI DSVCKEIWVS
EQGTVKRFEG TIYDYRDYIL QSADAAGVVK KH
