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 07-OCT-2020, entry version 186. DE RecName: Full=Protein GCN20 {ECO:0000305}; 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 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 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 [10] 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 amino acid starvation (PubMed:7621831). CC Component of the GCN1-GCN20 complex that forms a complex with GCN2 on CC translating ribosomes; during this process, GCN20 helps GCN1 to act as CC a chaperone to facilitate delivery of uncharged tRNAs that enter the A CC site of ribosomes to the tRNA-binding domain of GCN2, and hence CC stimulating GCN2 kinase activity (PubMed:7621831, PubMed:9234705, CC PubMed:10775272, PubMed:15722345). Participates in gene-specific mRNA CC translation activation, such as the transcriptional activator GCN4, by CC promoting the GCN2-mediated phosphorylation of eukaryotic translation CC initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52', and hence allowing CC GCN4-mediated reprogramming of amino acid biosynthetic gene expression CC to alleviate nutrient depletion (PubMed:15722345). CC {ECO:0000269|PubMed:10775272, ECO:0000269|PubMed:15722345, CC ECO:0000269|PubMed:7621831, 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 -!- 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 SMR; P43535; -. DR BioGRID; 31159; 343. 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 EuPathDB; FungiDB:YFR009W; -. DR SGD; S000001905; GCN20. DR eggNOG; KOG0062; Eukaryota. DR GeneTree; ENSGT00940000155604; -. DR HOGENOM; CLU_000604_36_6_1; -. DR InParanoid; P43535; -. DR KO; K06158; -. DR OMA; GNYTFWY; -. 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:ATPase 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 InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR032781; ABC_tran_Xtn. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_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:0000244|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 NP_BIND 232..239 FT /note="ATP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT NP_BIND 565..572 FT /note="ATP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000244|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 //