CAF20_YEAST
ID CAF20_YEAST Reviewed; 161 AA.
AC P12962; D6W2X6;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cap-associated protein CAF20;
DE AltName: Full=20 kDa cap-associated protein;
DE AltName: Full=CCR4-associated factor 2;
DE AltName: Full=p20;
GN Name=CAF20; Synonyms=CAF2, CAP20; OrderedLocusNames=YOR276W;
GN ORFNames=O5453W;
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].
RX PubMed=2678000; DOI=10.1093/nar/17.18.7520;
RA Altmann M., Krieger M., Trachsel H.;
RT "Nucleotide sequence of the gene encoding a 20 kDa protein associated with
RT the cap binding protein eIF-4E from Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 17:7520-7520(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8896271;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b%3c1059::aid-yea994%3e3.0.co;2-7;
RA Cheret G., Bernardi A., Sor F.J.;
RT "DNA sequence analysis of the VPH1-SNF2 region on chromosome XV of
RT Saccharomyces cerevisiae.";
RL Yeast 12:1059-1064(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE OF 156-161.
RX PubMed=8265354; DOI=10.1093/nar/21.23.5391;
RA Balakin A.G., Schneider G.S., Corbett M.S., Ni J., Fournier M.J.;
RT "SnR31, snR32, and snR33: three novel, non-essential snRNAs from
RT Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 21:5391-5397(1993).
RN [6]
RP INTERACTION WITH TIF45.
RX PubMed=1400427; DOI=10.1016/s0021-9258(19)36812-7;
RA Lanker S., Mueller P.P., Altmann M., Goyer C., Sonenberg N., Trachsel H.;
RT "Interactions of the eIF-4F subunits in the yeast Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:21167-21171(1992).
RN [7]
RP IDENTIFICATION OF FRAMESHIFT, AND PHOSPHORYLATION.
RX PubMed=7592868; DOI=10.1074/jbc.270.44.26505;
RA Zanchin N.I.T., McCarthy J.E.G.;
RT "Characterization of the in vivo phosphorylation sites of the mRNA.cap-
RT binding complex proteins eukaryotic initiation factor-4E and p20 in
RT Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:26505-26510(1995).
RN [8]
RP FUNCTION, AND INTERACTION WITH TIF45.
RX PubMed=9118949; DOI=10.1093/emboj/16.5.1114;
RA Altmann M., Schmitz N., Berset C., Trachsel H.;
RT "A novel inhibitor of cap-dependent translation initiation in yeast: p20
RT competes with eIF4G for binding to eIF4E.";
RL EMBO J. 16:1114-1121(1997).
RN [9]
RP CHARACTERIZATION.
RX PubMed=9144215; DOI=10.1073/pnas.94.10.5201;
RA de la Cruz J., Iost I., Kressler D., Linder P.;
RT "The p20 and Ded1 proteins have antagonistic roles in eIF4E-dependent
RT translation in Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:5201-5206(1997).
RN [10]
RP FUNCTION, AND INTERACTION WITH TIF45.
RX PubMed=9707439; DOI=10.1093/emboj/17.16.4798;
RA Ptushkina M., von der Haar T., Vasilescu S., Frank R., Birkenhaeger R.,
RA McCarthy J.E.G.;
RT "Cooperative modulation by eIF4G of eIF4E-binding to the mRNA 5' cap in
RT yeast involves a site partially shared by p20.";
RL EMBO J. 17:4798-4808(1998).
RN [11]
RP FUNCTION, AND INTERACTION WITH TIF45.
RX PubMed=10848587; DOI=10.1128/mcb.20.13.4604-4613.2000;
RA Cosentino G.P., Schmelzle T., Haghighat A., Helliwell S.B., Hall M.N.,
RA Sonenberg N.;
RT "Eap1p, a novel eukaryotic translation initiation factor 4E-associated
RT protein in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 20:4604-4613(2000).
RN [12]
RP FUNCTION IN MRNA STABILIZATION.
RX PubMed=12054793; DOI=10.1016/s0022-2836(02)00162-6;
RA Ramirez C.V., Vilela C., Berthelot K., McCarthy J.E.G.;
RT "Modulation of eukaryotic mRNA stability via the cap-binding translation
RT complex eIF4F.";
RL J. Mol. Biol. 318:951-962(2002).
RN [13]
RP FUNCTION, AND INTERACTION WITH TIF45.
RX PubMed=12406227; DOI=10.1046/j.1365-2958.2002.03172.x;
RA von der Haar T., McCarthy J.E.G.;
RT "Intracellular translation initiation factor levels in Saccharomyces
RT cerevisiae and their role in cap-complex function.";
RL Mol. Microbiol. 46:531-544(2002).
RN [14]
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 [15]
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 [16]
RP FUNCTION IN REGULATION OF STE12 TRANSLATION.
RX PubMed=17041186; DOI=10.1128/ec.00121-06;
RA Park Y.-U., Hur H., Ka M., Kim J.;
RT "Identification of translational regulation target genes during filamentous
RT growth in Saccharomyces cerevisiae: regulatory role of Caf20 and Dhh1.";
RL Eukaryot. Cell 5:2120-2127(2006).
RN [17]
RP FUNCTION IN PSEUDOHYPHAL GROWTH, AND MUTAGENESIS OF TYR-4 AND LEU-9.
RX PubMed=17083129; DOI=10.1002/yea.1415;
RA Ibrahimo S., Holmes L.E.A., Ashe M.P.;
RT "Regulation of translation initiation by the yeast eIF4E binding proteins
RT is required for the pseudohyphal response.";
RL Yeast 23:1075-1088(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91 AND THR-102, AND
RP IDENTIFICATION BY 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-91; THR-102 AND SER-154, AND
RP IDENTIFICATION BY 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-91; THR-99; THR-101;
RP THR-102 AND SER-154, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Acts as an inhibitor of cap-dependent translation. Competes
CC with eIF4G1/TIF4631 and EAP1 for binding to eIF4E/TIF45 and interferes
CC with the formation of the eIF4F complex, inhibiting translation and
CC stabilizing mRNA. Binding affinity for eIF4E/TIF45 is 10-fold less than
CC that of eIF4G1/TIF4631. Required for induction of pseudohyphal growth
CC in response to nitrogen limitation, probably by regulating STE12
CC translation. {ECO:0000269|PubMed:10848587, ECO:0000269|PubMed:12054793,
CC ECO:0000269|PubMed:12406227, ECO:0000269|PubMed:17041186,
CC ECO:0000269|PubMed:17083129, ECO:0000269|PubMed:9118949,
CC ECO:0000269|PubMed:9707439}.
CC -!- SUBUNIT: Interacts with TIF45. {ECO:0000269|PubMed:10848587,
CC ECO:0000269|PubMed:12406227, ECO:0000269|PubMed:1400427,
CC ECO:0000269|PubMed:9118949, ECO:0000269|PubMed:9707439}.
CC -!- INTERACTION:
CC P12962; P07260: CDC33; NbExp=7; IntAct=EBI-9010, EBI-150;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- PTM: Phosphorylated by casein kinase II complex (CK2).
CC {ECO:0000269|PubMed:7592868}.
CC -!- MISCELLANEOUS: Present with 26900 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CAF20 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16544.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=CAA33752.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X15731; CAA33752.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X89633; CAA61782.1; -; Genomic_DNA.
DR EMBL; Z75184; CAA99501.1; -; Genomic_DNA.
DR EMBL; L22433; AAA16544.1; ALT_SEQ; Unassigned_DNA.
DR EMBL; BK006948; DAA11042.1; -; Genomic_DNA.
DR PIR; S67178; S67178.
DR RefSeq; NP_014919.3; NM_001183695.3.
DR PDB; 6FC3; X-ray; 1.75 A; B=1-49.
DR PDBsum; 6FC3; -.
DR AlphaFoldDB; P12962; -.
DR SMR; P12962; -.
DR BioGRID; 34665; 1077.
DR DIP; DIP-1222N; -.
DR ELM; P12962; -.
DR IntAct; P12962; 25.
DR MINT; P12962; -.
DR STRING; 4932.YOR276W; -.
DR iPTMnet; P12962; -.
DR MaxQB; P12962; -.
DR PaxDb; P12962; -.
DR PRIDE; P12962; -.
DR EnsemblFungi; YOR276W_mRNA; YOR276W; YOR276W.
DR GeneID; 854450; -.
DR KEGG; sce:YOR276W; -.
DR SGD; S000005802; CAF20.
DR VEuPathDB; FungiDB:YOR276W; -.
DR eggNOG; ENOG502S2E7; Eukaryota.
DR HOGENOM; CLU_128343_0_0_1; -.
DR InParanoid; P12962; -.
DR OMA; GHFNRRR; -.
DR BioCyc; YEAST:G3O-33765-MON; -.
DR PRO; PR:P12962; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P12962; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005845; C:mRNA cap binding complex; IEA:InterPro.
DR GO; GO:0008190; F:eukaryotic initiation factor 4E binding; IDA:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:SGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR InterPro; IPR031456; Caf20.
DR Pfam; PF17052; CAF20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Protein synthesis inhibitor; Reference proteome;
KW Translation regulation.
FT CHAIN 1..161
FT /note="Cap-associated protein CAF20"
FT /id="PRO_0000084163"
FT REGION 52..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..69
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MUTAGEN 4
FT /note="Y->A: Reduces interaction with eIF4E/TIF45. Prevents
FT pseudohyphal growth. Further reduces interaction with
FT eIF4E/TIF45; when associated with A-9."
FT /evidence="ECO:0000269|PubMed:17083129"
FT MUTAGEN 9
FT /note="L->A: Further reduces interaction with eIF4E/TIF45;
FT when associated with A-4."
FT /evidence="ECO:0000269|PubMed:17083129"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:6FC3"
FT HELIX 24..41
FT /evidence="ECO:0007829|PDB:6FC3"
SQ SEQUENCE 161 AA; 18223 MW; 870CA17343798805 CRC64;
MIKYTIDELF QLKPSLTLEV NFDAVEFRAI IEKVKQLQHL KEEEFNSHHV GHFGRRRSSH
HHGRPKIKHN KPKVTTDSDG WCTFEAKKKG SGEDDEEETE TTPTSTVPVA TIAQETLKVK
PNNKNISSNR PADTRDIVAD KPILGFNAFA ALESEDEDDE A
