CAF20_YEAS7
ID CAF20_YEAS7 Reviewed; 161 AA.
AC A6ZPB3;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 38.
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; ORFNames=SCY_5328;
OS Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=307796;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJM789;
RX PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA Steinmetz L.M.;
RT "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT strain YJM789.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with TIF45. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: Phosphorylated by casein kinase II complex (CK2). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CAF20 family. {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; AAFW02000032; EDN63603.1; -; Genomic_DNA.
DR AlphaFoldDB; A6ZPB3; -.
DR SMR; A6ZPB3; -.
DR PRIDE; A6ZPB3; -.
DR EnsemblFungi; EDN63603; EDN63603; SCY_5328.
DR HOGENOM; CLU_128343_0_0_1; -.
DR Proteomes; UP000007060; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005845; C:mRNA cap binding complex; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR InterPro; IPR031456; Caf20.
DR Pfam; PF17052; CAF20; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Initiation factor; Phosphoprotein; Protein biosynthesis;
KW Protein synthesis inhibitor; Translation regulation.
FT CHAIN 1..161
FT /note="Cap-associated protein CAF20"
FT /id="PRO_0000330092"
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:0000250|UniProtKB:P12962"
FT MOD_RES 91
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12962"
FT MOD_RES 99
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12962"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12962"
FT MOD_RES 102
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12962"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12962"
SQ SEQUENCE 161 AA; 18209 MW; 26BDDAB999198815 CRC64;
MIKYTIDELF QLKPSVTLEV NFDAVEFRAI IEKVKQLQHL KEEEFNSHHV GHFGRRRSSH
HHGRPKIKHN KPKVTTDSDG WCTFEAKKKG SGEDDEEETE TTPTSTVPVA TIAQETLKVK
PNNKNISSNR PADTRDIVAD KPILGFNAFA ALESEDEDDE A
