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P31384 (CCR4_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glucose-repressible alcohol dehydrogenase transcriptional effector

EC=3.1.13.4
Alternative name(s):
Carbon catabolite repressor protein 4
Cytoplasmic deadenylase
Gene names
Name:CCR4
Ordered Locus Names:YAL021C
ORF Names:FUN27
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts as catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. CCR4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also low exonuclease activity towards single-stranded DNA. Discovered because of its role in the control of ADH2 gene expression. It is required for the expression of genes involved in non-fermentative growth and it mediates or is required for the action of the SPT6 and SPT10 genes. Ref.6 Ref.8 Ref.10 Ref.11

Catalytic activity

Exonucleolytic cleavage of poly(A) to 5'-AMP.

Cofactor

Magnesium.

Subunit structure

Subunit of the 1.0 MDa CCR4-NOT core complex that contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In the complex interacts with NOT1. The core complex probably is part of a less characterized 1.9 MDa CCR4-NOT complex. Ref.6 Ref.7 Ref.9

Subcellular location

Cytoplasm. Nucleus Ref.8.

Domain

The 169 C-terminal residues are important for deadenylase activity.

Miscellaneous

Present with 2780 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the CCR4/nocturin family.

Contains 5 LRR (leucine-rich) repeats.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainLeucine-rich repeat
Repeat
   LigandMagnesium
Metal-binding
RNA-binding
   Molecular functionActivator
Exonuclease
Hydrolase
Nuclease
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from genetic interaction PubMed 17158920. Source: SGD

DNA replication checkpoint

Inferred from genetic interaction PubMed 17158920. Source: SGD

RNA phosphodiester bond hydrolysis, exonucleolytic

Inferred from direct assay Ref.11. Source: GOC

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Inferred from direct assay Ref.11. Source: SGD

nuclear-transcribed mRNA poly(A) tail shortening

Inferred from direct assay Ref.11. Source: SGD

positive regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay PubMed 21406554. Source: SGD

regulation of transcription from RNA polymerase II promoter

Inferred from physical interaction Ref.7. Source: SGD

replication fork protection

Inferred from genetic interaction PubMed 17158920. Source: SGD

transcription elongation from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 11404327. Source: SGD

traversing start control point of mitotic cell cycle

Inferred from mutant phenotype PubMed 15075273. Source: SGD

   Cellular_componentCCR4-NOT core complex

Inferred from physical interaction Ref.7. Source: SGD

cytoplasm

Inferred from direct assay Ref.11. Source: SGD

cytoplasmic mRNA processing body

Inferred from direct assay PubMed 18611963. Source: SGD

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3'-5'-exoribonuclease activity

Inferred from direct assay Ref.11. Source: SGD

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A)-specific ribonuclease activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 837837Glucose-repressible alcohol dehydrogenase transcriptional effector
PRO_0000218577

Regions

Repeat334 – 35623LRR 1
Repeat358 – 37922LRR 2
Repeat381 – 40222LRR 3
Repeat404 – 42623LRR 4
Repeat427 – 44721LRR 5
Compositional bias15 – 2410Poly-Gln
Compositional bias77 – 10327Asn-rich
Compositional bias89 – 10315Poly-Asn
Compositional bias190 – 20617Gln-rich

Sites

Metal binding5561Magnesium

Amino acid modifications

Modified residue331Phosphothreonine Ref.15
Modified residue2781Phosphoserine Ref.14 Ref.15
Modified residue2851Phosphothreonine Ref.13 Ref.15

Experimental info

Mutagenesis5561E → A: Loss of activity. Ref.10
Mutagenesis7131D → A: Strongly reduces activity. Ref.10
Mutagenesis7801D → A: Reduces activity. Ref.10
Mutagenesis8181H → A: Loss of activity. Ref.10
Sequence conflict5441I → L in AAB24455. Ref.1
Sequence conflict8031V → E in AAB24455. Ref.1

Secondary structure

.............................................. 837
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31384 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: 5CDB2E8FEDDBEF6F

FASTA83794,670
        10         20         30         40         50         60 
MNDPSLLGYP NVGPQQQQQQ QQQQHAGLLG KGTPNALQQQ LHMNQLTGIP PPGLMNNSDV 

        70         80         90        100        110        120 
HTSSNNNSRQ LLDQLANGNA NMLNMNMDNN NNNNNNNNNN NNNGGGSGVM MNASTAAVNS 

       130        140        150        160        170        180 
IGMVPTVGTP VNINVNASNP LLHPHLDDPS LLNNPIWKLQ LHLAAVSAQS LGQPNIYARQ 

       190        200        210        220        230        240 
NAMKKYLATQ QAQQAQQQAQ QQAQQQVPGP FGPGPQAAPP ALQPTDFQQS HIAEASKSLV 

       250        260        270        280        290        300 
DCTKQALMEM ADTLTDSKTA KKQQPTGDST PSGTATNSAV STPLTPKIEL FANGKDEANQ 

       310        320        330        340        350        360 
ALLQHKKLSQ YSIDEDDDIE NRMVMPKDSK YDDQLWHALD LSNLQIFNIS ANIFKYDFLT 

       370        380        390        400        410        420 
RLYLNGNSLT ELPAEIKNLS NLRVLDLSHN RLTSLPAELG SCFQLKYFYF FDNMVTTLPW 

       430        440        450        460        470        480 
EFGNLCNLQF LGVEGNPLEK QFLKILTEKS VTGLIFYLRD NRPEIPLPHE RRFIEINTDG 

       490        500        510        520        530        540 
EPQREYDSLQ QSTEHLATDL AKRTFTVLSY NTLCQHYATP KMYRYTPSWA LSWDYRRNKL 

       550        560        570        580        590        600 
KEQILSYDSD LLCLQEVESK TFEEYWVPLL DKHGYTGIFH AKARAKTMHS KDSKKVDGCC 

       610        620        630        640        650        660 
IFFKRDQFKL ITKDAMDFSG AWMKHKKFQR TEDYLNRAMN KDNVALFLKL QHIPSGDTIW 

       670        680        690        700        710        720 
AVTTHLHWDP KFNDVKTFQV GVLLDHLETL LKEETSHNFR QDIKKFPVLI CGDFNSYINS 

       730        740        750        760        770        780 
AVYELINTGR VQIHQEGNGR DFGYMSEKNF SHNLALKSSY NCIGELPFTN FTPSFTDVID 

       790        800        810        820        830 
YIWFSTHALR VRGLLGEVDP EYVSKFIGFP NDKFPSDHIP LLARFEFMKT NTGSKKV 

« Hide

References

« Hide 'large scale' references
[1]"The CCR4 protein from Saccharomyces cerevisiae contains a leucine-rich repeat region which is required for its control of ADH2 gene expression."
Malvar T., Biron R.W., Kaback D.B., Denis C.L.
Genetics 132:951-962(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequencing of chromosome I from Saccharomyces cerevisiae: analysis of a 32 kb region between the LTE1 and SPO7 genes."
Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.-W., Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.
Genome 36:32-42(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]"Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: analysis of the genes in the FUN38-MAK16-SPO7 region."
Barton A.B., Kaback D.B.
J. Bacteriol. 176:1872-1880(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[4]"The nucleotide sequence of chromosome I from Saccharomyces cerevisiae."
Bussey H., Kaback D.B., Zhong W.-W., Vo D.H., Clark M.W., Fortin N., Hall J., Ouellette B.F.F., Keng T., Barton A.B., Su Y., Davies C.J., Storms R.K.
Proc. Natl. Acad. Sci. U.S.A. 92:3809-3813(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[6]"The NOT proteins are part of the CCR4 transcriptional complex and affect gene expression both positively and negatively."
Liu H.Y., Badarinarayana V., Audino D.C., Rappsilber J., Mann M., Denis C.L.
EMBO J. 17:1096-1106(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, FUNCTION OF THE CCR4-NOT CORE COMPLEX IN TRANSCRIPTIONAL REGULATION.
[7]"The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and functionally separated from NOT2, NOT4, and NOT5."
Bai Y., Salvadore C., Chiang Y.C., Collart M.A., Liu H.Y., Denis C.L.
Mol. Cell. Biol. 19:6642-6651(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOT1.
[8]"The transcription factor associated Ccr4 and Caf1 proteins are components of the major cytoplasmic mRNA deadenylase in Saccharomyces cerevisiae."
Tucker M., Valencia-Sanchez M.A., Staples R.R., Chen J., Denis C.L., Parker R.
Cell 104:377-386(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEADENYLATION, SUBCELLULAR LOCATION.
[9]"Purification and characterization of the 1.0 MDa CCR4-NOT complex identifies two novel components of the complex."
Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.
J. Mol. Biol. 314:683-694(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX.
[10]"CCR4, a 3'-5' poly(A) RNA and ssDNA exonuclease, is the catalytic component of the cytoplasmic deadenylase."
Chen J., Chiang Y.-C., Denis C.L.
EMBO J. 21:1414-1426(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEADENYLATION, MUTAGENESIS OF GLU-556; ASP-713; ASP-780 AND HIS-818.
[11]"Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae."
Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.
EMBO J. 21:1427-1436(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MRNA DEADENYLATION.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[14]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-33; SER-278 AND THR-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S50459 Genomic DNA. Translation: AAB24455.1.
L05146 Genomic DNA. Translation: AAC04936.1.
BK006935 Genomic DNA. Translation: DAA06967.1.
PIRS36713.
RefSeqNP_009381.1. NM_001178166.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4B8CX-ray3.41D/J/K/L111-837[»]
ProteinModelPortalP31384.
SMRP31384. Positions 135-192, 287-827.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid31745. 281 interactions.
DIPDIP-2522N.
IntActP31384. 31 interactions.
MINTMINT-615079.
STRING4932.YAL021C.

Proteomic databases

PaxDbP31384.
PeptideAtlasP31384.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYAL021C; YAL021C; YAL021C.
GeneID851212.
KEGGsce:YAL021C.

Organism-specific databases

SGDS000000019. CCR4.

Phylogenomic databases

eggNOGCOG4886.
GeneTreeENSGT00550000074364.
HOGENOMHOG000294222.
KOK12603.
OMAFEYNSVC.
OrthoDBEOG7KWSS5.

Enzyme and pathway databases

BioCycYEAST:G3O-28833-MONOMER.

Gene expression databases

GenevestigatorP31384.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
PF12799. LRR_4. 1 hit.
[Graphical view]
SMARTSM00369. LRR_TYP. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
PROSITEPS51450. LRR. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio968091.
PROP31384.

Entry information

Entry nameCCR4_YEAST
AccessionPrimary (citable) accession number: P31384
Secondary accession number(s): D6VPJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome I

Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references