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Protein

Glucose-repressible alcohol dehydrogenase transcriptional effector

Gene

CCR4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

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

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi556Magnesium1

GO - Molecular functioni

GO - Biological processi

  • DNA replication Source: SGD
  • DNA replication checkpoint Source: SGD
  • nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: SGD
  • nuclear-transcribed mRNA poly(A) tail shortening Source: SGD
  • positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  • regulation of transcription from RNA polymerase II promoter Source: SGD
  • replication fork protection Source: SGD
  • transcription elongation from RNA polymerase II promoter Source: SGD
  • traversing start control point of mitotic cell cycle Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Activator, Exonuclease, Hydrolase, Nuclease, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28833-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glucose-repressible alcohol dehydrogenase transcriptional effector (EC:3.1.13.4)
Alternative name(s):
Carbon catabolite repressor protein 4
Cytoplasmic deadenylase
Gene namesi
Name:CCR4
Ordered Locus Names:YAL021C
ORF Names:FUN27
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:YAL021C.
SGDiS000000019. CCR4.

Subcellular locationi

GO - Cellular componenti

  • CCR4-NOT core complex Source: SGD
  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi556E → A: Loss of activity. 1 Publication1
Mutagenesisi713D → A: Strongly reduces activity. 1 Publication1
Mutagenesisi780D → A: Reduces activity. 1 Publication1
Mutagenesisi818H → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002185771 – 837Glucose-repressible alcohol dehydrogenase transcriptional effectorAdd BLAST837

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei33PhosphothreonineCombined sources1
Modified residuei278PhosphoserineCombined sources1
Modified residuei285PhosphothreonineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP31384.
PRIDEiP31384.
TopDownProteomicsiP31384.

PTM databases

iPTMnetiP31384.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAF40P538298EBI-4396,EBI-28306
CDC39P256557EBI-4396,EBI-12139
MOT2P349094EBI-4396,EBI-12174
POP2P390089EBI-4396,EBI-13629

Protein-protein interaction databases

BioGridi31745. 285 interactors.
DIPiDIP-2522N.
IntActiP31384. 31 interactors.
MINTiMINT-615079.

Structurei

Secondary structure

1837
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni140 – 142Combined sources3
Helixi144 – 146Combined sources3
Helixi155 – 169Combined sources15
Helixi176 – 186Combined sources11
Helixi245 – 258Combined sources14
Beta strandi338 – 340Combined sources3
Helixi351 – 355Combined sources5
Helixi374 – 379Combined sources6
Beta strandi384 – 386Combined sources3
Helixi399 – 402Combined sources4
Beta strandi406 – 409Combined sources4
Helixi441 – 460Combined sources20
Helixi515 – 517Combined sources3
Turni520 – 522Combined sources3
Helixi528 – 531Combined sources4
Helixi533 – 546Combined sources14
Beta strandi550 – 554Combined sources5
Helixi559 – 563Combined sources5
Turni564 – 566Combined sources3
Beta strandi600 – 602Combined sources3
Helixi800 – 803Combined sources4
Beta strandi807 – 811Combined sources5
Beta strandi816 – 818Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B8CX-ray3.41D/J/K/L111-837[»]
ProteinModelPortaliP31384.
SMRiP31384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati334 – 356LRR 1Add BLAST23
Repeati358 – 379LRR 2Add BLAST22
Repeati381 – 402LRR 3Add BLAST22
Repeati404 – 426LRR 4Add BLAST23
Repeati427 – 447LRR 5Add BLAST21

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi15 – 24Poly-Gln10
Compositional biasi77 – 103Asn-richAdd BLAST27
Compositional biasi89 – 103Poly-AsnAdd BLAST15
Compositional biasi190 – 206Gln-richAdd BLAST17

Domaini

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

Sequence similaritiesi

Belongs to the CCR4/nocturin family.Curated
Contains 5 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

GeneTreeiENSGT00550000074364.
HOGENOMiHOG000294222.
InParanoidiP31384.
KOiK12603.
OMAiCTKQALM.
OrthoDBiEOG092C0WZC.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS51450. LRR. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31384-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNDPSLLGYP NVGPQQQQQQ QQQQHAGLLG KGTPNALQQQ LHMNQLTGIP
60 70 80 90 100
PPGLMNNSDV HTSSNNNSRQ LLDQLANGNA NMLNMNMDNN NNNNNNNNNN
110 120 130 140 150
NNNGGGSGVM MNASTAAVNS IGMVPTVGTP VNINVNASNP LLHPHLDDPS
160 170 180 190 200
LLNNPIWKLQ LHLAAVSAQS LGQPNIYARQ NAMKKYLATQ QAQQAQQQAQ
210 220 230 240 250
QQAQQQVPGP FGPGPQAAPP ALQPTDFQQS HIAEASKSLV DCTKQALMEM
260 270 280 290 300
ADTLTDSKTA KKQQPTGDST PSGTATNSAV STPLTPKIEL FANGKDEANQ
310 320 330 340 350
ALLQHKKLSQ YSIDEDDDIE NRMVMPKDSK YDDQLWHALD LSNLQIFNIS
360 370 380 390 400
ANIFKYDFLT RLYLNGNSLT ELPAEIKNLS NLRVLDLSHN RLTSLPAELG
410 420 430 440 450
SCFQLKYFYF FDNMVTTLPW EFGNLCNLQF LGVEGNPLEK QFLKILTEKS
460 470 480 490 500
VTGLIFYLRD NRPEIPLPHE RRFIEINTDG EPQREYDSLQ QSTEHLATDL
510 520 530 540 550
AKRTFTVLSY NTLCQHYATP KMYRYTPSWA LSWDYRRNKL KEQILSYDSD
560 570 580 590 600
LLCLQEVESK TFEEYWVPLL DKHGYTGIFH AKARAKTMHS KDSKKVDGCC
610 620 630 640 650
IFFKRDQFKL ITKDAMDFSG AWMKHKKFQR TEDYLNRAMN KDNVALFLKL
660 670 680 690 700
QHIPSGDTIW AVTTHLHWDP KFNDVKTFQV GVLLDHLETL LKEETSHNFR
710 720 730 740 750
QDIKKFPVLI CGDFNSYINS AVYELINTGR VQIHQEGNGR DFGYMSEKNF
760 770 780 790 800
SHNLALKSSY NCIGELPFTN FTPSFTDVID YIWFSTHALR VRGLLGEVDP
810 820 830
EYVSKFIGFP NDKFPSDHIP LLARFEFMKT NTGSKKV
Length:837
Mass (Da):94,670
Last modified:October 5, 2010 - v2
Checksum:i5CDB2E8FEDDBEF6F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti544I → L in AAB24455 (PubMed:1459446).Curated1
Sequence conflicti803V → E in AAB24455 (PubMed:1459446).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50459 Genomic DNA. Translation: AAB24455.1.
L05146 Genomic DNA. Translation: AAC04936.1.
BK006935 Genomic DNA. Translation: DAA06967.1.
PIRiS36713.
RefSeqiNP_009381.1. NM_001178166.1.

Genome annotation databases

EnsemblFungiiYAL021C; YAL021C; YAL021C.
GeneIDi851212.
KEGGisce:YAL021C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S50459 Genomic DNA. Translation: AAB24455.1.
L05146 Genomic DNA. Translation: AAC04936.1.
BK006935 Genomic DNA. Translation: DAA06967.1.
PIRiS36713.
RefSeqiNP_009381.1. NM_001178166.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4B8CX-ray3.41D/J/K/L111-837[»]
ProteinModelPortaliP31384.
SMRiP31384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31745. 285 interactors.
DIPiDIP-2522N.
IntActiP31384. 31 interactors.
MINTiMINT-615079.

PTM databases

iPTMnetiP31384.

Proteomic databases

MaxQBiP31384.
PRIDEiP31384.
TopDownProteomicsiP31384.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYAL021C; YAL021C; YAL021C.
GeneIDi851212.
KEGGisce:YAL021C.

Organism-specific databases

EuPathDBiFungiDB:YAL021C.
SGDiS000000019. CCR4.

Phylogenomic databases

GeneTreeiENSGT00550000074364.
HOGENOMiHOG000294222.
InParanoidiP31384.
KOiK12603.
OMAiCTKQALM.
OrthoDBiEOG092C0WZC.

Enzyme and pathway databases

BioCyciYEAST:G3O-28833-MONOMER.

Miscellaneous databases

PROiP31384.

Family and domain databases

Gene3Di3.60.10.10. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR005135. Endo/exonuclease/phosphatase.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
[Graphical view]
PfamiPF03372. Exo_endo_phos. 1 hit.
PF13855. LRR_8. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 2 hits.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
SSF56219. SSF56219. 1 hit.
PROSITEiPS51450. LRR. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCR4_YEAST
AccessioniPrimary (citable) accession number: P31384
Secondary accession number(s): D6VPJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 5, 2010
Last modified: November 2, 2016
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2780 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome I
    Yeast (Saccharomyces cerevisiae) chromosome I: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.