CCR4_SCHPO
ID CCR4_SCHPO Reviewed; 690 AA.
AC O74874;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4 {ECO:0000312|PomBase:SPCC31H12.08c};
DE EC=3.1.13.4;
DE AltName: Full=Carbon catabolite repressor protein 4;
DE AltName: Full=Cytoplasmic deadenylase;
DE AltName: Full=Glucose-repressible alcohol dehydrogenase transcriptional effector;
GN Name=ccr4; ORFNames=SPCC31H12.08c, SPCC5E4.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION, INTERACTION WITH PIR2, AND DISRUPTION PHENOTYPE.
RX PubMed=26942678; DOI=10.1016/j.molcel.2016.01.029;
RA Sugiyama T., Thillainadesan G., Chalamcharla V.R., Meng Z.,
RA Balachandran V., Dhakshnamoorthy J., Zhou M., Grewal S.I.S.;
RT "Enhancer of Rudimentary Cooperates with Conserved RNA-Processing Factors
RT to Promote Meiotic mRNA Decay and Facultative Heterochromatin Assembly.";
RL Mol. Cell 61:747-759(2016).
CC -!- FUNCTION: Acts as catalytic component of the CCR4-NOT core complex,
CC which in the nucleus seems to be a general transcription factor, and in
CC the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By
CC similarity). Ccr4 has 3'-5' RNase activity with a strong preference for
CC polyadenylated substrates and also low exonuclease activity towards
CC single-stranded DNA (By similarity). Participates in the shortening of
CC poly(A)-tails (PubMed:26942678). Erh1-mmi1 complex-mediated recruitment
CC of CCR4-NOT to target RNAs promotes heterochromatin formation at RNAi-
CC dependent heterochromatin domains (HOODs), including a subset of
CC meiotic genes, lncRNAs and retrotransposons (PubMed:26942678).
CC Recruitment of the CCR4-NOT complex to rDNA promotes rDNA
CC heterochromatin assembly (PubMed:26942678).
CC {ECO:0000250|UniProtKB:P31384, ECO:0000269|PubMed:26942678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Subunit of the CCR4-NOT core complex (By similarity).
CC Interacts with pir2 (PubMed:26942678). {ECO:0000250|UniProtKB:P31384,
CC ECO:0000269|PubMed:26942678}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Decreases heterochromatin formation at rDNA and
CC subtelomeres. {ECO:0000269|PubMed:26942678}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; CU329672; CAA21225.1; -; Genomic_DNA.
DR PIR; T41296; T41296.
DR RefSeq; NP_587901.1; NM_001022893.2.
DR AlphaFoldDB; O74874; -.
DR SMR; O74874; -.
DR BioGRID; 275490; 531.
DR STRING; 4896.SPCC31H12.08c.1; -.
DR iPTMnet; O74874; -.
DR MaxQB; O74874; -.
DR PaxDb; O74874; -.
DR PRIDE; O74874; -.
DR EnsemblFungi; SPCC31H12.08c.1; SPCC31H12.08c.1:pep; SPCC31H12.08c.
DR GeneID; 2538913; -.
DR KEGG; spo:SPCC31H12.08c; -.
DR PomBase; SPCC31H12.08c; ccr4.
DR VEuPathDB; FungiDB:SPCC31H12.08c; -.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_4_0_1; -.
DR InParanoid; O74874; -.
DR OMA; YHFPSDH; -.
DR PhylomeDB; O74874; -.
DR PRO; PR:O74874; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:PomBase.
DR GO; GO:0030015; C:CCR4-NOT core complex; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000932; C:P-body; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:PomBase.
DR Gene3D; 3.60.10.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SUPFAM; SSF56219; SSF56219; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Exonuclease; Hydrolase; Leucine-rich repeat;
KW Magnesium; Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat;
KW Repressor; RNA-binding; Transcription; Transcription regulation.
FT CHAIN 1..690
FT /note="CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4"
FT /id="PRO_0000290617"
FT REPEAT 157..180
FT /note="LRR 1"
FT REPEAT 182..203
FT /note="LRR 2"
FT REPEAT 205..226
FT /note="LRR 3"
FT REPEAT 228..249
FT /note="LRR 4"
FT REPEAT 251..272
FT /note="LRR 5"
FT REGION 110..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 690 AA; 76456 MW; 3A6E242F017C636C CRC64;
MFNPRYTQGT IYPGAHPGLL TPDHQHAAIL SVQNSPALEN SNISEHWKQQ IALATQSRSF
SSPHQRAHNA AALARSGGPG FSMNYNARTG AFTGGPNAAG LSSLGGKYNT SSTTTTLTTS
TTLNTSSGTT LNSTSKTTTS SVAVDDQKSK SDSKKERRDW TCLDLGGIGL RNVSTDLFKF
SFLTELYINH NNLTRLPPEI GKLKNLVILD ASGNSIKTIP PELGLLTELR EVLLFDNMIS
VIPAELGTLF QLKILGIEGN PLQDVYKNQI MESGTAGLIA ALRDGCPVGP PPPERGWEKL
VSDDDDDVND NVSTSVRDLT AADSNKPSTT SKNLKFTIMS YNVLCERYAT STLYGYTPSW
ALSWSYRKDL IMQELGGYNA DIICLQEVDV ENYDTFFAPQ MSLKGYKGVH FPKSRVRTMN
EVERRIVDGC ATFFKTSKYV MHEKMVIEYN QAPSLRRQDI KLTSNMYNRV MTKDNISVIT
LLENKENGSR LIVANCHIHW DPQFRDVKVI QVAMLMDEIA QVATKFRNMP SKIPSDQLKD
ERPTYPEYLK IPILICGDFN SVQGSGVYDF LSSGSISQNH EDFMNNDYGE YTVNGRSHAF
NLKSAYGESE ALSFTNYTPG FKGAIDHIWY TGNSLEVTGL LKGVDKDYLS GVVGFPNAHF
PSDHICLLAE FKVKQEKTPL PSSKFNNDKK
