CCR4E_ARATH
ID CCR4E_ARATH Reviewed; 454 AA.
AC Q0WKY2; Q6NNI4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Carbon catabolite repressor protein 4 homolog 5;
DE Short=CCR4 homolog 5;
DE EC=3.1.13.4;
GN Name=CCR4-5; OrderedLocusNames=At1g73875; ORFNames=F2P9.30;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=cv. Columbia;
RA Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000250}.
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: Component of the CCR4-NOT complex, at least composed of CRR4
CC and CAF1 proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q0WKY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0WKY2-2; Sequence=VSP_035834, VSP_035835;
CC Name=3;
CC IsoId=Q0WKY2-3; Sequence=VSP_035833, VSP_035836;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
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DR EMBL; AC016662; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE35519.1; -; Genomic_DNA.
DR EMBL; BT010832; AAR24199.1; -; mRNA.
DR EMBL; BT011303; AAR92339.1; -; mRNA.
DR EMBL; AK230427; BAF02225.1; -; mRNA.
DR RefSeq; NP_683491.2; NM_148650.4. [Q0WKY2-1]
DR AlphaFoldDB; Q0WKY2; -.
DR SMR; Q0WKY2; -.
DR STRING; 3702.AT1G73875.1; -.
DR PaxDb; Q0WKY2; -.
DR PRIDE; Q0WKY2; -.
DR EnsemblPlants; AT1G73875.1; AT1G73875.1; AT1G73875. [Q0WKY2-1]
DR GeneID; 843724; -.
DR Gramene; AT1G73875.1; AT1G73875.1; AT1G73875. [Q0WKY2-1]
DR KEGG; ath:AT1G73875; -.
DR Araport; AT1G73875; -.
DR TAIR; locus:504956231; AT1G73875.
DR eggNOG; KOG2338; Eukaryota.
DR HOGENOM; CLU_016428_0_0_1; -.
DR InParanoid; Q0WKY2; -.
DR OMA; EMNCEDP; -.
DR OrthoDB; 704519at2759; -.
DR PhylomeDB; Q0WKY2; -.
DR PRO; PR:Q0WKY2; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WKY2; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleus; Reference proteome; Repeat; RNA-binding;
KW Transcription; Transcription regulation.
FT CHAIN 1..454
FT /note="Carbon catabolite repressor protein 4 homolog 5"
FT /id="PRO_0000355048"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
FT VAR_SEQ 1..219
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035833"
FT VAR_SEQ 175
FT /note="S -> I (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035834"
FT VAR_SEQ 176..454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_035835"
FT VAR_SEQ 435..454
FT /note="NWGSDHLAIACELGFVNDWQ -> VSFFF (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_035836"
SQ SEQUENCE 454 AA; 52152 MW; 89F14DE33407FFDC CRC64;
MSGYERKNTT ANSITITKRK RNSISEQSEN VYEKSNRKES ITLKPHRSFT PGFSQRDCKP
VRHSKSSLRR RRRTKEKISS SVEREWVFSA NNFENLADKL VLVSYNLLGV DNASNHMDLY
YNVPRKHLEW SRRKHLICKE ISRYNASILC LQEVDRFDDL DVLLKNRGFR GVHKSRTGEA
SDGCAIFWKE NLFELLDHQH IEFDKFGMRN NVAQLCVLEM NCEEDPKSKL RVRSSDPRRL
VVGNIHVLFN PKRGDIKLGQ VRLFLEKAYK LSQEWGNIPV AIAGDLNSTP QSAIYDFIAS
ADLDTQLHDR RQISGQTEVE PKERSFRNHY AFSASASISG SLLNEWSQEE LQLATGGQET
THVQHQLKLN SAYSGVPGTY RTRDQRGEPL ATTYHSRFLG TVDYIWHTKE LVPVRVLETL
PADVLRRTGG LPSENWGSDH LAIACELGFV NDWQ
