CCR4A_ARATH
ID CCR4A_ARATH Reviewed; 602 AA.
AC Q8W0Z9; Q9M2G0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Carbon catabolite repressor protein 4 homolog 1;
DE Short=CCR4 homolog 1;
DE EC=3.1.13.4;
GN Name=CCR4-1; OrderedLocusNames=At3g58560; ORFNames=F14P22.150;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 -!- SIMILARITY: Belongs to the CCR4/nocturin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB68194.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL137082; CAB68194.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE79799.1; -; Genomic_DNA.
DR EMBL; AF462845; AAL58932.1; -; mRNA.
DR EMBL; AY133538; AAM91368.1; -; mRNA.
DR PIR; T45676; T45676.
DR RefSeq; NP_191415.2; NM_115718.4.
DR AlphaFoldDB; Q8W0Z9; -.
DR SMR; Q8W0Z9; -.
DR BioGRID; 10340; 9.
DR IntAct; Q8W0Z9; 10.
DR STRING; 3702.AT3G58560.1; -.
DR iPTMnet; Q8W0Z9; -.
DR PaxDb; Q8W0Z9; -.
DR PRIDE; Q8W0Z9; -.
DR ProteomicsDB; 223933; -.
DR EnsemblPlants; AT3G58560.1; AT3G58560.1; AT3G58560.
DR GeneID; 825025; -.
DR Gramene; AT3G58560.1; AT3G58560.1; AT3G58560.
DR KEGG; ath:AT3G58560; -.
DR Araport; AT3G58560; -.
DR TAIR; locus:2076426; AT3G58560.
DR eggNOG; KOG0620; Eukaryota.
DR HOGENOM; CLU_016428_5_0_1; -.
DR InParanoid; Q8W0Z9; -.
DR OMA; MMEMSSG; -.
DR OrthoDB; 724242at2759; -.
DR PhylomeDB; Q8W0Z9; -.
DR PRO; PR:Q8W0Z9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8W0Z9; baseline and differential.
DR Genevisible; Q8W0Z9; AT.
DR GO; GO:0030014; C:CCR4-NOT complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000932; C:P-body; IPI:TAIR.
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; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IGI:TAIR.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR GO; GO:0019252; P:starch biosynthetic process; IGI:TAIR.
DR GO; GO:0005986; P:sucrose biosynthetic process; IGI:TAIR.
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 Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleus; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation.
FT CHAIN 1..602
FT /note="Carbon catabolite repressor protein 4 homolog 1"
FT /id="PRO_0000355044"
FT REGION 113..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:O95551"
SQ SEQUENCE 602 AA; 66761 MW; 233754749BCE74DC CRC64;
MLSVIRVHLP SEIPIVGCEL TPYVLLRRPD KTPSTDDVPE SAPLEGHFLK YRWFRVQSDK
KVAICSVHPS ETATLQCLGC LKSKVPVAKS YHCSTKCFSD AWQHHRVLHE RAASAATEGN
DEEELPRLNS SGSGSGVLST SVSLTNGSSS VYPSAITQKT GAGGETLVEV GRSKTYTPMA
DDICHVLKFE CVVVNAETKQ NVGLSCTILT SRVIPAPSPS PRRLISISGT DVTGHLDSNG
RPLSMGTFTV LSYNILSDTY ASSDIYSYCP TWALAWTYRR QNLLREIVKY RADIVCLQEV
QNDHFEEFFL PELDKHGYQG LFKRKTNEVF IGNTNTIDGC ATFFRRDRFS HVKKYEVEFN
KAAQSLTEAI IPVSQKKNAL NRLVKDNVAL IVVLEAKFGS QAADNPGKRQ LLCVANTHVN
VPHELKDVKL WQVHTLLKGL EKIAASADIP MLVCGDFNTV PASAPHTLLA VGKVDPLHPD
LMVDPLGILR PHSKLTHQLP LVSAYSQFAK MGGNVITEQQ RRRLDPASSE PLFTNCTRDF
IGTLDYIFYT ADTLTVESLL ELLDEESLRK DTALPSPEWS SDHIALLAEF RCMPRARRNN
IL
