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CCR4F_ARATH
ID   CCR4F_ARATH             Reviewed;         754 AA.
AC   Q8VYU4; Q9LFM2;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Carbon catabolite repressor protein 4 homolog 6;
DE            Short=CCR4 homolog 6;
DE            EC=3.1.13.4;
GN   Name=CCR4-6; OrderedLocusNames=At5g11350; ORFNames=F2I11_240;
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=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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=CAB96670.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL360314; CAB96670.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91664.1; -; Genomic_DNA.
DR   EMBL; AY069916; AAL47464.1; -; mRNA.
DR   EMBL; AY143977; AAN28916.1; -; mRNA.
DR   RefSeq; NP_196696.2; NM_121173.5.
DR   AlphaFoldDB; Q8VYU4; -.
DR   SMR; Q8VYU4; -.
DR   STRING; 3702.AT5G11350.1; -.
DR   iPTMnet; Q8VYU4; -.
DR   PaxDb; Q8VYU4; -.
DR   PRIDE; Q8VYU4; -.
DR   EnsemblPlants; AT5G11350.1; AT5G11350.1; AT5G11350.
DR   GeneID; 831006; -.
DR   Gramene; AT5G11350.1; AT5G11350.1; AT5G11350.
DR   KEGG; ath:AT5G11350; -.
DR   Araport; AT5G11350; -.
DR   TAIR; locus:2832132; AT5G11350.
DR   eggNOG; KOG2338; Eukaryota.
DR   HOGENOM; CLU_008664_0_0_1; -.
DR   InParanoid; Q8VYU4; -.
DR   PhylomeDB; Q8VYU4; -.
DR   PRO; PR:Q8VYU4; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8VYU4; baseline and differential.
DR   Genevisible; Q8VYU4; AT.
DR   GO; GO:0005737; C:cytoplasm; IDA:TAIR.
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; -; 2.
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..754
FT                   /note="Carbon catabolite repressor protein 4 homolog 6"
FT                   /id="PRO_0000355049"
FT   REGION          34..65
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          404..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          494..558
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:O95551"
FT   CONFLICT        291
FT                   /note="G -> R (in Ref. 3; AAN28916/AAL47464)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   754 AA;  84925 MW;  B53A55C92AC288CF CRC64;
     MRRSRFVAQV FSDVTFADAS TISAPIFTMS TRAPYRGARG RGRGRGGRSF SDRPYNDDAG
     RDQFVTGDSH FQSVHDANFR FRHGEPYRQH QPPLDQRQQP PFNQNYEFRP PPPSRGQWQQ
     FRQPNQFPSN QNYAACPPPP FYQNQMSRPP PQQSFRQRPR SKPSDYREWE YAKTPPSPGS
     EKFVVLSYNI LADYLANDHW RSLYFHIPRN MLSWGWRKSK LVFELSLWSA DIMCLQEVDK
     FQDLEEEMKH RGYSAIWKMR TGNAVDGCAI FWRSNRFKLV HEESIQFNQL GLRDNVAQIC
     VLETLLTSHT KENETPPPES SAGSHRVVIC NIHVLFNPKR GDFKLGQVRT LLDKAHAVSK
     LWDDAPIVLC GDFNCTPKSP LYNFISDRKL DLSGLARDKV SGQVSAEFRP PRPENYTTRY
     QSANKSPQGQ VQPPNLITNA HMENNSNIDV GTAPSEKTSE LPCGDTILAG HEATSSSDQV
     LPCENMASDC QFGIENRKPD DSGNLSTAED LSSLTISDTE PQHASSARED LNTDRSVSSG
     LSETEQTPEE ICSSDQDISS SLSTKVDTFV AEMKLDGLKL DEPVVFAQDE ESLGEDGETF
     LAKLHDNNEN LSQKGELVSE VPLKWSSEAL NSDKITYSPS SWTPMEIATA TGDPERTTVE
     HALELKSTYS EVEGQANTRD ENGEPVVTSY HRCFMGTVDY IWRSEGLQTV RVLAPIPKQA
     MQWTPGFPTP KWGSDHIALV SELAFCSSKT LPKS
 
 
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