CTF64_ARATH
ID CTF64_ARATH Reviewed; 461 AA.
AC Q9M9G6; Q8LKG6;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Cleavage stimulating factor 64 {ECO:0000303|PubMed:12379796};
DE Short=AtCstF-64 {ECO:0000303|PubMed:12379796};
DE Short=AtCstF64 {ECO:0000303|PubMed:16282318};
DE AltName: Full=CF-1 64 kDa subunit {ECO:0000305};
DE AltName: Full=Cleavage stimulation factor 64 kDa subunit {ECO:0000305};
DE Short=CSTF 64 kDa subunit {ECO:0000305};
DE AltName: Full=Protein ENHANCED SILENCING PHENOTYPE 1 {ECO:0000303|PubMed:17008405};
DE AltName: Full=Protein SUPPRESSORS OF OVEREXPRESSED FCA 19 {ECO:0000303|PubMed:19965720};
DE Short=SOF19 {ECO:0000303|PubMed:19965720};
GN Name=CSTF64 {ECO:0000303|PubMed:12379796};
GN Synonyms=ESP1 {ECO:0000303|PubMed:17008405};
GN OrderedLocusNames=At1g71800 {ECO:0000312|Araport:AT1G71800};
GN ORFNames=F14O23.18 {ECO:0000312|EMBL:AAF43233.1};
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 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH CSTF77 AND MRNA.
RC STRAIN=cv. Columbia;
RX PubMed=12379796; DOI=10.1093/jxb/erf073;
RA Yao Y., Song L., Katz Y., Galili G.;
RT "Cloning and characterization of Arabidopsis homologues of the animal CstF
RT complex that regulates 3' mRNA cleavage and polyadenylation.";
RL J. Exp. Bot. 53:2277-2278(2002).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.
RN [5]
RP GENE FAMILY.
RX PubMed=16282318; DOI=10.1074/jbc.m510964200;
RA Forbes K.P., Addepalli B., Hunt A.G.;
RT "An Arabidopsis Fip1 homolog interacts with RNA and provides conceptual
RT links with a number of other polyadenylation factor subunits.";
RL J. Biol. Chem. 281:176-186(2006).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17008405; DOI=10.1073/pnas.0606536103;
RA Herr A.J., Molnar A., Jones A., Baulcombe D.C.;
RT "Defective RNA processing enhances RNA silencing and influences flowering
RT of Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14994-15001(2006).
RN [7]
RP INTERACTION WITH CSTF50; CSTF77; FIPS3 AND FIPS5, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=18479511; DOI=10.1186/1471-2164-9-220;
RA Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R., Xing D.,
RA Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
RA Von Lanken C., Li Q.Q.;
RT "Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
RT protein-protein interactions and gene expression profiling.";
RL BMC Genomics 9:220-220(2008).
RN [8]
RP INTERACTION WITH CSTF77.
RX PubMed=18221017; DOI=10.2174/092986608783330431;
RA Addepalli B., Hunt A.G.;
RT "The interaction between two Arabidopsis polyadenylation factor subunits
RT involves an evolutionarily-conserved motif and has implications for the
RT assembly and function of the polyadenylation complex.";
RL Protein Pept. Lett. 15:76-88(2008).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19965720; DOI=10.1126/science.1180278;
RA Liu F., Marquardt S., Lister C., Swiezewski S., Dean C.;
RT "Targeted 3' processing of antisense transcripts triggers Arabidopsis FLC
RT chromatin silencing.";
RL Science 327:94-97(2010).
CC -!- FUNCTION: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of pre-mRNAs (By similarity). This subunit is directly
CC involved in the binding to pre-mRNAs, especially on the 3' non-coding
CC region (PubMed:12379796). Required for the targeted 3' processing of
CC antisense transcripts that triggers transcriptional silencing of the
CC corresponding sense gene (PubMed:17008405, PubMed:19965720).
CC {ECO:0000250|UniProtKB:Q8C7E9, ECO:0000269|PubMed:12379796,
CC ECO:0000269|PubMed:17008405, ECO:0000269|PubMed:19965720}.
CC -!- SUBUNIT: Belongs to the CSTF complex (By similarity). Binds to mRNA.
CC Forms a complex with cleavage and polyadenylation specificity factor
CC (CPSF) subunits CSTF50, CSTF77, FIPS3 and FIPS5 (PubMed:12379796,
CC PubMed:18479511, PubMed:18221017). {ECO:0000250|UniProtKB:P33240,
CC ECO:0000269|PubMed:12379796, ECO:0000269|PubMed:18221017,
CC ECO:0000269|PubMed:18479511}.
CC -!- INTERACTION:
CC Q9M9G6; Q8GUP1: CSTF77; NbExp=3; IntAct=EBI-1775671, EBI-1775543;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P33240}.
CC -!- DISRUPTION PHENOTYPE: Impaired antisense-RNA-mediated gene silencing
CC (e.g. suppression of overexpression of FCA-mediated FLC repression).
CC Reduced fertility, early flowering, reduced organ size and pale leaves.
CC {ECO:0000269|PubMed:17008405, ECO:0000269|PubMed:19965720}.
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DR EMBL; AF515695; AAM64164.1; -; mRNA.
DR EMBL; AC012654; AAF43233.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35234.1; -; Genomic_DNA.
DR EMBL; AK229116; BAF00992.1; -; mRNA.
DR PIR; E96740; E96740.
DR RefSeq; NP_177325.2; NM_105838.5.
DR AlphaFoldDB; Q9M9G6; -.
DR SMR; Q9M9G6; -.
DR BioGRID; 28730; 5.
DR IntAct; Q9M9G6; 5.
DR STRING; 3702.AT1G71800.1; -.
DR PaxDb; Q9M9G6; -.
DR PRIDE; Q9M9G6; -.
DR ProteomicsDB; 222697; -.
DR EnsemblPlants; AT1G71800.1; AT1G71800.1; AT1G71800.
DR GeneID; 843510; -.
DR Gramene; AT1G71800.1; AT1G71800.1; AT1G71800.
DR KEGG; ath:AT1G71800; -.
DR Araport; AT1G71800; -.
DR TAIR; locus:2013016; AT1G71800.
DR eggNOG; KOG0108; Eukaryota.
DR HOGENOM; CLU_028601_4_0_1; -.
DR InParanoid; Q9M9G6; -.
DR OMA; QAPSHMT; -.
DR OrthoDB; 1455080at2759; -.
DR PhylomeDB; Q9M9G6; -.
DR PRO; PR:Q9M9G6; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9M9G6; baseline and differential.
DR Genevisible; Q9M9G6; AT.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0042868; P:antisense RNA metabolic process; IMP:UniProtKB.
DR GO; GO:0048589; P:developmental growth; IMP:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:TAIR.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IMP:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR GO; GO:0031123; P:RNA 3'-end processing; IMP:TAIR.
DR Gene3D; 1.10.20.70; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR025742; CSTF2_hinge.
DR InterPro; IPR026896; CSTF_C.
DR InterPro; IPR038192; CSTF_C_sf.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF14327; CSTF2_hinge; 1.
DR Pfam; PF14304; CSTF_C; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..461
FT /note="Cleavage stimulating factor 64"
FT /id="PRO_0000431323"
FT DOMAIN 9..87
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 84..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 145
FT /note="L -> I (in Ref. 1; AAM64164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 50137 MW; C8D010D082AA8657 CRC64;
MASSSSQRRC VFVGNIPYDA TEEQLREICG EVGPVVSFRL VTDRETGKPK GYGFCEYKDE
ETALSARRNL QSYEINGRQL RVDFAENDKG TDKTRDQSQG GPGLPSTTTV TESQKQIGGP
VDSNMHQPVG LHLATTAASV IAGALGGPQV GSQFTQSNLQ VPASDPLALH LAKMSRSQLT
EIISSIKLMA TQNKEHARQL LVSRPQLLKA VFLAQVMLGI VSPQVLQSPN IVQAPSHMTG
SSIQDAQLSG QNLLPPLAQR SQQLSRAPHS QYPVQQSSKQ PFSQIPQLVA QPGPSSVNPP
PRSQVKVENA PFQRQQVVPA STNIGYSSQN SVPNNAIQPS QVPHQALPNS VMQQGGQTVS
LNFGKRINEG PPHQSMNRPS KMMKVEDRRT TSLPGGHVSN SMLPNQAQAP QTHISPDVQS
TLLQQVMNLT PEQLRLLTPE QQQEVLKLQQ ALKQDHMMQP S
