CTF77_ARATH
ID CTF77_ARATH Reviewed; 734 AA.
AC Q8GUP1; Q8LKG5; Q9FZ58;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Cleavage stimulation factor subunit 77 {ECO:0000303|PubMed:12379796};
DE Short=AtCstF-77 {ECO:0000303|PubMed:12379796};
DE Short=AtCstF77 {ECO:0000303|PubMed:16282318};
DE AltName: Full=CF-1 77 kDa subunit {ECO:0000305};
DE AltName: Full=Cleavage stimulation factor 77 kDa subunit {ECO:0000305};
DE Short=CSTF 77 kDa subunit {ECO:0000305};
DE AltName: Full=Protein SUPPRESSORS OF OVEREXPRESSED FCA 2 {ECO:0000303|PubMed:19965720};
DE Short=SOF2 {ECO:0000303|PubMed:19965720};
GN Name=CSTF77 {ECO:0000303|PubMed:12379796};
GN OrderedLocusNames=At1g17760 {ECO:0000312|Araport:AT1G17760};
GN ORFNames=F11A6.10 {ECO:0000312|EMBL:AAF99818.1};
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|EMBL:AAN86153.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CSTF64.
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;
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).
RN [5]
RP GENE FAMILY, AND INTERACTION WITH FIPS5.
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 INTERACTION WITH CSTF64; CPSF30; FIPS5; PCFS1 AND PCFS5, 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 [7]
RP INTERACTION WITH FIPS5 AND CSTF64.
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 [8]
RP INTERACTION WITH CPSF30.
RX PubMed=20214900; DOI=10.1016/j.febslet.2010.03.007;
RA Bell S.A., Hunt A.G.;
RT "The Arabidopsis ortholog of the 77 kDa subunit of the cleavage stimulatory
RT factor (AtCstF-77) involved in mRNA polyadenylation is an RNA-binding
RT protein.";
RL FEBS Lett. 584:1449-1454(2010).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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). Required for the targeted
CC 3' processing of antisense transcripts that triggers transcriptional
CC silencing of the corresponding sense gene (PubMed:19965720).
CC {ECO:0000250|UniProtKB:Q12996, ECO:0000269|PubMed:19965720}.
CC -!- SUBUNIT: Homodimer. Belongs to the CSTF complex (By similarity). Forms
CC a complex with cleavage and polyadenylation specificity factor (CPSF)
CC subunits CPSF30, CSTF64, PCFS1, PCFS5 and FIPS5 (PubMed:12379796,
CC PubMed:16282318, PubMed:18479511, PubMed:18221017, PubMed:20214900).
CC {ECO:0000250|UniProtKB:Q12996, ECO:0000269|PubMed:12379796,
CC ECO:0000269|PubMed:16282318, ECO:0000269|PubMed:18221017,
CC ECO:0000269|PubMed:18479511, ECO:0000269|PubMed:20214900}.
CC -!- INTERACTION:
CC Q8GUP1; A9LNK9: CPSF30; NbExp=2; IntAct=EBI-1775543, EBI-962511;
CC Q8GUP1; Q9M9G6: CSTF64; NbExp=3; IntAct=EBI-1775543, EBI-1775671;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q12996}.
CC -!- DISRUPTION PHENOTYPE: Impaired antisense-RNA-mediated gene silencing
CC (e.g. suppression of overexpression of FCA-mediated FLC repression).
CC Delayed flowering and female gametophytic lethality.
CC {ECO:0000269|PubMed:19965720}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF99818.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF515697; AAM64166.1; -; mRNA.
DR EMBL; AC034257; AAF99818.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29633.1; -; Genomic_DNA.
DR EMBL; BT002320; AAN86153.1; -; mRNA.
DR PIR; F86312; F86312.
DR RefSeq; NP_173218.2; NM_101639.3.
DR AlphaFoldDB; Q8GUP1; -.
DR SMR; Q8GUP1; -.
DR BioGRID; 23593; 9.
DR IntAct; Q8GUP1; 5.
DR MINT; Q8GUP1; -.
DR STRING; 3702.AT1G17760.1; -.
DR PaxDb; Q8GUP1; -.
DR PRIDE; Q8GUP1; -.
DR ProteomicsDB; 222698; -.
DR EnsemblPlants; AT1G17760.1; AT1G17760.1; AT1G17760.
DR GeneID; 838354; -.
DR Gramene; AT1G17760.1; AT1G17760.1; AT1G17760.
DR KEGG; ath:AT1G17760; -.
DR Araport; AT1G17760; -.
DR TAIR; locus:2007973; AT1G17760.
DR eggNOG; KOG1914; Eukaryota.
DR HOGENOM; CLU_007630_3_0_1; -.
DR InParanoid; Q8GUP1; -.
DR OMA; LCYIDYL; -.
DR OrthoDB; 331411at2759; -.
DR PhylomeDB; Q8GUP1; -.
DR PRO; PR:Q8GUP1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8GUP1; baseline and differential.
DR Genevisible; Q8GUP1; AT.
DR GO; GO:0005634; C:nucleus; 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:0009553; P:embryo sac development; IMP:TAIR.
DR GO; GO:0031047; P:gene silencing by RNA; IMP:UniProtKB.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:InterPro.
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:0031123; P:RNA 3'-end processing; IMP:TAIR.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR19980; PTHR19980; 1.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 10.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW mRNA processing; Nucleus; Reference proteome; Repeat;
KW RNA-mediated gene silencing.
FT CHAIN 1..734
FT /note="Cleavage stimulation factor subunit 77"
FT /id="PRO_0000431324"
FT REPEAT 20..52
FT /note="HAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 54..85
FT /note="HAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 93..128
FT /note="HAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 139..172
FT /note="HAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 198..237
FT /note="HAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 246..278
FT /note="HAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 280..312
FT /note="HAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 314..345
FT /note="HAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 347..379
FT /note="HAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 382..414
FT /note="HAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 416..450
FT /note="HAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 474..505
FT /note="HAT 12"
FT /evidence="ECO:0000255"
FT REGION 637..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..684
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 573
FT /note="N -> S (in Ref. 1; AAM64166)"
SQ SEQUENCE 734 AA; 82650 MW; FB12DEB0174E4463 CRC64;
MADKYIVEEA EALAKRALHS PIAQATPIYE QLLSLYPTSA RFWKQYVEAQ MAVNNDDATK
QIFSRCLLTC LQVPLWQCYI RFIRKVYDKK GAEGQEETTK AFEFMLNYIG TDIASGPIWT
EYIAFLKSLP ALNLNEDLHR KTALRKVYHR AILTPTHHVE QLWKDYENFE NTVNRQLAKG
LVNEYQPKFN SARAVYRERK KYIEEIDWNM LAVPPTGTSK EETQWVAWKK FLSFEKGNPQ
RIDTASSTKR IIYAYEQCLM CLYHYPDVWY DYAEWHVKSG STDAAIKVFQ RALKAIPDSE
MLKYAFAEME ESRGAIQSAK KLYENILGAS TNSLAHIQYL RFLRRAEGVE AARKYFLDAR
KSPSCTYHVY IAFATMAFCI DKEPKVAHNI FEEGLKLYMS EPVYILKYAD FLTRLNDDRN
IRALFERALS TLPVEDSAEV WKRFIQFEQT YGDLASILKV EQRMKEALSG KGEEGSSPPE
SSLQDVVSRY SYMDLWPCTS NDLDHLARQE LLVKNLNKKA GKTNLPHVPA AIGSVASSSK
VVYPDTSQMV VQDPTKKSEF ASSANPVAAS ASNTFPSTVT ATATHGSAST FDEIPKTTPP
ALVAFLANLP IVDGPTPNVD VVLSICLQSD FPTGQTVKQS FAAKGNPPSQ NDPSGPTRGV
SQRLPRDRRA TKRKDSDRQE EDDTATVQSQ PLPTDVFRLR QMRKARGIAT SSQTPTGSTS
YGSAFSGELS GSTG
