CFIS1_ARATH
ID CFIS1_ARATH Reviewed; 222 AA.
AC Q94AF0; Q9SZQ4;
DT 26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Pre-mRNA cleavage factor Im 25 kDa subunit 1 {ECO:0000303|PubMed:18479511};
DE AltName: Full=Cleavage and polyadenylation specificity factor 25 kDa subunit {ECO:0000303|PubMed:16282318};
DE Short=AtCFI-25 {ECO:0000303|PubMed:16282318};
DE Short=CFIm-25 {ECO:0000303|PubMed:16282318};
DE Short=CPSF 25 kDa subunit {ECO:0000305};
DE AltName: Full=Cleavage and polyadenylation specificity factor subunit 25 {ECO:0000303|PubMed:16282318};
GN Name=CFIS1 {ECO:0000303|PubMed:18479511};
GN Synonyms=CFIM25 {ECO:0000303|PubMed:16282318};
GN OrderedLocusNames=At4g29820 {ECO:0000312|Araport:AT4G29820};
GN ORFNames=F27B13.60 {ECO:0000312|EMBL:CAB43657.1};
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:AAK82492.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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 FIPS5, GENE FAMILY, AND 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).
CC -!- FUNCTION: Component of the cleavage factor Im (CFIm) complex that plays
CC a key role in pre-mRNA 3'-processing. Involved in association with
CC CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A)
CC addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA
CC substrates. The homodimer mediates simultaneous sequence-specific
CC recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to,
CC but does not hydrolyze mono- and di-adenosine nucleotides. May have a
CC role in mRNA export. {ECO:0000250|UniProtKB:O43809}.
CC -!- SUBUNIT: Homodimer. Component of the cleavage factor Im (CFIm) complex
CC (By similarity). Forms a complex with cleavage and polyadenylation
CC specificity factor (CPSF) subunits FIPS5 (PubMed:16282318,
CC PubMed:18479511). {ECO:0000250|UniProtKB:O43809,
CC ECO:0000269|PubMed:16282318, ECO:0000269|PubMed:18479511}.
CC -!- INTERACTION:
CC Q94AF0; F4KDH9: FIPS5; NbExp=3; IntAct=EBI-962531, EBI-962489;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O43809}. Note=In
CC punctate subnuclear structures localized adjacent to nuclear speckles,
CC called paraspeckles. {ECO:0000250|UniProtKB:O43809}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB43657.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB79740.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL050352; CAB43657.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161575; CAB79740.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE85682.1; -; Genomic_DNA.
DR EMBL; AY048229; AAK82492.1; -; mRNA.
DR EMBL; AY091704; AAM10303.1; -; mRNA.
DR EMBL; AY085984; AAM63194.1; -; mRNA.
DR PIR; T08543; T08543.
DR RefSeq; NP_567835.1; NM_119128.3.
DR AlphaFoldDB; Q94AF0; -.
DR SMR; Q94AF0; -.
DR BioGRID; 14391; 10.
DR IntAct; Q94AF0; 9.
DR STRING; 3702.AT4G29820.1; -.
DR PaxDb; Q94AF0; -.
DR PRIDE; Q94AF0; -.
DR ProteomicsDB; 241231; -.
DR EnsemblPlants; AT4G29820.1; AT4G29820.1; AT4G29820.
DR GeneID; 829104; -.
DR Gramene; AT4G29820.1; AT4G29820.1; AT4G29820.
DR KEGG; ath:AT4G29820; -.
DR Araport; AT4G29820; -.
DR TAIR; locus:2123919; AT4G29820.
DR eggNOG; KOG1689; Eukaryota.
DR HOGENOM; CLU_068704_1_1_1; -.
DR InParanoid; Q94AF0; -.
DR OMA; DIYPLNH; -.
DR OrthoDB; 1194206at2759; -.
DR PhylomeDB; Q94AF0; -.
DR PRO; PR:Q94AF0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AF0; baseline and differential.
DR Genevisible; Q94AF0; AT.
DR GO; GO:0005849; C:mRNA cleavage factor complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IBA:GO_Central.
DR InterPro; IPR016706; Cleav_polyA_spec_factor_su5.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR PANTHER; PTHR13047; PTHR13047; 1.
DR Pfam; PF13869; NUDIX_2; 1.
DR PIRSF; PIRSF017888; CPSF-25; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
PE 1: Evidence at protein level;
KW Metal-binding; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..222
FT /note="Pre-mRNA cleavage factor Im 25 kDa subunit 1"
FT /id="PRO_0000431331"
FT DOMAIN 67..194
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 94..96
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT MOTIF 101..122
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT SITE 55
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
FT SITE 201
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250|UniProtKB:O43809"
SQ SEQUENCE 222 AA; 25561 MW; EEE18D3C747B59CD CRC64;
MGEEARALDM EEISDNTTRR NDVVHDLMVD LYPLSSYYFG SKEALRVKDE IISDRVIRLK
SNYAAHGLRT CVEAVLLVEL FKHPHVLLLQ YRNSIFKLPG GRLRPGESDI EGLKRKLASK
LSVNENVGVS GYEVGECIGM WWRPNFETLM YPFLPPNIKH PKECTKLFLV RLPVHQQFVV
PKNFKLLAVP LCQLHENEKT YGPIMSQIPK LLSKFSFNMM EI
