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CFIS2_ARATH
ID   CFIS2_ARATH             Reviewed;         200 AA.
AC   Q8GXS3; O65606; Q570Y1; Q9M0K5;
DT   26-NOV-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 127.
DE   RecName: Full=Pre-mRNA cleavage factor Im 25 kDa subunit 2 {ECO:0000303|PubMed:18479511};
GN   Name=CFIS2 {ECO:0000303|PubMed:18479511};
GN   OrderedLocusNames=At4g25550 {ECO:0000312|Araport:AT4G25550};
GN   ORFNames=M7J2.80 {ECO:0000312|EMBL:BAC42701.1};
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:BAC42701.1};
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] (ISOFORM 1).
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH FIPS5; PAPS4 AND CPSF30, 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, PAPS4 and CPSF30
CC       (PubMed:18479511). {ECO:0000250|UniProtKB:O43809,
CC       ECO:0000269|PubMed:18479511}.
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8GXS3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8GXS3-2; Sequence=VSP_057237;
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family. CPSF5 subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA18171.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB81365.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL022197; CAA18171.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161563; CAB81365.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85076.1; -; Genomic_DNA.
DR   EMBL; AK118070; BAC42701.1; -; mRNA.
DR   EMBL; BT005519; AAO63939.1; -; mRNA.
DR   EMBL; AK220576; BAD94845.1; -; mRNA.
DR   EMBL; AK228476; BAF00402.1; -; mRNA.
DR   PIR; C85295; C85295.
DR   PIR; T05792; T05792.
DR   RefSeq; NP_194285.2; NM_118687.3. [Q8GXS3-1]
DR   AlphaFoldDB; Q8GXS3; -.
DR   SMR; Q8GXS3; -.
DR   BioGRID; 13947; 11.
DR   IntAct; Q8GXS3; 11.
DR   STRING; 3702.AT4G25550.1; -.
DR   PaxDb; Q8GXS3; -.
DR   PRIDE; Q8GXS3; -.
DR   ProteomicsDB; 220611; -. [Q8GXS3-1]
DR   EnsemblPlants; AT4G25550.1; AT4G25550.1; AT4G25550. [Q8GXS3-1]
DR   GeneID; 828660; -.
DR   Gramene; AT4G25550.1; AT4G25550.1; AT4G25550. [Q8GXS3-1]
DR   KEGG; ath:AT4G25550; -.
DR   Araport; AT4G25550; -.
DR   TAIR; locus:2131839; AT4G25550.
DR   eggNOG; KOG1689; Eukaryota.
DR   HOGENOM; CLU_068704_1_1_1; -.
DR   InParanoid; Q8GXS3; -.
DR   OMA; EHYEQYG; -.
DR   PhylomeDB; Q8GXS3; -.
DR   PRO; PR:Q8GXS3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8GXS3; baseline and differential.
DR   Genevisible; Q8GXS3; AT.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
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   GO; GO:0006364; P:rRNA processing; IMP:TAIR.
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   Alternative splicing; Metal-binding; mRNA processing; Nucleus;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..200
FT                   /note="Pre-mRNA cleavage factor Im 25 kDa subunit 2"
FT                   /id="PRO_0000431332"
FT   DOMAIN          45..172
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   REGION          72..74
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250|UniProtKB:O43809"
FT   MOTIF           79..100
FT                   /note="Nudix box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT   SITE            33
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250|UniProtKB:O43809"
FT   SITE            179
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000250|UniProtKB:O43809"
FT   VAR_SEQ         57..200
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_057237"
SQ   SEQUENCE   200 AA;  22830 MW;  557862865ACB39C8 CRC64;
     MAMSQVVNTY PLSNYSFGTK EPKLEKDTSV ADRLARMKIN YMKEGMRTSV EGILLVQEHN
     HPHILLLQIG NTFCKLPGGR LKPGENEADG LKRKLTSKLG GNSAALVPDW TVGECVATWW
     RPNFETMMYP YCPPHITKPK ECKRLYIVHL SEKEYFAVPK NLKLLAVPLF ELYDNVQRYG
     PVISTIPQQL SRFHFNMISS
 
 
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