CPSF2_ARATH
ID CPSF2_ARATH Reviewed; 739 AA.
AC Q9LKF9; Q9FF92;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 150.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE Short=AtCPSF100;
DE Short=CPSF 100 kDa subunit;
DE AltName: Full=Protein EMBRYO DEFECTIVE 1265;
DE AltName: Full=Protein ENHANCED SILENCING PHENOTYPE 5 {ECO:0000303|PubMed:17008405};
GN Name=CPSF100; Synonyms=EMB1265, ESP5 {ECO:0000303|PubMed:17008405};
GN OrderedLocusNames=At5g23880 {ECO:0000312|Araport:AT5G23880};
GN ORFNames=MRO11.8 {ECO:0000312|EMBL:BAB10061.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12602868; DOI=10.1023/a:1022035219500;
RA Elliott B.J., Dattaroy T., Meeks-Midkiff L.R., Forbes K.P., Hunt A.G.;
RT "An interaction between an Arabidopsis poly(A) polymerase and a homologue
RT of the 100 kDa subunit of CPSF.";
RL Plant Mol. Biol. 51:373-384(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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 FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
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 [6]
RP INTERACTION WITH CPSF160; PAPS2; CSTF50; FY AND CPSF30, 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 SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF30.
RX PubMed=19573236; DOI=10.1186/1471-2121-10-51;
RA Rao S., Dinkins R.D., Hunt A.G.;
RT "Distinctive interactions of the Arabidopsis homolog of the 30 kD subunit
RT of the cleavage and polyadenylation specificity factor (AtCPSF30) with
RT other polyadenylation factor subunits.";
RL BMC Cell Biol. 10:51-51(2009).
RN [8]
RP COMPONENT OF CPSF COMPLEX.
RX PubMed=19748916; DOI=10.1104/pp.109.142729;
RA Zhao H., Xing D., Li Q.Q.;
RT "Unique features of plant cleavage and polyadenylation specificity factor
RT revealed by proteomic studies.";
RL Plant Physiol. 151:1546-1556(2009).
RN [9]
RP INTERACTION WITH FY.
RX PubMed=19439664; DOI=10.1073/pnas.0903444106;
RA Manzano D., Marquardt S., Jones A.M., Baurle I., Liu F., Dean C.;
RT "Altered interactions within FY/AtCPSF complexes required for Arabidopsis
RT FCA-mediated chromatin silencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8772-8777(2009).
CC -!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
CC recognizing the AAUAAA signal sequence and interacting with
CC poly(A)polymerase and other factors to bring about cleavage and poly(A)
CC addition (By similarity). Required for antisense-RNA-mediated gene
CC silencing (PubMed:17008405). {ECO:0000250|UniProtKB:O17403,
CC ECO:0000269|PubMed:17008405}.
CC -!- SUBUNIT: Component of the CPSF complex, at least composed of CPSF160,
CC CPSF100, CPSF73-I, CPSF73-II, CPSF30, FY and FIPS5. Forms a complex
CC with cleavage and polyadenylation specificity factor (CPSF) subunits
CC FY, PAPS2, CSTF50, CPSF30, CPSF73-I, CPSF73-II and CPSF160.
CC {ECO:0000269|PubMed:17008405, ECO:0000269|PubMed:18479511,
CC ECO:0000269|PubMed:19439664, ECO:0000269|PubMed:19573236}.
CC -!- INTERACTION:
CC Q9LKF9; Q9FGR0: CPSF160; NbExp=4; IntAct=EBI-1775444, EBI-1775436;
CC Q9LKF9; A9LNK9: CPSF30; NbExp=3; IntAct=EBI-1775444, EBI-962511;
CC Q9LKF9; Q9C952: CPSF73-I; NbExp=4; IntAct=EBI-1775444, EBI-1775464;
CC Q9LKF9; Q8GUU3: CPSF73-II; NbExp=3; IntAct=EBI-1775444, EBI-1775477;
CC Q9LKF9; Q6NLV4: FY; NbExp=3; IntAct=EBI-1775444, EBI-1632908;
CC Q9LKF9; O82312: PAPS2; NbExp=5; IntAct=EBI-1775444, EBI-1775513;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:19573236}. Note=Localized in the cytoplasm when
CC associated with CPSF30. {ECO:0000269|PubMed:19573236}.
CC -!- DISRUPTION PHENOTYPE: Impaired antisense-RNA-mediated gene silencing.
CC Early flowering. {ECO:0000269|PubMed:17008405}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF283277; AAF82809.1; -; mRNA.
DR EMBL; AB005244; BAB10061.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93228.1; -; Genomic_DNA.
DR EMBL; AY034982; AAK59487.1; -; mRNA.
DR EMBL; BT004374; AAO42368.1; -; mRNA.
DR RefSeq; NP_197776.1; NM_122293.4.
DR AlphaFoldDB; Q9LKF9; -.
DR SMR; Q9LKF9; -.
DR BioGRID; 17728; 20.
DR DIP; DIP-40385N; -.
DR IntAct; Q9LKF9; 9.
DR STRING; 3702.AT5G23880.1; -.
DR iPTMnet; Q9LKF9; -.
DR PaxDb; Q9LKF9; -.
DR PRIDE; Q9LKF9; -.
DR ProteomicsDB; 222618; -.
DR DNASU; 832453; -.
DR EnsemblPlants; AT5G23880.1; AT5G23880.1; AT5G23880.
DR GeneID; 832453; -.
DR Gramene; AT5G23880.1; AT5G23880.1; AT5G23880.
DR KEGG; ath:AT5G23880; -.
DR Araport; AT5G23880; -.
DR TAIR; locus:2172843; AT5G23880.
DR eggNOG; KOG1135; Eukaryota.
DR HOGENOM; CLU_002227_3_0_1; -.
DR InParanoid; Q9LKF9; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR PhylomeDB; Q9LKF9; -.
DR PRO; PR:Q9LKF9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LKF9; baseline and differential.
DR Genevisible; Q9LKF9; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IBA:GO_Central.
DR GO; GO:0006379; P:mRNA cleavage; ISS:TAIR.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:TAIR.
DR GO; GO:0035194; P:post-transcriptional gene silencing by RNA; IMP:TAIR.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..739
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 2"
FT /id="PRO_0000074398"
FT REGION 411..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 49
FT /note="S -> P (in Ref. 1; AAF82809)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="I -> V (in Ref. 1; AAF82809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 82139 MW; 9ABFC916712AD464 CRC64;
MGTSVQVTPL CGVYNENPLS YLVSIDGFNF LIDCGWNDLF DTSLLEPLSR VASTIDAVLL
SHPDTLHIGA LPYAMKQLGL SAPVYATEPV HRLGLLTMYD QFLSRKQVSD FDLFTLDDID
SAFQNVIRLT YSQNYHLSGK GEGIVIAPHV AGHMLGGSIW RITKDGEDVI YAVDYNHRKE
RHLNGTVLQS FVRPAVLITD AYHALYTNQT ARQQRDKEFL DTISKHLEVG GNVLLPVDTA
GRVLELLLIL EQHWSQRGFS FPIYFLTYVS SSTIDYVKSF LEWMSDSISK SFETSRDNAF
LLRHVTLLIN KTDLDNAPPG PKVVLASMAS LEAGFAREIF VEWANDPRNL VLFTETGQFG
TLARMLQSAP PPKFVKVTMS KRVPLAGEEL IAYEEEQNRL KREEALRASL VKEEETKASH
GSDDNSSEPM IIDTKTTHDV IGSHGPAYKD ILIDGFVPPS SSVAPMFPYY DNTSEWDDFG
EIINPDDYVI KDEDMDRGAM HNGGDVDGRL DEATASLMLD TRPSKVMSNE LIVTVSCSLV
KMDYEGRSDG RSIKSMIAHV SPLKLVLVHA IAEATEHLKQ HCLNNICPHV YAPQIEETVD
VTSDLCAYKV QLSEKLMSNV IFKKLGDSEV AWVDSEVGKT ERDMRSLLPM PGAASPHKPV
LVGDLKIADF KQFLSSKGVQ VEFAGGGALR CGEYVTLRKV GPTGQKGGAS GPQQILIEGP
LCEDYYKIRD YLYSQFYLL
