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Cleavage and polyadenylation specificity factor subunit 2 (Cleavage and polyadenylation specificity factor 100 kDa subunit) (AtCPSF100) (CPSF 100 kDa subunit) (Protein EMBRYO DEFECTIVE 1265) (Protein ENHANCED SILENCING PHENOTYPE 5)

 CPSF2_ARATH             Reviewed;         739 AA.
Q9LKF9; Q9FF92;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
18-OCT-2001, sequence version 2.
07-NOV-2018, entry version 135.
RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
Short=AtCPSF100;
Short=CPSF 100 kDa subunit;
AltName: Full=Protein EMBRYO DEFECTIVE 1265;
AltName: Full=Protein ENHANCED SILENCING PHENOTYPE 5 {ECO:0000303|PubMed:17008405};
Name=CPSF100; Synonyms=EMB1265, ESP5 {ECO:0000303|PubMed:17008405};
OrderedLocusNames=At5g23880 {ECO:0000312|Araport:AT5G23880};
ORFNames=MRO11.8 {ECO:0000312|EMBL:BAB10061.1};
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12602868; DOI=10.1023/A:1022035219500;
Elliott B.J., Dattaroy T., Meeks-Midkiff L.R., Forbes K.P., Hunt A.G.;
"An interaction between an Arabidopsis poly(A) polymerase and a
homologue of the 100 kDa subunit of CPSF.";
Plant Mol. Biol. 51:373-384(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=9330910; DOI=10.1093/dnares/4.3.215;
Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
Miyajima N., Tabata S.;
"Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
features of the 1.6 Mb regions covered by twenty physically assigned
P1 clones.";
DNA Res. 4:215-230(1997).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
PubMed=17008405; DOI=10.1073/pnas.0606536103;
Herr A.J., Molnar A., Jones A., Baulcombe D.C.;
"Defective RNA processing enhances RNA silencing and influences
flowering of Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 103:14994-15001(2006).
[6]
INTERACTION WITH CPSF160; PAPS2; CSTF50; FY AND CPSF30, GENE FAMILY,
AND NOMENCLATURE.
PubMed=18479511; DOI=10.1186/1471-2164-9-220;
Hunt A.G., Xu R., Addepalli B., Rao S., Forbes K.P., Meeks L.R.,
Xing D., Mo M., Zhao H., Bandyopadhyay A., Dampanaboina L., Marion A.,
Von Lanken C., Li Q.Q.;
"Arabidopsis mRNA polyadenylation machinery: comprehensive analysis of
protein-protein interactions and gene expression profiling.";
BMC Genomics 9:220-220(2008).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH CPSF30.
PubMed=19573236; DOI=10.1186/1471-2121-10-51;
Rao S., Dinkins R.D., Hunt A.G.;
"Distinctive interactions of the Arabidopsis homolog of the 30 kD
subunit of the cleavage and polyadenylation specificity factor
(AtCPSF30) with other polyadenylation factor subunits.";
BMC Cell Biol. 10:51-51(2009).
[8]
COMPONENT OF CPSF COMPLEX.
PubMed=19748916; DOI=10.1104/pp.109.142729;
Zhao H., Xing D., Li Q.Q.;
"Unique features of plant cleavage and polyadenylation specificity
factor revealed by proteomic studies.";
Plant Physiol. 151:1546-1556(2009).
[9]
INTERACTION WITH FY.
PubMed=19439664; DOI=10.1073/pnas.0903444106;
Manzano D., Marquardt S., Jones A.M., Baurle I., Liu F., Dean C.;
"Altered interactions within FY/AtCPSF complexes required for
Arabidopsis FCA-mediated chromatin silencing.";
Proc. Natl. Acad. Sci. U.S.A. 106:8772-8777(2009).
-!- FUNCTION: CPSF plays a key role in pre-mRNA 3'-end formation,
recognizing the AAUAAA signal sequence and interacting with
poly(A)polymerase and other factors to bring about cleavage and
poly(A) addition (By similarity). Required for antisense-RNA-
mediated gene silencing (PubMed:17008405).
{ECO:0000250|UniProtKB:O17403, ECO:0000269|PubMed:17008405}.
-!- SUBUNIT: Component of the CPSF complex, at least composed of
CPSF160, CPSF100, CPSF73-I, CPSF73-II, CPSF30, FY and FIPS5. Forms
a complex with cleavage and polyadenylation specificity factor
(CPSF) subunits FY, PAPS2, CSTF50, CPSF30, CPSF73-I, CPSF73-II and
CPSF160. {ECO:0000269|PubMed:17008405,
ECO:0000269|PubMed:18479511, ECO:0000269|PubMed:19439664,
ECO:0000269|PubMed:19573236}.
-!- INTERACTION:
Q9FGR0:CPSF160; NbExp=4; IntAct=EBI-1775444, EBI-1775436;
A9LNK9:CPSF30; NbExp=3; IntAct=EBI-1775444, EBI-962511;
Q9C952:CPSF73-I; NbExp=4; IntAct=EBI-1775444, EBI-1775464;
Q8GUU3:CPSF73-II; NbExp=3; IntAct=EBI-1775444, EBI-1775477;
Q6NLV4:FY; NbExp=3; IntAct=EBI-1775444, EBI-1632908;
O82312:PAPS2; NbExp=5; IntAct=EBI-1775444, EBI-1775513;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
{ECO:0000269|PubMed:19573236}. Note=Localized in the cytoplasm
when associated with CPSF30. {ECO:0000269|PubMed:19573236}.
-!- DISRUPTION PHENOTYPE: Impaired antisense-RNA-mediated gene
silencing. Early flowering. {ECO:0000269|PubMed:17008405}.
-!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
RNA-metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF283277; AAF82809.1; -; mRNA.
EMBL; AB005244; BAB10061.1; -; Genomic_DNA.
EMBL; CP002688; AED93228.1; -; Genomic_DNA.
EMBL; AY034982; AAK59487.1; -; mRNA.
EMBL; BT004374; AAO42368.1; -; mRNA.
RefSeq; NP_197776.1; NM_122293.4.
UniGene; At.25191; -.
ProteinModelPortal; Q9LKF9; -.
BioGrid; 17728; 12.
DIP; DIP-40385N; -.
IntAct; Q9LKF9; 9.
STRING; 3702.AT5G23880.1; -.
iPTMnet; Q9LKF9; -.
PaxDb; Q9LKF9; -.
PRIDE; Q9LKF9; -.
EnsemblPlants; AT5G23880.1; AT5G23880.1; AT5G23880.
GeneID; 832453; -.
Gramene; AT5G23880.1; AT5G23880.1; AT5G23880.
KEGG; ath:AT5G23880; -.
Araport; AT5G23880; -.
TAIR; locus:2172843; AT5G23880.
eggNOG; KOG1135; Eukaryota.
eggNOG; COG1236; LUCA.
HOGENOM; HOG000264343; -.
InParanoid; Q9LKF9; -.
KO; K14402; -.
OMA; WKNKESG; -.
OrthoDB; EOG093604D9; -.
PhylomeDB; Q9LKF9; -.
Reactome; R-ATH-72163; mRNA Splicing - Major Pathway.
Reactome; R-ATH-72187; mRNA 3'-end processing.
Reactome; R-ATH-77595; Processing of Intronless Pre-mRNAs.
PRO; PR:Q9LKF9; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q9LKF9; baseline and differential.
Genevisible; Q9LKF9; AT.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; ISS:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009506; C:plasmodesma; IDA:TAIR.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006379; P:mRNA cleavage; ISS:TAIR.
GO; GO:0006378; P:mRNA polyadenylation; ISS:TAIR.
GO; GO:0035194; P:posttranscriptional gene silencing by RNA; IMP:TAIR.
CDD; cd16293; CPSF2-like_MBL-fold; 1.
Gene3D; 3.60.15.10; -; 1.
InterPro; IPR022712; Beta_Casp.
InterPro; IPR027075; CPSF2.
InterPro; IPR025069; Cpsf2_C.
InterPro; IPR035639; CPSF2_MBL.
InterPro; IPR001279; Metallo-B-lactamas.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
InterPro; IPR011108; RMMBL.
PANTHER; PTHR11203:SF5; PTHR11203:SF5; 1.
Pfam; PF10996; Beta-Casp; 1.
Pfam; PF13299; CPSF100_C; 1.
Pfam; PF16661; Lactamase_B_6; 1.
Pfam; PF07521; RMMBL; 1.
SMART; SM01027; Beta-Casp; 1.
SMART; SM00849; Lactamase_B; 1.
SUPFAM; SSF56281; SSF56281; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; mRNA processing; Nucleus;
Reference proteome; RNA-binding.
CHAIN 1 739 Cleavage and polyadenylation specificity
factor subunit 2.
/FTId=PRO_0000074398.
CONFLICT 49 49 S -> P (in Ref. 1; AAF82809).
{ECO:0000305}.
CONFLICT 441 441 I -> V (in Ref. 1; AAF82809).
{ECO:0000305}.
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


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