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Pre-mRNA cleavage complex 2 protein Pcf11
Known also as: Pre-mRNA cleavage complex II protein Pcf11
Known abbreviations: PCF11, hPcf11, KIAA0824
Yeast homolog: PCF11
Protein
Models Domains Secondary structure NTD, CTD |
This protein is highly disordered (87 % of residues are predicted to be disordered)
Top 3 models:
 |  |  |
| Template: 1sz9, chain A Method: hhsearch Fragment: 11-146 | Template: 3dxj, chain N Method: compass Fragment: 36-456 | Template: 2c3f, chain A Method: mgenthreader Fragment: 336-629 |
| Sequence length: | 1555 aa |
| Molecular weight: | 173.05 kDa |
| Isoelectric point: | 8.52 |
Sequence:
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MSEQTPAEAGAAGAREDACRDYQSSLEDLTFNSKPHINMLTILAEENLPFAKEIVSLIEAQTAKAPSSEKLPVMYLMDSIVKNVGREYLTAFTKNLVATFICVFEKVDENTRKSLFKLRSTWDEIFPLKK
LYALDVRVNSLDPAWPIKPLPPNVNTSSIHVNPKFLNKSPEEPSTPGTVVSSPSISTPPIVPDIQKNLTQEQLIRQQLLAKQKQLLELQQKKLELELEQAKAQLAVSLSVQQETSNLGPGSAPSKLHVSQ
IPPMAVKAPHQVPVQSEKSRPGPSLQIQDLKGTNRDPRLNRISQHSHGKDQSHRKEFLMNTLNQSDTKTSKTIPSEKLNSSKQEKSKSGEKITKKELDQLDSKSKSKSKSPSPLKNKLSHTKDLKNQESE
SMRLSDMNKRDPRLKKHLQDKTDGKDDDVKEKRKTAEKKDKDEHMKSSEHRLAGSRNKIINGIVQKQDTITEESEKQGTKPGRSSTRKRSRSRSPKSRSPIIHSPKRRDRRSPKRRQRSMSPTSTPKAGK
IRQSGAKQSHMEEFTPPSREDRNAKRSTKQDIRDPRRMKKTEEERPQETTNQHSTKSGTEPKENVENWQSSKSAKRWKSGWEENKSLQQVDEHSKPPHLRHRESWSSTKGILSPRAPKQQQHRLSVDANL
QIPKELTLASKRELLQKTSERLASGEITQDDFLVVVHQIRQLFQYQEGVREEQRSPFNDRFPLKRPRYEDSDKPFVDSPASRFAGLDTNQRLTALAEDRPLFDGPSRPSVARDGPTKMIFEGPNKLSPRI
DGPPTPASLRFDGSPGQMGGGGPLRFEGPQGQLGGGCPLRFEGPPGPVGTPLRFEGPIGQAGGGGFRFEGSPGLRFEGSPGGLRFEGPGGQPVGGLRFEGHRGQPVGGLRFEGPHGQPVGGLRFDNPRGQ
PVGGLRFEGGHGPSGAAIRFDGPHGQPGGGIRFEGPLLQQGVGMRFEGPHGQSVAGLRFEGQHNQLGGNLRFEGPHGQPGVGIRFEGPLVQQGGGMRFEGPSVPGGGLRIEGPLGQGGPRFEGCHALRFD
GQPGQPSLLPRFDGLHGQPGPRFERTPGQPGPQRFDGPPGQQVQPRFDGVPQRFDGPQHQQASRFDIPLGLQGTRFDNHPSQRLESVSFNQTGPYNDPPGNAFNAPSQGLQFQRHEQIFDSPQGPNFNGP
HGPGNQSFSNPLNRASGHYFDEKNLQSSQFGNFGNIPAPMTVGNIQASQQVLSGVAQPVAFGQGQQFLPVHPQNPGFVQNPSGALPKAYPDNHLSQVDVNELFSKLLKTGILKLSQTDSATTQVSEVTAQ
PPPEEEEDQNEDQDVPDLTNFTVEELKQRYDSVINRLYTGIQCYSCGMRFTTSQTDVYADHLDWHYRQNRTEKDVSRKVTHRRWYYSLTDWIEFEEIADLEERAKSQFFEKVHEEVVLKTQEAAKEKEFQ
SVPAGPAGAVESCEICQEQFEQYWDEEEEEWHLKNAIRVDGKIYHPSCYEDYQNTSSFDCTPSPSKTPVENPLNIMLNIVKNELQEPCDSPKVKEERIDTPPACTEESIATPSEIKTENDTVESV
Gene location: 11q13
Summary
Component of pre-mRNA cleavage complex II. Functions as a scaffold for the processing machinery during the termination and polyadenylation of transcripts.
Yeast Pcf11p is only about half the size of hPcf11, and is equivalent to the N-terminal half of hPcf11. The function of the C-terminal half of hPcf11 is not known.
Pcf11p contains a conserved PolII CTD interacting domain (CID) that covers ~130 residues in the N-terminus, which prefers the phosphorylated form of the CTD. The crystal structure of Pcf11p in complex with a phosphorylated CTD peptide has been reported. Mutations in the CID reduce or abolish binding to the CTD and result in cell death. Interestingly, these mutations do not affect 3?-end processing, but instead cause incorrect transcriptional termination (can also bind RNA to affect transcriptional termination). Studies of the CID indicate that the RNA binding and the protein binding regions overlap, and this competition for binding may play a role in the release of the 3?-end processing factors from PolII.
The CID is followed by a 20-residue stretch of glutamines (234–253 in Pcf11p), which is followed by the Rna14p/Rna15p binding domain. The binding of Rna14p/Rna15p to Pcf11p is dependent on the binding of Clp1p first. This CstF binding region is followed by the Clp1 interacting segment (477–499), which is flanked by a zinc finger on each side (N-terminal C2H2 and C-terminal C2HC type). Pcf11p also interacts with Cft1p/ Yhh1p, Cft2p/Y.
See this protein in other databases:
Literature:
- de Vries H, Ruegsegger U, Hubner W et al. Human pre-mRNA cleavage factor II(m) contains homologs of yeast proteins and bridges two other cleavage factors. EMBO J 2000 19(21):5895-904, doi: 10.1093/emboj/19.21.5895, PMID: 11060040.
- Hollingworth D, Kelly G, Frenkiel TA et al. Backbone assignment of PCF11 CTD binding domain. J Biomol NMR 2005 31(4):363, doi: 10.1007/s10858-005-1392-1, PMID: 15929005.
- Noble CG, Beuth B, Taylor IA et al. Structure of a nucleotide-bound Clp1-Pcf11 polyadenylation factor. Nucleic Acids Res 2007 35(1):87-99, doi: 10.1093/nar/gkl1010, PMID: 17151076.
- West S, Proudfoot NJ. Human Pcf11 enhances degradation of RNA polymerase II-associated nascent RNA and transcriptional termination. Nucleic Acids Res 2008 36(3):905-14, doi: 10.1093/nar/gkm1112, PMID: 18086705.
- Seoane S, Lamas-Maceiras M, Rodriguez-Torres AM et al. Involvement of Pta1, Pcf11 and a KlCYC1 AU-rich element in alternative RNA 3"-end processing selection in yeast. FEBS Lett 2009 583(17):2843-8, doi: 10.1016/j. febslet.2009.07.042, PMID: 19646984.
- Ghazy MA, Gordon JM, Lee SD et al. The interaction of Pcf11 and Clp1 is needed for mRNA 3"-end formation and is modulated by amino acids in the ATP-binding site. Nucleic Acids Res 2012 40(3):1214-25, doi: 10.1093/nar/gkr801, PMID: 21993299.
- Amrani N, Minet M, Wyers F et al. PCF11 encodes a third protein component of yeast cleavage and polyadenylation factor I. Mol Cell Biol 1997 17(3):1102-9, doi: , PMID: 9032237.
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