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Cleavage stimulation factor subunit 3
Known also as: Cleavage stimulation factor 77 kDa subunit
Known abbreviations: CSTF3, CstF-77
Yeast homolog: RNA14
Protein
Models Domains Secondary structure Disorder |
Top 3 models:
 |  |  |
| Template: 2ooe, chain A Method: mgenthreader Fragment: 20-548 | Template: 2pff, chain A Method: compass Fragment: 286-704 | Template: 2uy1, chain A Method: hhsearch Fragment: 32-580 |
This protein has alternative isoforms:
Isoform 1:
| Sequence length: | 717 aa |
| Molecular weight: | 82.922 kDa |
| Isoelectric point: | 8.06 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEIKAKNYDKVEKLFQRCLMKVLHIDLWKCYLSYVRETKGKLPSYKEKMAQAYDFAL
DKIGMEIMSYQIWVDYINFLKGVEAVGSYAENQRITAVRRVYQRGCVNPMINIEQLWRDYNKYEEGINIHLAKKMIEDRSRDYMNARRVAKEYETVMKGLDRNAPSVPPQNTPQEAQQVDMWKKYIQWEK
SNPLRTEDQTLITKRVMFAYEQCLLVLGHHPDIWYEAAQYLEQSSKLLAEKGDMNNAKLFSDEAANIYERAISTLLKKNMLLYFAYADYEESRMKYEKVHSIYNRLLAIEDIDPTLVYIQYMKFARRAEG
IKSGRMIFKKAREDTRTRHHVYVTAALMEYYCSKDKSVAFKIFELGLKKYGDIPEYVLAYIDYLSHLNEDNNTRVLFERVLTSGSLPPEKSGEIWARFLAFESNIGDLASILKVEKRRFTAFKEEYEGKE
TALLVDRYKFMDLYPCSASELKALGYKDVSRAKLAAIIPDPVVAPSIVPVLKDEVDRKPEYPKPDTQQMIPFQPRHLAPPGLHPVPGGVFPVPPAAVVLMKLLPPPICFQGPFVQVDELMEIFRRCKIPN
TVEEAVRIITGGAPELAVEGNGPVESNAVLTKAVKRPNEDSDEDEEKGAVVPPVHDIYRARQQKRIR
Isoform 2:
| Sequence length: | 103 aa |
| Molecular weight: | 12.102 kDa |
| Isoelectric point: | 6.94 |
1........10........20........30........40........50........60........70........80........90........100.......110.......120.......130
MSGDGATEQAAEYVPEKVKKAEKKLEENPYDLDAWSILIREAQNQPIDKARKTYERLVAQFPSSGRFWKLYIEAEVTILFYFFLYQYCSIHCSDRKQVRNIAN
Gene location: 11p13
Summary
The CSTF-77 protein functions as a homodimer and interacts directly with both CSTF1 and CSTF2 in the CSTF complex. CstF-77 is required for proper 3?-end cleavage.
Mutation of the Drosophila homolog of CstF-77, suppressor of forked su(f), results in the utilization of alternative poly(A) sites. This defect can be rescued by the addition of human CstF-77.
CstF-77 contains 12 repeated sequences at the N-terminus, which are called HAT (half a TPR) motifs for their similarity to tetratricopeptide repeat (TPR) motifs. TPR motifs often mediate protein-protein interactions. Structural and biochemical data suggest that the HAT domain can be further divided into two sub-domains, HAT-N domain (residues 1– 240, with HAT motifs 1 through 5) and HAT-C domain (residues 241–549, HAT motifs 6 through 12). Most importantly, the structures reveal that the HAT domain is an intimately associated dimer, mediated by the HAT-C domain. The data suggest that CstF-77 may function as a dimer at a crucial stage in pre-mRNA 3?-end processing. The HAT domain is followed by a proline-rich segment in CstF-77. Far Western experiments showed that this segment binds the hinge region of CstF-64 and the WD-40 repeats of CstF-50. Electron microscopy and AUC experiments showed that Rna14p and Rna15p can form a heterotetramer. CstF-77 binds specifically to the CTD of PolII but with less efficiency than CstF-50. Rna14p binds to unphosphorylated CTD, but the binding increases upon phosphorylation of the CTD.
Acts as a homodimer.
CSTF3 directly interacts with CSTF1 and CSTF2.
Interacts with FIP1L1.
See this protein in other databases:
Literature:
- Takagaki Y, Manley JL. Complex protein interactions within the human polyadenylation machinery identify a novel component. Mol Cell Biol 2000 20(5):1515-25, doi: , PMID: 10669729.
- Rouget C, Papin C, Mandart E et al. Cytoplasmic CstF-77 protein belongs to a masking complex with cytoplasmic polyadenylation element-binding protein in Xenopus oocytes. J Biol Chem 2006 281(39):28687-98, doi: 10.1074/jbc.M601116200, PMID: 16882666.
- Bai Y, Auperin TC, Chou CY et al. Crystal structure of murine CstF-77: dimeric association and implications for polyadenylation of mRNA precursors. Mol Cell 2007 25(6):863-75, doi: 10.1016/j.molcel.2007.01.034, PMID: 17386263.
- Legrand P, Pinaud N, Minvielle-Sebastia L et al. The structure of the CstF-77 homodimer provides insights into CstF assembly. Nucleic Acids Res 2007 35(13):4515-22, doi: 10.1093/nar/gkm458, PMID: 17584787.
- Ruepp MD, Schweingruber C, Kleinschmidt N et al. Interactions of CstF-64, CstF-77, and symplekin: implications on localisation and function. Mol Biol Cell 2011 22(1):91-104, doi: 10.1091/mbc.E10-06-0543, PMID: 21119002.
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