| General information | | DisProt: | DP00625 | | Name: | Pre-mRNA polyadenylation factor FIP1 | | Synonym(s): | FIP1_YEAST
FIP1
| | First appeared in release: | Release 5.5 (11/17/2010) | | UniProt: | P45976 | | UniGene: | | | SwissProt: | FIP1_YEAST | | TrEMBL: | | | NCBI (GI): | 1169683 | | Source organism: | Saccharomyces cerevisiae (Baker's yeast) | | Sequence length: | 327 | | Percent disordered: | 8% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MSSSEDEDDK FLYGSDSELA LPSSKRSRDD EADAGASSNP DIVKRQKFDS PVEETPATAR - 60
DDRSDEDIYS DSSDDDSDSD LEVIISLGPD PTRLDAKLLD SYSTAATSSS KDVISVATDV - 120
SNTITKTSDE RLITEGEANQ GVTATTVKAT ESDGNVPKAM TGSIDLDKEG IFDSVGITTI - 180
DPEVLKEKPW RQPGANLSDY FNYGFNEFTW MEYLHRQEKL QQDYNPRRIL MGLLSLQQQG - 240
KLNSANDTDS NLGNIIDNNN NVNNANMSNL NSNMGNSMSG TPNPPAPPMH PSFPPLPMFG - 300
SFPPFPMPGM MPPMNQQPNQ NQNQNSK
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| Functional narrative |
Polymerase-regulating component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | Pap1 binding domain | | Location: | 80 - 105 | | Length: | 26 | | Region sequence: |
DLEVIISLGPDPTRLDAKLLDSYSTA | | Modification type: | Fragment
| | PDB: | 3C66:A, 3C66:B | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | | | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, near-UV (278 K; pH: 7.5; cuvette 0.1 cm; Jasco J-810 (spectropolarimeter ); protein (stock dilution) 600 x; resolution 2.6 A; Tris 5 mM)
- Sensitivity to proteolysis (pH: 7.5; CaCl2 1 mM; concentrated Fip220 (protein) 0.5 mg/mL; glycerol 10 %; MgCl2 1 mM; NaCl 100 mM; Tris (buffer) 20 mM)
- Analytical ultracentrifugation (293 K; pH: 7.5; BeckmanCoulter XL-I (analytical ultracentrifuge); NaCl 100 mM; speed 50000 rpm; Tris (buffer) 100 mM)
- Dynamic light scattering (298 K; pH: 7.5; NaCl 100 mM; PD2000 instrument )
| References:
- Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. "Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein." 2008; 47(26): 6859-6869. PubMed: 18537269
| Comments:According to Meinke, et al (2008), loops appear at aa 85-91 and 97-103.
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| Comments |
Sent for AV 10-26-2010 (PubMed: 18537269)
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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