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Protein

Pre-mRNA polyadenylation factor FIP1

Gene

FIP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

Miscellaneous

Present with 1310 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • protein binding, bridging Source: SGD

GO - Biological processi

  • mRNA polyadenylation Source: SGD
  • pre-mRNA cleavage required for polyadenylation Source: SGD

Keywordsi

Biological processmRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-31720-MONOMER
ReactomeiR-SCE-77595 Processing of Intronless Pre-mRNAs

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA polyadenylation factor FIP1
Gene namesi
Name:FIP1
Ordered Locus Names:YJR093C
ORF Names:J1911
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJR093C
SGDiS000003853 FIP1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002150421 – 327Pre-mRNA polyadenylation factor FIP1Add BLAST327

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei50PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP45976
PaxDbiP45976
PRIDEiP45976

PTM databases

iPTMnetiP45976

Interactioni

Subunit structurei

Component of the cleavage and polyadenylation factor (CPF) complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2, PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1. In the CPF complex probably interacts directly with PAP1 and YTH1. Interacts with RNA14.6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • protein binding, bridging Source: SGD

Protein-protein interaction databases

BioGridi33847, 480 interactors
ComplexPortaliCPX-1053 Cleavage and polyadenylation specificity factor complex
DIPiDIP-2029N
IntActiP45976, 37 interactors
MINTiP45976
STRINGi4932.YJR093C

Structurei

Secondary structure

1327
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi83 – 85Combined sources3
Beta strandi87 – 90Combined sources4
Beta strandi93 – 95Combined sources3
Helixi96 – 98Combined sources3
Helixi99 – 102Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3C66X-ray2.60C/D80-105[»]
DisProtiDP00625
ProteinModelPortaliP45976
SMRiP45976
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45976

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi61 – 80Asp-rich (acidic)Add BLAST20
Compositional biasi258 – 266Poly-Asn9
Compositional biasi284 – 318Pro-richAdd BLAST35

Domaini

Circular dichroism measurements suggest that the protein is largely unstructured in the absence of interaction with PAP1.1 Publication

Sequence similaritiesi

Belongs to the FIP1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00730000111028
HOGENOMiHOG000000819
InParanoidiP45976
KOiK14405
OMAiQAMMQQM
OrthoDBiEOG092C4SHL

Family and domain databases

InterProiView protein in InterPro
IPR007854 Fip1
PfamiView protein in Pfam
PF05182 Fip1, 1 hit

Sequencei

Sequence statusi: Complete.

P45976-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSEDEDDK FLYGSDSELA LPSSKRSRDD EADAGASSNP DIVKRQKFDS
60 70 80 90 100
PVEETPATAR DDRSDEDIYS DSSDDDSDSD LEVIISLGPD PTRLDAKLLD
110 120 130 140 150
SYSTAATSSS KDVISVATDV SNTITKTSDE RLITEGEANQ GVTATTVKAT
160 170 180 190 200
ESDGNVPKAM TGSIDLDKEG IFDSVGITTI DPEVLKEKPW RQPGANLSDY
210 220 230 240 250
FNYGFNEFTW MEYLHRQEKL QQDYNPRRIL MGLLSLQQQG KLNSANDTDS
260 270 280 290 300
NLGNIIDNNN NVNNANMSNL NSNMGNSMSG TPNPPAPPMH PSFPPLPMFG
310 320
SFPPFPMPGM MPPMNQQPNQ NQNQNSK
Length:327
Mass (Da):35,777
Last modified:November 1, 1995 - v1
Checksum:i471CA2B0CDF99D0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83796 Genomic DNA Translation: CAA58727.1
Z49593 Genomic DNA Translation: CAA89621.1
BK006943 Genomic DNA Translation: DAA08877.1
PIRiA56545
RefSeqiNP_012626.1, NM_001181750.1

Genome annotation databases

EnsemblFungiiYJR093C; YJR093C; YJR093C
GeneIDi853555
KEGGisce:YJR093C

Similar proteinsi

Entry informationi

Entry nameiFIP1_YEAST
AccessioniPrimary (citable) accession number: P45976
Secondary accession number(s): D6VWR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 20, 2018
This is version 137 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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