ID   FIP1_YEAST              Reviewed;         327 AA.
AC   P45976; D6VWR1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Pre-mRNA polyadenylation factor FIP1;
GN   Name=FIP1; OrderedLocusNames=YJR093C; ORFNames=J1911;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INTERACTION WITH PAP1.
RX   PubMed=7736590; DOI=10.1016/0092-8674(95)90391-7;
RA   Preker P.J., Lingner J., Minvielle-Sebastia L., Keller W.;
RT   "The FIP1 gene encodes a component of a yeast pre-mRNA polyadenylation
RT   factor that directly interacts with poly(A) polymerase.";
RL   Cell 81:379-389(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA   Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA   Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA   Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA   Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA   Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA   Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA   Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA   Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA   To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA   von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL   EMBO J. 15:2031-2049(1996).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   INTERACTION WITH PFS2; RNA14 AND YSH1.
RX   PubMed=10619842; DOI=10.1093/emboj/19.1.37;
RA   Ohnacker M., Barabino S.M.L., Preker P.J., Keller W.;
RT   "The WD-repeat protein pfs2p bridges two essential factors within the yeast
RT   pre-mRNA 3'-end-processing complex.";
RL   EMBO J. 19:37-47(2000).
RN   [5]
RP   FUNCTION, AND INTERACTION WITH PAP1 AND YTH1.
RX   PubMed=11238938; DOI=10.1128/mcb.21.6.2026-2037.2001;
RA   Helmling S., Zhelkovsky A., Moore C.L.;
RT   "Fip1 regulates the activity of Poly(A) polymerase through multiple
RT   interactions.";
RL   Mol. Cell. Biol. 21:2026-2037(2001).
RN   [6]
RP   IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY.
RX   PubMed=12819204; DOI=10.1074/jbc.m304454200;
RA   Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T.,
RA   Buratowski S., Moore C.L., Greenblatt J.;
RT   "Organization and function of APT, a subcomplex of the yeast cleavage and
RT   polyadenylation factor involved in the formation of mRNA and small
RT   nucleolar RNA 3'-ends.";
RL   J. Biol. Chem. 278:33000-33010(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   INTERACTION WITH YTH1.
RX   PubMed=12626716; DOI=10.1093/nar/gkg265;
RA   Tacahashi Y., Helmling S., Moore C.L.;
RT   "Functional dissection of the zinc finger and flanking domains of the Yth1
RT   cleavage/polyadenylation factor.";
RL   Nucleic Acids Res. 31:1744-1752(2003).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 80-105 IN COMPLEX WITH PAP1,
RP   SUBUNIT, DOMAIN, AND CIRCULAR DICHROISM.
RX   PubMed=18537269; DOI=10.1021/bi800204k;
RA   Meinke G., Ezeokonkwo C., Balbo P., Stafford W., Moore C., Bohm A.;
RT   "Structure of yeast poly(A) polymerase in complex with a peptide from Fip1,
RT   an intrinsically disordered protein.";
RL   Biochemistry 47:6859-6869(2008).
CC   -!- FUNCTION: Polymerase-regulating component of the cleavage and
CC       polyadenylation factor (CPF) complex, which plays a key role in
CC       polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with
CC       cleavage factors including the CFIA complex and NAB4/CFIB. Pre-mRNA
CC       polyadenylation factor that directly interacts with poly(A) polymerase
CC       PAP1. This inhibits the extension of an oligo(A) primer by limiting
CC       access of the RNA substrate to the C-terminal RNA binding domain of
CC       PAP1. Seems to tether PAP1 to the cleavage factor I.
CC       {ECO:0000269|PubMed:11238938}.
CC   -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC       complex, which is composed of PTI1, SYC1, SSU72, GLC7, MPE1, REF2,
CC       PFS2, PTA1, YSH1/BRR5, SWD2, CFT2/YDH1, YTH1, CFT1/YHH1, FIP1 and PAP1.
CC       In the CPF complex probably interacts directly with PAP1 and YTH1.
CC       Interacts with RNA14. {ECO:0000269|PubMed:10619842,
CC       ECO:0000269|PubMed:11238938, ECO:0000269|PubMed:12626716,
CC       ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:18537269,
CC       ECO:0000269|PubMed:7736590}.
CC   -!- INTERACTION:
CC       P45976; P29468: PAP1; NbExp=9; IntAct=EBI-6940, EBI-12917;
CC       P45976; Q01329: PTA1; NbExp=5; IntAct=EBI-6940, EBI-14145;
CC       P45976; Q06102: YTH1; NbExp=5; IntAct=EBI-6940, EBI-38049;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12819204}.
CC   -!- DOMAIN: Circular dichroism measurements suggest that the protein is
CC       largely unstructured in the absence of interaction with PAP1.
CC       {ECO:0000269|PubMed:18537269}.
CC   -!- MISCELLANEOUS: Present with 1310 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the FIP1 family. {ECO:0000305}.
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DR   EMBL; X83796; CAA58727.1; -; Genomic_DNA.
DR   EMBL; Z49593; CAA89621.1; -; Genomic_DNA.
DR   EMBL; BK006943; DAA08877.1; -; Genomic_DNA.
DR   PIR; A56545; A56545.
DR   RefSeq; NP_012626.1; NM_001181750.1.
DR   PDB; 3C66; X-ray; 2.60 A; C/D=80-105.
DR   PDBsum; 3C66; -.
DR   AlphaFoldDB; P45976; -.
DR   SMR; P45976; -.
DR   BioGRID; 33847; 483.
DR   ComplexPortal; CPX-1053; Cleavage and polyadenylation specificity factor complex.
DR   DIP; DIP-2029N; -.
DR   IntAct; P45976; 37.
DR   MINT; P45976; -.
DR   STRING; 4932.YJR093C; -.
DR   iPTMnet; P45976; -.
DR   MaxQB; P45976; -.
DR   PaxDb; 4932-YJR093C; -.
DR   PeptideAtlas; P45976; -.
DR   EnsemblFungi; YJR093C_mRNA; YJR093C; YJR093C.
DR   GeneID; 853555; -.
DR   KEGG; sce:YJR093C; -.
DR   AGR; SGD:S000003853; -.
DR   SGD; S000003853; FIP1.
DR   VEuPathDB; FungiDB:YJR093C; -.
DR   eggNOG; KOG1049; Eukaryota.
DR   GeneTree; ENSGT00940000162578; -.
DR   HOGENOM; CLU_039307_2_1_1; -.
DR   InParanoid; P45976; -.
DR   OMA; GFNEYTW; -.
DR   OrthoDB; 449619at2759; -.
DR   BioCyc; YEAST:G3O-31720-MONOMER; -.
DR   BioGRID-ORCS; 853555; 10 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P45976; -.
DR   PRO; PR:P45976; -.
DR   Proteomes; UP000002311; Chromosome X.
DR   RNAct; P45976; Protein.
DR   GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:SGD.
DR   GO; GO:0006378; P:mRNA polyadenylation; IDA:ComplexPortal.
DR   GO; GO:0006397; P:mRNA processing; IDA:SGD.
DR   GO; GO:0030846; P:termination of RNA polymerase II transcription, poly(A)-coupled; NAS:ComplexPortal.
DR   DisProt; DP00625; -.
DR   InterPro; IPR007854; Fip1_dom.
DR   PANTHER; PTHR13484; FIP1-LIKE 1 PROTEIN; 1.
DR   PANTHER; PTHR13484:SF0; PRE-MRNA 3'-END-PROCESSING FACTOR FIP1; 1.
DR   Pfam; PF05182; Fip1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; mRNA processing; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..327
FT                   /note="Pre-mRNA polyadenylation factor FIP1"
FT                   /id="PRO_0000215042"
FT   REGION          1..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          272..327
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..313
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         50
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:3C66"
FT   STRAND          87..90
FT                   /evidence="ECO:0007829|PDB:3C66"
FT   STRAND          93..95
FT                   /evidence="ECO:0007829|PDB:3C66"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:3C66"
FT   HELIX           99..102
FT                   /evidence="ECO:0007829|PDB:3C66"
SQ   SEQUENCE   327 AA;  35777 MW;  471CA2B0CDF99D0A CRC64;
     MSSSEDEDDK FLYGSDSELA LPSSKRSRDD EADAGASSNP DIVKRQKFDS PVEETPATAR
     DDRSDEDIYS DSSDDDSDSD LEVIISLGPD PTRLDAKLLD SYSTAATSSS KDVISVATDV
     SNTITKTSDE RLITEGEANQ GVTATTVKAT ESDGNVPKAM TGSIDLDKEG IFDSVGITTI
     DPEVLKEKPW RQPGANLSDY FNYGFNEFTW MEYLHRQEKL QQDYNPRRIL MGLLSLQQQG
     KLNSANDTDS NLGNIIDNNN NVNNANMSNL NSNMGNSMSG TPNPPAPPMH PSFPPLPMFG
     SFPPFPMPGM MPPMNQQPNQ NQNQNSK
//