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UniProtKB/Swiss-Prot entry P29468


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PAP_YEAST
Primary accession number P29468
Secondary accession numbers None
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 1, 1993 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Poly(A) polymerase
Synonyms PAP
EC 2.7.7.19
Polynucleotide adenylyltransferase
Gene name
Name: PAP1
OrderedLocusNames: YKR002W
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 204510 / AB320;
DOI=10.1038/354496a0; PubMed=1840648 [NCBI, ExPASy, EBI, Israel, Japan]
Lingner J., Kellermann J., Keller W.;
"Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae.";
Nature 354:496-498(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1441752 [NCBI, ExPASy, EBI, Israel, Japan]
Duesterhoeft A., Philippsen P.;
"DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames.";
Yeast 8:749-759(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1038/369371a0; PubMed=8196765 [NCBI, ExPASy, EBI, Israel, Japan]
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[4]
INTERACTION WITH FIR1.
DOI=10.1007/s004380050491; PubMed=9236779 [NCBI, ExPASy, EBI, Israel, Japan]
del Olmo M., Mizrahi N., Gross S., Moore C.L.;
"The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts.";
Mol. Gen. Genet. 255:209-218(1997).
[5]
IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1074/jbc.M304454200; PubMed=12819204 [NCBI, ExPASy, EBI, Israel, Japan]
Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J.;
"Organization and function of APT, a subcomplex of the yeast cleavage and polyadenylation factor involved in the formation of mRNA and small nucleolar RNA 3'-ends.";
J. Biol. Chem. 278:33000-33010(2003).
[6]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-548, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[8]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537.
DOI=10.1126/science.289.5483.1346; PubMed=10958780 [NCBI, ExPASy, EBI, Israel, Japan]
Bard J., Zhelkovsky A.M., Helmling S., Earnest T.N., Moore C.L., Bohm A.;
"Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.";
Science 289:1346-1349(2000).
Comments
  • FUNCTION: Polymerase 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.
  • CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: 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. Interacts with FIR1.
  • SUBCELLULAR LOCATION: Nucleus.
  • MISCELLANEOUS: Present with 17100 molecules/cell in log phase SD medium.
  • SIMILARITY: Belongs to the poly(A) polymerase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X60307; CAA42852.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X65124; CAA46250.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z28227; CAA82072.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S19031; S19031.
RefSeq NP_012927.1; -.
3D structure databases
PDB
1FA0; X-ray; 2.60 A; A/B=1-537.[ExPASy / RCSB / EBI]
2HHP; X-ray; 1.80 A; A=1-530.[ExPASy / RCSB / EBI]
2O1P; X-ray; 2.70 A; A/B=1-542.[ExPASy / RCSB / EBI]
2Q66; X-ray; 1.80 A; A=5-529.[ExPASy / RCSB / EBI]
3C66; X-ray; 2.60 A; A/B=1-537.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FA0; -.
2HHP; -.
2O1P; -.
2Q66; -.
3C66; -.
ModBase P29468.
Protein-protein interaction databases
DIP DIP:2297N; -.
Organism-specific databases
CYGD YKR002w; -.
SGD S000001710; PAP1.
Yeast-GFP YKR002W.
Gene expression databases
ArrayExpress P29468; -.
GermOnline YKR002W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005847; Cellular component: mRNA cleavage and polyadenylation specificity factor complex (inferred from physical interaction from SGD).
GO:0004652; Molecular function: polynucleotide adenylyltransferase activity (inferred from electronic annotation from InterPro).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from InterPro).
GO:0006406; Biological process: mRNA export from nucleus (inferred from mutant phenotype from SGD).
GO:0006378; Biological process: mRNA polyadenylation (inferred from direct assay from SGD).
GO:0006350; Biological process: transcription (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002934; Nucleotidyltransferase.
IPR007012; PolA_pol_centr.
IPR007010; PolA_pol_RNA-bd.
IPR014492; PolyA_polymerase.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.590; PolA_pol_RNA-bd; 1.
Pfam PF01909; NTP_transf_2; 1.
PF04928; PAP_central; 1.
PF04926; PAP_RNA-bind; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF018425; PolyA_polymerase; 1.
BLOCKS P29468.
ProtoNet P29468.
Proteomic databases
PeptideAtlas P29468; -.
Genome annotation databases
Ensembl YKR002W; Saccharomyces cerevisiae. [Contig view]
GeneID 853871; -.
GenomeReviews Y13137_GR; YKR002W.
KEGG sce:YKR002W; -.
NMPDR fig|4932.3.peg.3913; -.
Phylogenomic databases
HOGENOM P29468; -.
Other
LinkHub P29468; -.
NextBio 975142; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; mRNA processing; Nucleus; Phosphoprotein; RNA-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   568  568     Poly(A) polymerase. PRO_0000051621
ACT_SITE   100   100         
ACT_SITE   102   102         
ACT_SITE   154   154         
MOD_RES   452   452        Phosphoserine. 
MOD_RES   548   548        Phosphoserine. 
HELIX   5     7  3      
HELIX   20    35  16      
HELIX   42    69  28      
HELIX   74    79  6      
STRAND   83    87  5      
HELIX   88    92  5      
STRAND   101   107  7      
HELIX   113   125  13      
STRAND   130   136  7      
STRAND   139   141  3      
STRAND   143   148  6      
STRAND   151   159  9      
STRAND   161   163  3      
HELIX   174   177  4      
HELIX   182   200  19      
HELIX   204   220  17      
HELIX   226   228  3      
HELIX   233   246  14      
HELIX   252   265  14      
STRAND   272   275  4      
TURN   289   291  3      
HELIX   293   296  4      
STRAND   305   308  4      
TURN   312   315  4      
HELIX   318   339  22      
HELIX   345   348  4      
HELIX   354   357  4      
STRAND   359   370  12      
HELIX   372   394  23      
STRAND   399   404  6      
STRAND   409   414  6      
STRAND   417   419  3      
HELIX   420   427  8      
HELIX   431   434  4      
STRAND   458   470  13      
HELIX   482   494  13      
TURN   497   500  4      
STRAND   502   513  12      
HELIX   514   516  3      
HELIX   519   521  3      
Sequence information
Length: 568 AA [This is the length of the unprocessed precursor] Molecular weight: 64552 Da [This is the MW of the unprocessed precursor] CRC64: 759DE5210DC8D881 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSSQKVFGIT GPVSTVGATA AENKLNDSLI QELKKEGSFE TEQETANRVQ VLKILQELAQ 

        70         80         90        100        110        120 
RFVYEVSKKK NMSDGMARDA GGKIFTYGSY RLGVHGPGSD IDTLVVVPKH VTREDFFTVF 

       130        140        150        160        170        180 
DSLLRERKEL DEIAPVPDAF VPIIKIKFSG ISIDLICARL DQPQVPLSLT LSDKNLLRNL 

       190        200        210        220        230        240 
DEKDLRALNG TRVTDEILEL VPKPNVFRIA LRAIKLWAQR RAVYANIFGF PGGVAWAMLV 

       250        260        270        280        290        300 
ARICQLYPNA CSAVILNRFF IILSEWNWPQ PVILKPIEDG PLQVRVWNPK IYAQDRSHRM 

       310        320        330        340        350        360 
PVITPAYPSM CATHNITEST KKVILQEFVR GVQITNDIFS NKKSWANLFE KNDFFFRYKF 

       370        380        390        400        410        420 
YLEITAYTRG SDEQHLKWSG LVESKVRLLV MKLEVLAGIK IAHPFTKPFE SSYCCPTEDD 

       430        440        450        460        470        480 
YEMIQDKYGS HKTETALNAL KLVTDENKEE ESIKDAPKAY LSTMYIGLDF NIENKKEKVD 

       490        500        510        520        530        540 
IHIPCTEFVN LCRSFNEDYG DHKVFNLALR FVKGYDLPDE VFDENEKRPS KKSKRKNLDA 

       550        560 
RHETVKRSKS DAASGDNING TTAAVDVN 

P29468 in FASTA format

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