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UniProtKB/Swiss-Prot entry P25500

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

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Entry information
Entry name PAPOA_BOVIN
Primary accession number P25500
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 77)
Name and origin of the protein
Protein name Poly(A) polymerase alpha
Synonyms PAP-alpha
EC 2.7.7.19
Polynucleotide adenylyltransferase alpha
Gene name
Name: PAPOLA
Synonyms: PAP
From
Bos taurus (Bovine) [TaxID: 9913] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; Pecora; Bovidae; Bovinae; Bos.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN SEQUENCE OF 1-21; 207-255 AND 386-397.
TISSUE=Thymus;
PubMed=1756732 [NCBI, ExPASy, EBI, Israel, Japan]
Wahle E., Martin G., Schiltz E., Keller W.;
"Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase.";
EMBO J. 10:4251-4257(1991).
[2]
 SEQUENCE REVISION.
Wahle E.;
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
[3]
 NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 97-103 AND 445-468.
TISSUE=Heart muscle;
DOI=10.1038/353229a0; PubMed=1896071 [NCBI, ExPASy, EBI, Israel, Japan]
Raabe T., Bollum F.J., Manley J.L.;
"Primary structure and expression of bovine poly(A) polymerase.";
Nature 353:229-234(1991).
[4]
 DOMAINS, ACTIVE SITES, AND MUTAGENESIS.
PubMed=8665867 [NCBI, ExPASy, EBI, Israel, Japan]
Martin G., Keller W.;
"Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases.";
EMBO J. 15:2593-2603(1996).
[5]
 X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1093/emboj/19.16.4193; PubMed=10944102 [NCBI, ExPASy, EBI, Israel, Japan]
Martin G., Keller W., Doublie S.;
"Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP.";
EMBO J. 19:4193-4203(2000).
Comments
  • FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus.
  • CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
  • SUBUNIT: Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with NUDT21/CPSF5 and FIP1L1 (By similarity).
  • SUBCELLULAR LOCATION: Nucleus.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
    NameLong
    Isoform IDP25500-1
    This is the isoform sequence displayed in this entry.
    NameShort
    Isoform IDP25500-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_004524, VSP_004525, VSP_004526.
  • PTM: Phosphorylated. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF.
  • 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
X61585; CAA43782.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63436; CAA45031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S17875; S17875.
S17925; S17925.
S18642; S18642.
RefSeq NP_788820.1; -.
UniGene Bt.59483
3D structure databases
PDB
1F5A; X-ray; 2.50 A; A=1-513.[ExPASy / RCSB / EBI]
1Q78; X-ray; 2.80 A; A=1-514.[ExPASy / RCSB / EBI]
1Q79; X-ray; 2.15 A; A=1-514.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1F5A; -.
1Q78; -.
1Q79; -.
ModBase P25500.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from InterPro).
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:0006397; Biological process: mRNA processing (inferred from electronic annotation from UniProtKB-KW).
GO:0043631; Biological process: RNA polyadenylation (inferred from electronic annotation from InterPro).
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.
ProtoNet P25500.
Genome annotation databases
Ensembl ENSBTAG00000004054; Bos taurus. [Contig view]
GeneID 338051; -.
KEGG bta:338051; -.
Phylogenomic databases
HOVERGEN P25500; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Direct protein sequencing; mRNA processing; Nucleus; Phosphoprotein; RNA-binding; Transferase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   739  738     Poly(A) polymerase alpha. PRO_0000051611
MOTIF   490   507  18     Nuclear localization signal 1. 
MOTIF   644   659  16     Nuclear localization signal 2. 
ACT_SITE   113   113         
ACT_SITE   115   115         
ACT_SITE   167   167         
MOD_RES   24    24        Phosphoserine (By similarity). 
MOD_RES   553   553        Phosphoserine (By similarity). 
VAR_SEQ   663   683        Missing (in isoform Short). VSP_004524
VAR_SEQ   709   710        KT -> II (in isoform Short). VSP_004525
VAR_SEQ   711   739        Missing (in isoform Short). VSP_004526
CONFLICT   80    80        S -> R (in Ref. 3; CAA45031). 
STRAND   21    23  3      
HELIX   33    46  14      
HELIX   47    49  3      
HELIX   55    82  28      
HELIX   87    90  4      
STRAND   96   100  5      
HELIX   101   105  5      
STRAND   114   120  7      
HELIX   126   129  4      
HELIX   132   138  7      
STRAND   143   149  7      
STRAND   152   154  3      
STRAND   156   161  6      
STRAND   164   172  9      
STRAND   176   178  3      
HELIX   187   190  4      
HELIX   195   211  17      
STRAND   213   215  3      
HELIX   217   233  17      
TURN   239   242  4      
HELIX   246   259  14      
HELIX   265   277  13      
TURN   302   304  3      
HELIX   306   310  5      
STRAND   318   321  4      
TURN   325   328  4      
HELIX   331   352  22      
HELIX   358   361  4      
HELIX   367   370  4      
STRAND   372   383  12      
HELIX   384   395  12      
HELIX   398   406  9      
STRAND   411   416  6      
STRAND   433   443  11      
HELIX   457   473  17      
STRAND   482   489  8      
HELIX   490   493  4      
HELIX   494   496  3      
Sequence information
Length: 739 AA [This is the length of the unprocessed precursor] Molecular weight: 82441 Da [This is the MW of the unprocessed precursor] CRC64: 7C89C15E33232CFF [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG VFEEEEELQR 

        70         80         90        100        110        120 
RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA 

       130        140        150        160        170        180 
PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE 

       190        200        210        220        230        240 
DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI 

       250        260        270        280        290        300 
LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW 

       310        320        330        340        350        360 
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK 

       370        380        390        400        410        420 
LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS 

       430        440        450        460        470        480 
FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD 

       490        500        510        520        530        540 
MKIAAMHVKR KQLHQLLPSH VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS 

       550        560        570        580        590        600 
AMKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT 

       610        620        630        640        650        660 
QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH KEESPKKTKT 

       670        680        690        700        710        720 
EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT ATSLLASQKT SSTDLSDIPA 

       730 
LPANPIPVIK NSIKLRLNR
P25500 in FASTA format

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