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Q61183 (PAPOA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) polymerase alpha

Short name=PAP-alpha
EC=2.7.7.19
Alternative name(s):
Polynucleotide adenylyltransferase
Gene names
Name:Papola
Synonyms:Pap, Plap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length739 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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 By similarity. Ref.4 Ref.5

Catalytic activity

ATP + RNA(n) = diphosphate + RNA(n+1).

Cofactor

Binds 2 magnesium ions. Also active with manganese By similarity.

Subunit structure

Monomer. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts with FIP1L1 By similarity. Interacts with NUDT21; the interaction is diminished by acetylation. Interacts with KPNB1; the interaction promotes PAP nuclear import and is inhibited by acetylation of PAP By similarity. Ref.3

Subcellular location

Nucleus By similarity Ref.4.

Tissue specificity

Expressed in brain, thymus, lung, kidney, bladder, testis and spleen. Ref.4

Post-translational modification

Polysumoylated. Varying sumolyation depending on tissue- and cell-type. Highly sumoylated in bladder and NIH 3T3 cells. Sumoylation is required for nuclear localization and enhances PAP stability. Desumoylated by SENP1. Inhibits polymerase activity. Ref.4

Hyperphosphorylation on multiple CDK2 consensus and non-consensus sites in the C-terminal Ser/Thr-rich region represses PAP activity in late M-phase. Phosphorylation/dephosphorylation may regulate the interaction between PAP and CPSF By similarity.

Acetylated in the C-terminus. Acetylation decreases interaction with NUDT21 and KPNB1, and inhibits nuclear localization through inhibiting binding to the importin alpha/beta complex By similarity.

Sequence similarities

Belongs to the poly(A) polymerase family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q61183-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q61183-2)

Also known as: III;

The sequence of this isoform differs from the canonical sequence as follows:
     373-375: HYI → YVK
     376-739: Missing.
Isoform 3 (identifier: Q61183-3)

Also known as: V;

The sequence of this isoform differs from the canonical sequence as follows:
     305-317: NPSDRYHLMPIIT → SVLFFPLQIHTIQ
     318-375: Missing.
Isoform 4 (identifier: Q61183-4)

Also known as: VI;

The sequence of this isoform differs from the canonical sequence as follows:
     280-293: EWPNPVLLKQPEEC → YVFRLYYNKIDCRH
     294-375: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 739739Poly(A) polymerase alpha
PRO_0000051613

Regions

Nucleotide binding100 – 1023ATP By similarity
Nucleotide binding113 – 1153ATP By similarity
Nucleotide binding246 – 2472ATP By similarity
Region508 – 643136Ser/Thr-rich
Region671 – 73969Required for interaction with NUDT21
Motif490 – 50718Nuclear localization signal 1 By similarity
Motif644 – 65916Nuclear localization signal 2 By similarity

Sites

Metal binding1131Magnesium 1; catalytic By similarity
Metal binding1131Magnesium 2; catalytic By similarity
Metal binding1151Magnesium 1; catalytic By similarity
Metal binding1151Magnesium 2; catalytic By similarity
Metal binding1671Magnesium 2; catalytic By similarity
Binding site1091ATP By similarity
Binding site1671ATP By similarity
Binding site2281ATP By similarity
Binding site2371ATP By similarity
Site1531Interaction with RNA By similarity
Site1581Interaction with RNA By similarity
Site3281Interaction with RNA By similarity
Site3991Interaction with RNA By similarity
Site5241Interaction with RNA By similarity

Amino acid modifications

Modified residue241Phosphoserine By similarity
Modified residue5371Phosphoserine; by MAPK Ref.5
Modified residue6351N6-acetyllysine By similarity
Modified residue6441N6-acetyllysine By similarity
Modified residue7301N6-acetyllysine; alternate By similarity
Modified residue7341N6-acetyllysine; alternate By similarity
Cross-link444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link506Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link730Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.4
Cross-link734Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.4

Natural variations

Alternative sequence280 – 29314EWPNP…QPEEC → YVFRLYYNKIDCRH in isoform 4.
VSP_004527
Alternative sequence294 – 37582Missing in isoform 4.
VSP_004528
Alternative sequence305 – 31713NPSDR…MPIIT → SVLFFPLQIHTIQ in isoform 3.
VSP_004529
Alternative sequence318 – 37558Missing in isoform 3.
VSP_004530
Alternative sequence373 – 3753HYI → YVK in isoform 2.
VSP_004531
Alternative sequence376 – 739364Missing in isoform 2.
VSP_004532

Experimental info

Mutagenesis444 – 4452KK → RR: Some loss of sumoylation. No change in nuclear localization. Ref.4
Mutagenesis5371S → A: Eliminates MAPK-mediated phosphorylation. Ref.4 Ref.5
Mutagenesis656 – 6572KK → RR: Some loss of sumoylation; Largely localized to the cytoplasm. Ref.4
Sequence conflict471K → L in AAC52586. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: BABE406BDF8EBEE9

FASTA73982,309
        10         20         30         40         50         60 
MPFPVTTQGS QQTQPPQRHY GITSPISLAA PKETDCLLTQ KLIETLKPFG 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 
FPAPKESPDR EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFELD 

       490        500        510        520        530        540 
MKIAAMHVKR KQLHQLLPSH VLQKRKKHST EGVKLTALND SSLDLSMDSD NSMSVPSPTS 

       550        560        570        580        590        600 
AMKTSPLNSS GSSQGRNSPA PAVTAASVTS IQASEVSVPQ ANSSESPGGP SSESIPQTAT 

       610        620        630        640        650        660 
QPAISPPPKP TVSRVVSSTR LVNPSPRPSG NTATKVPNPI VGVKRTSSPN KEESPKKTKT 

       670        680        690        700        710        720 
EEDETSEDAN CLALSGHDKT ETKEQVDLET SAVQSETVPA SASLLASQKT SSTDLSDIPA 

       730 
LPANPIPVIK NSIKLRLNR 

« Hide

Isoform 2 (III) [UniParc].

Checksum: 09C195A8E639A0B2
Show »

FASTA37543,110
Isoform 3 (V) [UniParc].

Checksum: AA7913AC868F72CF
Show »

FASTA68175,495
Isoform 4 (VI) [UniParc].

Checksum: 8EE01C27FBF14541
Show »

FASTA65772,874

References

[1]"Complex alternative RNA processing generates an unexpected diversity of poly(A) polymerase isoforms."
Zhao W., Manley J.L.
Mol. Cell. Biol. 16:2378-2386(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
Tissue: Brain.
[2]"Regulation of spermatogenesis by testis-specific, cytoplasmic poly(A) polymerase TPAP."
Kashiwabara S., Noguchi J., Zhuang T., Ohmura K., Honda A., Sugiura S., Miyamoto K., Takahashi S., Inoue K., Ogura A., Baba T.
Science 298:1999-2002(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Strain: 129/SvJ.
[3]"Interaction of poly(A) polymerase with the 25-kDa subunit of cleavage factor I."
Kim H., Lee Y.
Biochem. Biophys. Res. Commun. 289:513-518(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NUDT21.
[4]"Sumoylation regulates multiple aspects of mammalian poly(A) polymerase function."
Vethantham V., Rao N., Manley J.L.
Genes Dev. 22:499-511(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-444; LYS-445; LYS-506; LYS-507; LYS-730 AND LYS-734, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, FUNCTION, MUTAGENESIS OF 444-LYS-LYS-445; 506-LYS-LYS-507 AND 656-LYS-LYS-657.
[5]"ERK is a novel regulatory kinase for poly(A) polymerase."
Lee S.-H., Choi H.-S., Kim H., Lee Y.
Nucleic Acids Res. 36:803-813(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-537, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-537.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52197 mRNA. Translation: AAC52586.1.
U58134 mRNA. Translation: AAC52608.1.
U58135 mRNA. Translation: AAC52609.1.
AB086650 Genomic DNA. Translation: BAC00996.1.
RefSeqNP_035242.1. NM_011112.3.
UniGeneMm.255877.

3D structure databases

ProteinModelPortalQ61183.
SMRQ61183. Positions 19-498.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000098624.

PTM databases

PhosphoSiteQ61183.

Proteomic databases

PaxDbQ61183.
PRIDEQ61183.

Protocols and materials databases

DNASU18789.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021535; ENSMUSP00000021535; ENSMUSG00000021111. [Q61183-1]
ENSMUST00000109901; ENSMUSP00000105527; ENSMUSG00000021111. [Q61183-1]
ENSMUST00000166735; ENSMUSP00000128908; ENSMUSG00000021111.
GeneID18789.
KEGGmmu:18789.
UCSCuc007oyv.1. mouse. [Q61183-2]
uc007oyz.2. mouse. [Q61183-1]

Organism-specific databases

CTD10914.
MGIMGI:109301. Papola.

Phylogenomic databases

eggNOGCOG5186.
GeneTreeENSGT00390000017928.
HOGENOMHOG000204376.
HOVERGENHBG053502.
InParanoidQ61183.
KOK14376.
OMASPVTTQG.
OrthoDBEOG7XH6PT.
PhylomeDBQ61183.
TreeFamTF300842.

Gene expression databases

ArrayExpressQ61183.
BgeeQ61183.
CleanExMM_PAPOLA.
GenevestigatorQ61183.

Family and domain databases

Gene3D3.30.70.590. 1 hit.
InterProIPR002934. Nucleotidyltransferase.
IPR011068. NuclTrfase_I_C.
IPR007012. PolA_pol_cen_dom.
IPR007010. PolA_pol_RNA-bd_dom.
IPR014492. PolyA_polymerase.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view]
PIRSFPIRSF018425. PolyA_polymerase. 1 hit.
SUPFAMSSF55003. SSF55003. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPAPOLA. mouse.
NextBio295064.
PROQ61183.
SOURCESearch...

Entry information

Entry namePAPOA_MOUSE
AccessionPrimary (citable) accession number: Q61183
Secondary accession number(s): Q61208, Q61209, Q8K4X2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot