Poly(A) polymerase - Saccharomyces cerevisiae (Baker's yeast)

Names and origin

Protein names

Recommended name:
    Poly(A) polymerase
      Short name=PAP
    EC=2.7.7.19
Alternative name(s):
    Polynucleotide adenylyltransferase

Gene names

Name:	PAP1
Ordered Locus Names:	YKR002W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (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 structure	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 and RRP6. Ref.4 Ref.5
Subcellular location	Nucleus. Ref.6 Ref.7
Miscellaneous	Present with 17100 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the poly(A) polymerase family.

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Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	mRNA export from nucleus Inferred from mutant phenotype. Source: SGD mRNA polyadenylation Ref.1 Inferred from direct assay. Source: SGD transcription Inferred from electronic annotation. Source: InterPro
Cellular component	mRNA cleavage and polyadenylation specificity factor complex Ref.6 Inferred from physical interaction. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW polynucleotide adenylyltransferase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 568

568

Poly(A) polymerase

PRO_0000051621

Sites

Active site

100

1

Active site

102

1

Active site

154

1

Amino acid modifications

Modified residue

452

1

Phosphoserine Ref.9

Modified residue

548

1

Phosphoserine Ref.9

Secondary structure

1

.

568

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P29468-1 [UniParc].

Last modified April 1, 1993. Version 1.
Checksum: 759DE5210DC8D881
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FASTA

568

64,552

        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

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the essential gene for poly(A) polymerase from S. cerevisiae." Lingner J., Kellermann J., Keller W. Nature 354:496-498(1991) [PubMed: 1840648] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 204510 / AB320.
[2]	"DNA sequencing and analysis of a 24.7 kb segment encompassing centromere CEN11 of Saccharomyces cerevisiae reveals nine previously unknown open reading frames." Duesterhoeft A., Philippsen P. Yeast 8:749-759(1992) [PubMed: 1441752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome XI." 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. Mewes H.-W. Nature 369:371-378(1994) [PubMed: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	"The Uba2 and Ufd1 proteins of Saccharomyces cerevisiae interact with poly(A) polymerase and affect the polyadenylation activity of cell extracts." del Olmo M., Mizrahi N., Gross S., Moore C.L. Mol. Gen. Genet. 255:209-218(1997) [PubMed: 9236779] [Abstract] Cited for: INTERACTION WITH FIR1.
[5]	"A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p." Burkard K.T.D., Butler J.S. Mol. Cell. Biol. 20:604-616(2000) [PubMed: 10611239] [Abstract] Cited for: INTERACTION WITH RRP6.
[6]	"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." Nedea E., He X., Kim M., Pootoolal J., Zhong G., Canadien V., Hughes T., Buratowski S., Moore C.L., Greenblatt J. J. Biol. Chem. 278:33000-33010(2003) [PubMed: 12819204] [Abstract] Cited for: IDENTIFICATION IN THE CPF COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
[7]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452 AND SER-548, MASS SPECTROMETRY.
[10]	"Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP." Bard J., Zhelkovsky A.M., Helmling S., Earnest T.N., Moore C.L., Bohm A. Science 289:1346-1349(2000) [PubMed: 10958780] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-537.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X60307 Genomic DNA. Translation: CAA42852.1.
X65124 Genomic DNA. Translation: CAA46250.1.
Z28227 Genomic DNA. Translation: CAA82072.1.

PIR

S19031.

RefSeq

NP_012927.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FA0	X-ray	2.60	A/B	1-537	[»]
2HHP	X-ray	1.80	A	1-530	[»]
2O1P	X-ray	2.70	A/B	1-538	[»]
2Q66	X-ray	1.80	A	5-529	[»]
3C66	X-ray	2.60	A/B	1-537	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:2297N.

Proteomic databases

PeptideAtlas

P29468.

Genome annotation databases

Ensembl

YKR002W. Saccharomyces cerevisiae. [Contig view]

GeneID

853871.

GenomeReviews

Gene locus YKR002W in contig Y13137_GR.

KEGG

sce:YKR002W.

NMPDR

fig|4932.3.peg.3913.

Organism-specific databases

CYGD

YKR002w.

SGD

S000001710. PAP1.

Yeast-GFP

Search...

Phylogenomic databases

HOGENOM

P29468.

OMA

P29468. VTREDFF.

Enzyme and pathway databases

BRENDA

2.7.7.19. 250.

Gene expression databases

ArrayExpress

P29468.

GermOnline

YKR002W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR002934. Nucleotidyltransferase.
IPR007012. PolA_pol_centr.
IPR007010. PolA_pol_RNA-bd.
IPR014492. PolyA_polymerase.
[Graphical view]

Gene3D

G3DSA:3.30.70.590. PolA_pol_RNA-bd. 1 hit.

Pfam

PF01909. NTP_transf_2. 1 hit.
PF04928. PAP_central. 1 hit.
PF04926. PAP_RNA-bind. 1 hit.
[Graphical view]

PIRSF

PIRSF018425. PolyA_polymerase. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

975142.

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Entry information

Entry name

PAP_YEAST

Accession

Primary (citable) accession number: P29468

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	June 16, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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