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Q9D0D3 (PAPD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 75. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A) RNA polymerase, mitochondrial
Short name=PAP
EC=2.7.7.19
Alternative name(s):
PAP-associated domain-containing protein 1
Polynucleotide adenylyltransferase
Gene names
Name:Mtpap
Synonyms:Papd1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length585 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Polymerase that creates the 3' poly(A) tail of mitochondrial transcripts. Can use all four nucleotides, but has higher activity with ATP and UTP (in vitro). Plays a role in replication-dependent histone mRNA degradation. May be involved in the terminal uridylation of mature histone mRNAs before their degradation is initiated. Might be responsible for the creation of some UAA stop codons which are not encoded in mtDNA By similarity.

Catalytic activity

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

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity. Mitochondrion By similarity.

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Contains 1 PAP-associated domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3737Mitochondrion Potential
Chain38 – 585548Poly(A) RNA polymerase, mitochondrial
PRO_0000250690

Regions

Domain441 – 48646PAP-associated
Nucleotide binding107 – 1093ATP Potential
Nucleotide binding244 – 2452ATP Potential

Sites

Metal binding2461Magnesium or manganese; catalytic Potential
Metal binding2481Magnesium or manganese; catalytic Potential

Amino acid modifications

Modified residue901N6-acetyllysine By similarity

Experimental info

Sequence conflict741A → S in BAE22572. Ref.2
Sequence conflict1901E → G in BAC36396. Ref.2
Sequence conflict2491M → T in BAE22572. Ref.2
Sequence conflict5781K → E in BAC36396. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9D0D3 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 33DB6AC61A080B82

FASTA58565,229
        10         20         30         40         50         60 
MAARGVGLLT RLPVCSQRRN RIPRSISRLL SCPGTIAASI GSEEQSSVVA ETGIEDKTLQ 

        70         80         90        100        110        120 
KKFSEVQKER REQAQRTVLI HCPNNINEKK FLKYLSQHGP VNNHFFYESF GLFAVVEFCQ 

       130        140        150        160        170        180 
KDSIKSLQNG THTPTQSTEA AIPFKSRFLN LRLKNPSSQV SGQPFVQTTN QSPPSSKKLF 

       190        200        210        220        230        240 
ELLSYAESIE EQLNTLLKAF QLTEENIRLR HLTCSLIEDI AAAYFPSCVI RPFGSSVNTF 

       250        260        270        280        290        300 
GKLGCDLDMF LDLDETGKLD VHKNTGNFFM EFQVKNVPSE RIATQKILSV IGECLDNFGP 

       310        320        330        340        350        360 
GCVGVQKILN ARCPLVRFSH QGSGFQCDLT ANNSIALKSS ELLYIYGSLD SRVRALVFSV 

       370        380        390        400        410        420 
RCWARAHSLT SSIPGAWITN FSLTVMVIFF LQRRSPPILP TLDSLKSIAD AEDRCILEGN 

       430        440        450        460        470        480 
NCTFVQDVNK IQPSGNTETL ELLIKEFFEY FGNFAFNKNS INIRQGREQN KPDSSPLYIQ 

       490        500        510        520        530        540 
NPFETSLNIS KNVSQSQLQK FVELARDSAW ILEQEDKNQP FSSSRQPWGL AALLLPPGSG 

       550        560        570        580 
HTSLSRKKKK KPMSEKVKGL LASIKSNSPD SSTDTSGKRT ISTQA

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo, Muellerian duct and Testis.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK011546 mRNA. Translation: BAB27689.1.
AK076565 mRNA. Translation: BAC36396.1.
AK135537 mRNA. Translation: BAE22572.1.
BC057643 mRNA. Translation: AAH57643.1.
IPIIPI00459344.
RefSeqNP_080433.1. NM_026157.2.
UniGeneMm.49826.

3D structure databases

ProteinModelPortalQ9D0D3.
SMRQ9D0D3. Positions 62-535.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000025077.

PTM databases

PhosphoSiteQ9D0D3.

Proteomic databases

PaxDbQ9D0D3.
PRIDEQ9D0D3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025077; ENSMUSP00000025077; ENSMUSG00000024234.
GeneID67440.
KEGGmmu:67440.
UCSCuc008dyi.1. mouse.

Organism-specific databases

CTD55149.
MGIMGI:1914690. Mtpap.

Phylogenomic databases

eggNOGCOG5260.
GeneTreeENSGT00550000074490.
HOGENOMHOG000115438.
HOVERGENHBG082104.
InParanoidQ9D0D3.
OMAVRCWARA.
OrthoDBEOG45TCN5.

Gene expression databases

BgeeQ9D0D3.
CleanExMM_PAPD1.
GenevestigatorQ9D0D3.
GermOnlineENSMUSG00000024234. Mus musculus.

Family and domain databases

InterProIPR002058. PAP_assoc.
[Graphical view]
PfamPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio324570.
SOURCESearch...

Entry information

Entry namePAPD1_MOUSE
AccessionPrimary (citable) accession number: Q9D0D3
Secondary accession number(s): Q3UXJ1, Q8C651
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: June 1, 2001
Last modified: April 3, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents