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Protein

Poly(A) RNA polymerase, mitochondrial

Gene

Mtpap

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi246 – 2461Magnesium or manganese; catalyticSequence Analysis
Metal bindingi248 – 2481Magnesium or manganese; catalyticSequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi107 – 1093ATPSequence Analysis
Nucleotide bindingi244 – 2452ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. identical protein binding Source: MGI
  3. magnesium ion binding Source: UniProtKB
  4. manganese ion binding Source: UniProtKB
  5. poly(A) RNA binding Source: MGI
  6. polynucleotide adenylyltransferase activity Source: UniProtKB
  7. protein homodimerization activity Source: MGI
  8. UTP binding Source: UniProtKB

GO - Biological processi

  1. histone mRNA catabolic process Source: UniProtKB
  2. mRNA polyadenylation Source: UniProtKB
  3. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

mRNA processing, Transcription

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A) RNA polymerase, mitochondrial (EC:2.7.7.19)
Short name:
PAP
Alternative name(s):
PAP-associated domain-containing protein 1
Polynucleotide adenylyltransferase
Gene namesi
Name:Mtpap
Synonyms:Papd1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:1914690. Mtpap.

Subcellular locationi

Cytoplasm By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. intracellular membrane-bounded organelle Source: MGI
  3. mitochondrion Source: MGI
  4. nucleus Source: Ensembl
  5. plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3737MitochondrionSequence AnalysisAdd
BLAST
Chaini38 – 585548Poly(A) RNA polymerase, mitochondrialPRO_0000250690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei90 – 901N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9D0D3.
PaxDbiQ9D0D3.
PRIDEiQ9D0D3.

PTM databases

PhosphoSiteiQ9D0D3.

Expressioni

Gene expression databases

BgeeiQ9D0D3.
CleanExiMM_PAPD1.
GenevestigatoriQ9D0D3.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025077.

Structurei

3D structure databases

ProteinModelPortaliQ9D0D3.
SMRiQ9D0D3. Positions 62-535.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini441 – 48646PAP-associatedAdd
BLAST

Sequence similaritiesi

Belongs to the DNA polymerase type-B-like family.Curated
Contains 1 PAP-associated domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
HOGENOMiHOG000115438.
HOVERGENiHBG082104.
InParanoidiQ9D0D3.
KOiK18060.
OMAiDAEDKCI.
OrthoDBiEOG7353WD.
PhylomeDBiQ9D0D3.
TreeFamiTF354308.

Family and domain databases

InterProiIPR002058. PAP_assoc.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D0D3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAARGVGLLT RLPVCSQRRN RIPRSISRLL SCPGTIAASI GSEEQSSVVA
60 70 80 90 100
ETGIEDKTLQ KKFSEVQKER REQAQRTVLI HCPNNINEKK FLKYLSQHGP
110 120 130 140 150
VNNHFFYESF GLFAVVEFCQ KDSIKSLQNG THTPTQSTEA AIPFKSRFLN
160 170 180 190 200
LRLKNPSSQV SGQPFVQTTN QSPPSSKKLF ELLSYAESIE EQLNTLLKAF
210 220 230 240 250
QLTEENIRLR HLTCSLIEDI AAAYFPSCVI RPFGSSVNTF GKLGCDLDMF
260 270 280 290 300
LDLDETGKLD VHKNTGNFFM EFQVKNVPSE RIATQKILSV IGECLDNFGP
310 320 330 340 350
GCVGVQKILN ARCPLVRFSH QGSGFQCDLT ANNSIALKSS ELLYIYGSLD
360 370 380 390 400
SRVRALVFSV RCWARAHSLT SSIPGAWITN FSLTVMVIFF LQRRSPPILP
410 420 430 440 450
TLDSLKSIAD AEDRCILEGN NCTFVQDVNK IQPSGNTETL ELLIKEFFEY
460 470 480 490 500
FGNFAFNKNS INIRQGREQN KPDSSPLYIQ NPFETSLNIS KNVSQSQLQK
510 520 530 540 550
FVELARDSAW ILEQEDKNQP FSSSRQPWGL AALLLPPGSG HTSLSRKKKK
560 570 580
KPMSEKVKGL LASIKSNSPD SSTDTSGKRT ISTQA
Length:585
Mass (Da):65,229
Last modified:June 1, 2001 - v1
Checksum:i33DB6AC61A080B82
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741A → S in BAE22572 (PubMed:15489334).Curated
Sequence conflicti190 – 1901E → G in BAC36396 (PubMed:15489334).Curated
Sequence conflicti249 – 2491M → T in BAE22572 (PubMed:15489334).Curated
Sequence conflicti578 – 5781K → E in BAC36396 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011546 mRNA. Translation: BAB27689.1.
AK076565 mRNA. Translation: BAC36396.1.
AK135537 mRNA. Translation: BAE22572.1.
BC057643 mRNA. Translation: AAH57643.1.
CCDSiCCDS37718.1.
RefSeqiNP_080433.1. NM_026157.2.
UniGeneiMm.49826.

Genome annotation databases

EnsembliENSMUST00000025077; ENSMUSP00000025077; ENSMUSG00000024234.
GeneIDi67440.
KEGGimmu:67440.
UCSCiuc008dyi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011546 mRNA. Translation: BAB27689.1.
AK076565 mRNA. Translation: BAC36396.1.
AK135537 mRNA. Translation: BAE22572.1.
BC057643 mRNA. Translation: AAH57643.1.
CCDSiCCDS37718.1.
RefSeqiNP_080433.1. NM_026157.2.
UniGeneiMm.49826.

3D structure databases

ProteinModelPortaliQ9D0D3.
SMRiQ9D0D3. Positions 62-535.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025077.

PTM databases

PhosphoSiteiQ9D0D3.

Proteomic databases

MaxQBiQ9D0D3.
PaxDbiQ9D0D3.
PRIDEiQ9D0D3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025077; ENSMUSP00000025077; ENSMUSG00000024234.
GeneIDi67440.
KEGGimmu:67440.
UCSCiuc008dyi.1. mouse.

Organism-specific databases

CTDi55149.
MGIiMGI:1914690. Mtpap.

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
HOGENOMiHOG000115438.
HOVERGENiHBG082104.
InParanoidiQ9D0D3.
KOiK18060.
OMAiDAEDKCI.
OrthoDBiEOG7353WD.
PhylomeDBiQ9D0D3.
TreeFamiTF354308.

Miscellaneous databases

NextBioi324570.
PROiQ9D0D3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0D3.
CleanExiMM_PAPD1.
GenevestigatoriQ9D0D3.

Family and domain databases

InterProiIPR002058. PAP_assoc.
[Graphical view]
PfamiPF03828. PAP_assoc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiPAPD1_MOUSE
AccessioniPrimary (citable) accession number: Q9D0D3
Secondary accession number(s): Q3UXJ1, Q8C651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.