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Database: UniProt
Entry: Q8BY05_MOUSE
LinkDB: Q8BY05_MOUSE
Original site: Q8BY05_MOUSE 
ID   Q8BY05_MOUSE            Unreviewed;       429 AA.
AC   Q8BY05;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 145.
DE   RecName: Full=Poly(A) polymerase {ECO:0000256|PIRNR:PIRNR018425};
DE            EC=2.7.7.19 {ECO:0000256|PIRNR:PIRNR018425};
GN   Name=Papolg {ECO:0000313|Ensembl:ENSMUSP00000099927.3,
GN   ECO:0000313|MGI:MGI:2442119};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000313|EMBL:BAC31312.1};
RN   [1] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9;
RA   Carninci P., Hayashizaki Y.;
RT   "High-efficiency full-length cDNA cloning.";
RL   Methods Enzymol. 303:19-44(1999).
RN   [2] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=11042159; DOI=10.1101/gr.145100;
RA   Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M.,
RA   Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.;
RT   "Normalization and subtraction of cap-trapper-selected cDNAs to prepare
RT   full-length cDNA libraries for rapid discovery of new genes.";
RL   Genome Res. 10:1617-1630(2000).
RN   [3] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=11076861; DOI=10.1101/gr.152600;
RA   Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P.,
RA   Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N.,
RA   Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R.,
RA   Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S.,
RA   Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y.,
RA   Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y.,
RA   Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.;
RT   "RIKEN integrated sequence analysis (RISA) system--384-format sequencing
RT   pipeline with 384 multicapillary sequencer.";
RL   Genome Res. 10:1757-1771(2000).
RN   [4] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=11217851; DOI=10.1038/35055500;
RG   The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium;
RT   "Functional annotation of a full-length mouse cDNA collection.";
RL   Nature 409:685-690(2001).
RN   [5] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RA   Adachi J., Aizawa K., Akimura T., Arakawa T., Bono H., Carninci P.,
RA   Fukuda S., Furuno M., Hanagaki T., Hara A., Hashizume W., Hayashida K.,
RA   Hayatsu N., Hiramoto K., Hiraoka T., Hirozane T., Hori F., Imotani K.,
RA   Ishii Y., Itoh M., Kagawa I., Kasukawa T., Katoh H., Kawai J., Kojima Y.,
RA   Kondo S., Konno H., Kouda M., Koya S., Kurihara C., Matsuyama T.,
RA   Miyazaki A., Murata M., Nakamura M., Nishi K., Nomura K., Numazaki R.,
RA   Ohno M., Ohsato N., Okazaki Y., Saito R., Saitoh H., Sakai C., Sakai K.,
RA   Sakazume N., Sano H., Sasaki D., Shibata K., Shinagawa A., Shiraki T.,
RA   Sogabe Y., Tagami M., Tagawa A., Takahashi F., Takaku-Akahira S.,
RA   Takeda Y., Tanaka T., Tomaru A., Toya T., Yasunishi A., Muramatsu M.,
RA   Hayashizaki Y.;
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=12466851; DOI=10.1038/nature01266;
RG   The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team;
RT   "Analysis of the mouse transcriptome based on functional annotation of
RT   60,770 full-length cDNAs.";
RL   Nature 420:563-573(2002).
RN   [7] {ECO:0000313|EMBL:BAE23879.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAE23879.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAE23879.1};
RA   Arakawa T., Carninci P., Fukuda S., Hashizume W., Hayashida K., Hori F.,
RA   Iida J., Imamura K., Imotani K., Itoh M., Kanagawa S., Kawai J., Kojima M.,
RA   Konno H., Murata M., Nakamura M., Ninomiya N., Nishiyori H., Nomura K.,
RA   Ohno M., Sakazume N., Sano H., Sasaki D., Shibata K., Shiraki T.,
RA   Tagami M., Tagami Y., Waki K., Watahiki A., Muramatsu M., Hayashizaki Y.;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RG   The FANTOM Consortium;
RG   Riken Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group);
RT   "The Transcriptional Landscape of the Mammalian Genome.";
RL   Science 309:1559-1563(2005).
RN   [9] {ECO:0000313|EMBL:BAC31312.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C57BL/6J {ECO:0000313|EMBL:BAC31312.1};
RC   TISSUE=Cerebellum {ECO:0000313|EMBL:BAC31312.1};
RX   PubMed=16141073; DOI=10.1126/science.1112009;
RG   RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium;
RT   "Antisense Transcription in the Mammalian Transcriptome.";
RL   Science 309:1564-1566(2005).
RN   [10] {ECO:0000313|Ensembl:ENSMUSP00000099927.3, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099927.3,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [11] {ECO:0000313|Ensembl:ENSMUSP00000099927.3}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000099927.3};
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
CC       {ECO:0000256|PIRNR:PIRNR018425}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide;
CC         Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395,
CC         ChEBI:CHEBI:173115; EC=2.7.7.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00024620,
CC         ECO:0000256|PIRNR:PIRNR018425};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR018425-2};
CC       Note=Binds 2 magnesium ions. Also active with manganese.
CC       {ECO:0000256|PIRSR:PIRSR018425-2};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR018425}.
CC   -!- SIMILARITY: Belongs to the poly(A) polymerase family.
CC       {ECO:0000256|ARBA:ARBA00010912, ECO:0000256|PIRNR:PIRNR018425}.
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DR   EMBL; AK042629; BAC31312.1; -; mRNA.
DR   EMBL; AK139065; BAE23879.1; -; mRNA.
DR   SMR; Q8BY05; -.
DR   ProteomicsDB; 334867; -.
DR   Antibodypedia; 30527; 147 antibodies from 21 providers.
DR   Ensembl; ENSMUST00000102863.3; ENSMUSP00000099927.3; ENSMUSG00000020273.14.
DR   AGR; MGI:2442119; -.
DR   MGI; MGI:2442119; Papolg.
DR   VEuPathDB; HostDB:ENSMUSG00000020273; -.
DR   GeneTree; ENSGT00940000156467; -.
DR   HOGENOM; CLU_011511_4_3_1; -.
DR   OMA; WEGWIES; -.
DR   ChiTaRS; Papolg; mouse.
DR   Proteomes; UP000000589; Chromosome 11.
DR   Bgee; ENSMUSG00000020273; Expressed in secondary oocyte and 246 other cell types or tissues.
DR   ExpressionAtlas; Q8BY05; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1990817; F:poly(A) RNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0031123; P:RNA 3'-end processing; IEA:InterPro.
DR   CDD; cd05402; NT_PAP_TUTase; 1.
DR   Gene3D; 1.10.1410.10; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.30.70.590; Poly(A) polymerase predicted RNA binding domain; 1.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR011068; NuclTrfase_I-like_C.
DR   InterPro; IPR007012; PolA_pol_cen_dom.
DR   InterPro; IPR048840; PolA_pol_NTPase.
DR   InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR   InterPro; IPR014492; PolyA_polymerase.
DR   PANTHER; PTHR10682; POLY A POLYMERASE; 1.
DR   PANTHER; PTHR10682:SF6; POLY(A) POLYMERASE GAMMA; 1.
DR   Pfam; PF04928; PAP_central; 1.
DR   Pfam; PF20750; PAP_NTPase; 1.
DR   Pfam; PF04926; PAP_RNA-bind; 1.
DR   PIRSF; PIRSF018425; PolyA_polymerase; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF55003; PAP/Archaeal CCA-adding enzyme, C-terminal domain; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR018425};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR018425-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR018425-2};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR018425};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR018425};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR018425};
KW   Proteomics identification {ECO:0007829|EPD:Q8BY05,
KW   ECO:0007829|MaxQB:Q8BY05};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR018425}.
FT   DOMAIN          20..213
FT                   /note="Poly(A) polymerase nucleotidyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF20750"
FT   DOMAIN          218..362
FT                   /note="Poly(A) polymerase central"
FT                   /evidence="ECO:0000259|Pfam:PF04928"
FT   DOMAIN          365..426
FT                   /note="Poly(A) polymerase RNA-binding"
FT                   /evidence="ECO:0000259|Pfam:PF04926"
FT   BINDING         99..101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         108
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         112..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         166
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-2"
FT   BINDING         227
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         236
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
FT   BINDING         245..246
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018425-1"
SQ   SEQUENCE   429 AA;  49046 MW;  5C95199E3C03F220 CRC64;
     MKEMSANTML DSQRQQKHYG ITSPISLACP KEIDHIYTQK LIDAMKPFGV FEDEEELNHR
     LVVLGKLNNL VKEWISDISE SKNLPPSVVA TVGGKIFTFG SYRLGVHTKG ADIDALCVAP
     RHVERSDFFQ SFFEKLKHQD GIRNLRAVED AFVPVIKFEF DGIEIDLVFA RLAIQTISDN
     LDLRDDSRLR SLDIRCIRSL NGCRVTDEIL HLVPNKETFR LTLRAVKLWA KRRGIYSNML
     GFLGGVSWAM LVARTCQLYP NAAASTLVHK FFLVFSKWEW PNPVLLKQPE ESNLNLPVWD
     PRVNPSDRYH LMPIITPAYP QQNSTYNVST STRTVMVEEF KQGLAVTDEI LQGKSDWSKL
     LEPPNFFQKY RHYIVLTASA STEENHLEWV GLVESKIRVL VGNLERNEFI TLAHVNPQSF
     PGNKEHHKA
//
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