PAPOG_MOUSE
ID PAPOG_MOUSE Reviewed; 739 AA.
AC Q6PCL9; Q8BZC9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Poly(A) polymerase gamma;
DE Short=PAP-gamma;
DE EC=2.7.7.19;
DE AltName: Full=Polynucleotide adenylyltransferase gamma;
DE AltName: Full=SRP RNA 3'-adenylating enzyme;
DE AltName: Full=Signal recognition particle RNA-adenylating enzyme;
DE Short=SRP RNA-adenylating enzyme;
GN Name=Papolg;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bhattacharya R., Gaikwad A., Reddy R.;
RT "Comparative analysis of the sequences of the SRP 3'-adenylating enzyme in
RT human, mouse and Xenopus.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Liver, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Responsible for the post-transcriptional adenylation of the
CC 3'-terminal of mRNA precursors and several small RNAs including signal
CC recognition particle (SRP) RNA, nuclear 7SK RNA, U2 small nuclear RNA,
CC and ribosomal 5S RNA. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions. Also active with manganese. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BWT3}.
CC -!- SIMILARITY: Belongs to the poly(A) polymerase family. {ECO:0000305}.
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DR EMBL; DQ103505; AAZ80292.1; -; mRNA.
DR EMBL; AK035810; BAC29194.1; -; mRNA.
DR EMBL; AL662810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059271; AAH59271.1; -; mRNA.
DR CCDS; CCDS24481.1; -.
DR RefSeq; NP_766143.2; NM_172555.2.
DR AlphaFoldDB; Q6PCL9; -.
DR SMR; Q6PCL9; -.
DR BioGRID; 229763; 1.
DR STRING; 10090.ENSMUSP00000020513; -.
DR iPTMnet; Q6PCL9; -.
DR PhosphoSitePlus; Q6PCL9; -.
DR EPD; Q6PCL9; -.
DR MaxQB; Q6PCL9; -.
DR PaxDb; Q6PCL9; -.
DR PeptideAtlas; Q6PCL9; -.
DR PRIDE; Q6PCL9; -.
DR ProteomicsDB; 294005; -.
DR Antibodypedia; 30527; 135 antibodies from 21 providers.
DR Ensembl; ENSMUST00000020513; ENSMUSP00000020513; ENSMUSG00000020273.
DR GeneID; 216578; -.
DR KEGG; mmu:216578; -.
DR UCSC; uc007ifp.2; mouse.
DR CTD; 64895; -.
DR MGI; MGI:2442119; Papolg.
DR VEuPathDB; HostDB:ENSMUSG00000020273; -.
DR eggNOG; KOG2245; Eukaryota.
DR GeneTree; ENSGT00940000156467; -.
DR HOGENOM; CLU_011511_1_2_1; -.
DR InParanoid; Q6PCL9; -.
DR OMA; FTEHVIM; -.
DR OrthoDB; 326577at2759; -.
DR PhylomeDB; Q6PCL9; -.
DR TreeFam; TF300842; -.
DR BioGRID-ORCS; 216578; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Papolg; mouse.
DR PRO; PR:Q6PCL9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6PCL9; protein.
DR Bgee; ENSMUSG00000020273; Expressed in secondary oocyte and 243 other tissues.
DR ExpressionAtlas; Q6PCL9; baseline and differential.
DR Genevisible; Q6PCL9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; ISS:UniProtKB.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043631; P:RNA polyadenylation; ISS:UniProtKB.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR011068; NuclTrfase_I-like_C.
DR InterPro; IPR007012; PolA_pol_cen_dom.
DR InterPro; IPR007010; PolA_pol_RNA-bd_dom.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR Pfam; PF01909; NTP_transf_2; 1.
DR Pfam; PF04928; PAP_central; 1.
DR Pfam; PF04926; PAP_RNA-bind; 2.
DR SUPFAM; SSF55003; SSF55003; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Magnesium; Manganese; Metal-binding;
KW mRNA processing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding; Transferase.
FT CHAIN 1..739
FT /note="Poly(A) polymerase gamma"
FT /id="PRO_0000253025"
FT REGION 506..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 99..101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112..114
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 245..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 152
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 157
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 327
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 398
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT SITE 531
FT /note="Interaction with RNA"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 524
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BWT3"
FT CONFLICT 364
FT /note="P -> T (in Ref. 2; BAC29194)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 82957 MW; 603F1AB38DF985BE 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
PGNKEHHKAN NYVSMWFLGI IFRRVENAES VNIDLTYDIQ SFTDTVYRQA NNINMLKDGM
KIEATHVKKK QLHHYLPAEI LQKKKKSLSD VSRSSGGLQS KRSSLDSTCL DSSRDTDSGT
PFNSPVSANK PSNPDSPTGE IERSSAEPVA VVVEKLPSVP PAQGLSIPVI GAKVDPTAKA
VSSPAVCTIP TVVGRNVIPR ITTPHNPVQG QPHLNGISNI TKNVTPKRSH SPPTDGTSKR
LKDIEKFIRL ESAFKESRAA EDRKRKPMDS IGGESMPIPT IDTARKKRLP SKELPDSSSP
VPANNIRVIK NSIRLTLNR
