PAPD1_MOUSE
ID PAPD1_MOUSE Reviewed; 585 AA.
AC Q9D0D3; Q3UXJ1; Q8C651;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Poly(A) RNA polymerase, mitochondrial;
DE Short=PAP;
DE EC=2.7.7.19;
DE AltName: Full=PAP-associated domain-containing protein 1;
DE AltName: Full=Polynucleotide adenylyltransferase;
DE Flags: Precursor;
GN Name=Mtpap; Synonyms=Papd1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Muellerian duct, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Spleen;
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: Polymerase that creates the 3' poly(A) tail of mitochondrial
CC transcripts. Can use all four nucleotides, but has higher activity with
CC ATP and UTP (in vitro). Plays a role in replication-dependent histone
CC mRNA degradation. May be involved in the terminal uridylation of mature
CC histone mRNAs before their degradation is initiated. Might be
CC responsible for the creation of some UAA stop codons which are not
CC encoded in mtDNA (By similarity). {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 -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9NVV4}.
CC Mitochondrion {ECO:0000250|UniProtKB:Q9NVV4}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; AK011546; BAB27689.1; -; mRNA.
DR EMBL; AK076565; BAC36396.1; -; mRNA.
DR EMBL; AK135537; BAE22572.1; -; mRNA.
DR EMBL; BC057643; AAH57643.1; -; mRNA.
DR CCDS; CCDS37718.1; -.
DR RefSeq; NP_080433.1; NM_026157.2.
DR AlphaFoldDB; Q9D0D3; -.
DR SMR; Q9D0D3; -.
DR BioGRID; 212187; 2.
DR STRING; 10090.ENSMUSP00000025077; -.
DR iPTMnet; Q9D0D3; -.
DR PhosphoSitePlus; Q9D0D3; -.
DR EPD; Q9D0D3; -.
DR MaxQB; Q9D0D3; -.
DR PaxDb; Q9D0D3; -.
DR PeptideAtlas; Q9D0D3; -.
DR PRIDE; Q9D0D3; -.
DR ProteomicsDB; 288055; -.
DR Antibodypedia; 35309; 105 antibodies from 16 providers.
DR Ensembl; ENSMUST00000025077; ENSMUSP00000025077; ENSMUSG00000024234.
DR GeneID; 67440; -.
DR KEGG; mmu:67440; -.
DR UCSC; uc008dyi.1; mouse.
DR CTD; 55149; -.
DR MGI; MGI:1914690; Mtpap.
DR VEuPathDB; HostDB:ENSMUSG00000024234; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000158582; -.
DR HOGENOM; CLU_018757_3_1_1; -.
DR InParanoid; Q9D0D3; -.
DR OMA; RTVLIKC; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q9D0D3; -.
DR TreeFam; TF354308; -.
DR BioGRID-ORCS; 67440; 19 hits in 76 CRISPR screens.
DR ChiTaRS; Mtpap; mouse.
DR PRO; PR:Q9D0D3; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q9D0D3; protein.
DR Bgee; ENSMUSG00000024234; Expressed in manus and 230 other tissues.
DR ExpressionAtlas; Q9D0D3; baseline and differential.
DR Genevisible; Q9D0D3; MM.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002134; F:UTP binding; ISS:UniProtKB.
DR GO; GO:0071044; P:histone mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR Gene3D; 3.30.460.10; -; 1.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR041252; RL.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF17797; RL; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Magnesium; Manganese; Metal-binding;
KW Mitochondrion; mRNA processing; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transcription; Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..585
FT /note="Poly(A) RNA polymerase, mitochondrial"
FT /id="PRO_0000250690"
FT DOMAIN 441..486
FT /note="PAP-associated"
FT REGION 537..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 107..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 244..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NVV4"
FT CONFLICT 74
FT /note="A -> S (in Ref. 2; BAE22572)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="E -> G (in Ref. 2; BAC36396)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="M -> T (in Ref. 2; BAE22572)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="K -> E (in Ref. 2; BAC36396)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 585 AA; 65229 MW; 33DB6AC61A080B82 CRC64;
MAARGVGLLT RLPVCSQRRN RIPRSISRLL SCPGTIAASI GSEEQSSVVA ETGIEDKTLQ
KKFSEVQKER REQAQRTVLI HCPNNINEKK FLKYLSQHGP VNNHFFYESF GLFAVVEFCQ
KDSIKSLQNG THTPTQSTEA AIPFKSRFLN LRLKNPSSQV SGQPFVQTTN QSPPSSKKLF
ELLSYAESIE EQLNTLLKAF QLTEENIRLR HLTCSLIEDI AAAYFPSCVI RPFGSSVNTF
GKLGCDLDMF LDLDETGKLD VHKNTGNFFM EFQVKNVPSE RIATQKILSV IGECLDNFGP
GCVGVQKILN ARCPLVRFSH QGSGFQCDLT ANNSIALKSS ELLYIYGSLD SRVRALVFSV
RCWARAHSLT SSIPGAWITN FSLTVMVIFF LQRRSPPILP TLDSLKSIAD AEDRCILEGN
NCTFVQDVNK IQPSGNTETL ELLIKEFFEY FGNFAFNKNS INIRQGREQN KPDSSPLYIQ
NPFETSLNIS KNVSQSQLQK FVELARDSAW ILEQEDKNQP FSSSRQPWGL AALLLPPGSG
HTSLSRKKKK KPMSEKVKGL LASIKSNSPD SSTDTSGKRT ISTQA
