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   27-MAR-2024, entry version 134.
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; 3.
DR   STRING; 10090.ENSMUSP00000025077; -.
DR   iPTMnet; Q9D0D3; -.
DR   PhosphoSitePlus; Q9D0D3; -.
DR   SwissPalm; Q9D0D3; -.
DR   EPD; Q9D0D3; -.
DR   MaxQB; Q9D0D3; -.
DR   PaxDb; 10090-ENSMUSP00000025077; -.
DR   PeptideAtlas; Q9D0D3; -.
DR   ProteomicsDB; 288055; -.
DR   Pumba; Q9D0D3; -.
DR   Antibodypedia; 35309; 115 antibodies from 17 providers.
DR   Ensembl; ENSMUST00000025077.7; ENSMUSP00000025077.7; ENSMUSG00000024234.8.
DR   GeneID; 67440; -.
DR   KEGG; mmu:67440; -.
DR   UCSC; uc008dyi.1; mouse.
DR   AGR; MGI:1914690; -.
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; 170176at2759; -.
DR   PhylomeDB; Q9D0D3; -.
DR   TreeFam; TF354308; -.
DR   BioGRID-ORCS; 67440; 19 hits in 81 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 233 other cell types or tissues.
DR   ExpressionAtlas; Q9D0D3; baseline and differential.
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:1990817; F:poly(A) RNA polymerase activity; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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:0000965; P:mitochondrial RNA 3'-end processing; ISS:UniProtKB.
DR   GO; GO:0006378; P:mRNA polyadenylation; ISO:MGI.
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   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002058; PAP_assoc.
DR   InterPro; IPR041252; RL.
DR   PANTHER; PTHR12271; POLY A POLYMERASE CID PAP -RELATED; 1.
DR   PANTHER; PTHR12271:SF133; POLY(A) RNA POLYMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF03828; PAP_assoc; 1.
DR   Pfam; PF17797; RL; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81631; PAP/OAS1 substrate-binding domain; 1.
DR   Genevisible; Q9D0D3; MM.
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
//