PAPD1_HUMAN
ID PAPD1_HUMAN Reviewed; 582 AA.
AC Q9NVV4; D3DRX0; Q659E3; Q6P7E5; Q9HA74;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Poly(A) RNA polymerase, mitochondrial;
DE Short=PAP;
DE EC=2.7.7.19 {ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163};
DE AltName: Full=PAP-associated domain-containing protein 1;
DE AltName: Full=Polynucleotide adenylyltransferase;
DE AltName: Full=Terminal uridylyltransferase 1;
DE Short=TUTase 1;
DE AltName: Full=mtPAP;
DE Flags: Precursor;
GN Name=MTPAP; Synonyms=PAPD1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15547249; DOI=10.1093/nar/gkh923;
RA Tomecki R., Dmochowska A., Gewartowski K., Dziembowski A., Stepien P.P.;
RT "Identification of a novel human nuclear-encoded mitochondrial poly(A)
RT polymerase.";
RL Nucleic Acids Res. 32:6001-6014(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15769737; DOI=10.1074/jbc.m500804200;
RA Nagaike T., Suzuki T., Katoh T., Ueda T.;
RT "Human mitochondrial mRNAs are stabilized with polyadenylation regulated by
RT mitochondria-specific poly(A) polymerase and polynucleotide
RT phosphorylase.";
RL J. Biol. Chem. 280:19721-19727(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS HIS-221;
RP ARG-419 AND ASN-546.
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 [9]
RP FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=18172165; DOI=10.1101/gad.1622708;
RA Mullen T.E., Marzluff W.F.;
RT "Degradation of histone mRNA requires oligouridylation followed by
RT decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to
RT 5'.";
RL Genes Dev. 22:50-65(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-90, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 44-538, FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS
RP OF 221-TYR-PHE-222; PHE-230; 259-HIS--ILE-261; 294-HIS--PRO-297; LEU-312;
RP ASP-325 AND PHE-378.
RX PubMed=21292163; DOI=10.1016/j.molcel.2011.01.013;
RA Bai Y., Srivastava S.K., Chang J.H., Manley J.L., Tong L.;
RT "Structural basis for dimerization and activity of human PAPD1, a
RT noncanonical poly(A) polymerase.";
RL Mol. Cell 41:311-320(2011).
RN [13]
RP VARIANT SPAX4 ASP-478, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=20970105; DOI=10.1016/j.ajhg.2010.09.013;
RA Crosby A.H., Patel H., Chioza B.A., Proukakis C., Gurtz K., Patton M.A.,
RA Sharifi R., Harlalka G., Simpson M.A., Dick K., Reed J.A., Al-Memar A.,
RA Chrzanowska-Lightowlers Z.M., Cross H.E., Lightowlers R.N.;
RT "Defective mitochondrial mRNA maturation is associated with spastic
RT ataxia.";
RL Am. J. Hum. Genet. 87:655-660(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. {ECO:0000269|PubMed:15547249,
CC ECO:0000269|PubMed:15769737, ECO:0000269|PubMed:18172165,
CC ECO:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163}.
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:0000269|PubMed:20970105, ECO:0000269|PubMed:21292163};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21292163};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21292163};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.1 mM for ATP {ECO:0000269|PubMed:21292163};
CC KM=0.7 mM for UTP {ECO:0000269|PubMed:21292163};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21292163}.
CC -!- INTERACTION:
CC Q9NVV4; Q13137: CALCOCO2; NbExp=2; IntAct=EBI-2556166, EBI-739580;
CC Q9NVV4; Q9NVV4: MTPAP; NbExp=3; IntAct=EBI-2556166, EBI-2556166;
CC Q9NVV4; Q9UHD2: TBK1; NbExp=2; IntAct=EBI-2556166, EBI-356402;
CC Q9NVV4; Q9QYP6: Azi2; Xeno; NbExp=2; IntAct=EBI-2556166, EBI-6115874;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18172165}.
CC Mitochondrion {ECO:0000269|PubMed:15547249,
CC ECO:0000269|PubMed:15769737}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NVV4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVV4-2; Sequence=VSP_020724;
CC -!- TISSUE SPECIFICITY: Ubiquitous, with stronger expression in tissues
CC with high energy requirements: heart, brain, and skeletal muscle.
CC {ECO:0000269|PubMed:15547249}.
CC -!- DISEASE: Spastic ataxia 4, autosomal recessive (SPAX4) [MIM:613672]: A
CC slowly progressive neurodegenerative disease characterized by
CC cerebellar ataxia, spastic paraparesis, dysarthria, and optic atrophy.
CC {ECO:0000269|PubMed:20970105}. Note=The disease is caused by variants
CC affecting the gene represented in this entry. MTPAP mutations result in
CC a defect of mitochondrial mRNA maturation. Affected individuals exhibit
CC a drastic decrease in poly(A) tail length of mitochondrial mRNA
CC transcripts, including COX1 and RNA14 (PubMed:20970105).
CC {ECO:0000269|PubMed:20970105}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; AB194709; BAD98252.1; -; mRNA.
DR EMBL; AY364242; AAQ76801.1; -; mRNA.
DR EMBL; AK001348; BAA91641.1; -; mRNA.
DR EMBL; AK022188; BAB13981.1; -; mRNA.
DR EMBL; AL122121; CAH56395.1; -; mRNA.
DR EMBL; AL161651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL353796; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86014.1; -; Genomic_DNA.
DR EMBL; CH471072; EAW86015.1; -; Genomic_DNA.
DR EMBL; BC061703; AAH61703.1; -; mRNA.
DR CCDS; CCDS7165.1; -. [Q9NVV4-1]
DR RefSeq; NP_060579.3; NM_018109.3. [Q9NVV4-1]
DR PDB; 3PQ1; X-ray; 3.10 A; A/B=44-134, A/B=172-452, A/B=490-538.
DR PDBsum; 3PQ1; -.
DR AlphaFoldDB; Q9NVV4; -.
DR SMR; Q9NVV4; -.
DR BioGRID; 120452; 181.
DR IntAct; Q9NVV4; 27.
DR MINT; Q9NVV4; -.
DR STRING; 9606.ENSP00000263063; -.
DR iPTMnet; Q9NVV4; -.
DR PhosphoSitePlus; Q9NVV4; -.
DR SwissPalm; Q9NVV4; -.
DR BioMuta; MTPAP; -.
DR DMDM; 74753002; -.
DR EPD; Q9NVV4; -.
DR jPOST; Q9NVV4; -.
DR MassIVE; Q9NVV4; -.
DR MaxQB; Q9NVV4; -.
DR PaxDb; Q9NVV4; -.
DR PeptideAtlas; Q9NVV4; -.
DR PRIDE; Q9NVV4; -.
DR ProteomicsDB; 82864; -. [Q9NVV4-1]
DR ProteomicsDB; 82865; -. [Q9NVV4-2]
DR Antibodypedia; 35309; 105 antibodies from 16 providers.
DR DNASU; 55149; -.
DR Ensembl; ENST00000263063.9; ENSP00000263063.3; ENSG00000107951.15. [Q9NVV4-1]
DR GeneID; 55149; -.
DR KEGG; hsa:55149; -.
DR MANE-Select; ENST00000263063.9; ENSP00000263063.3; NM_018109.4; NP_060579.3.
DR UCSC; uc001iva.5; human. [Q9NVV4-1]
DR CTD; 55149; -.
DR DisGeNET; 55149; -.
DR GeneCards; MTPAP; -.
DR HGNC; HGNC:25532; MTPAP.
DR HPA; ENSG00000107951; Tissue enhanced (bone).
DR MalaCards; MTPAP; -.
DR MIM; 613669; gene.
DR MIM; 613672; phenotype.
DR neXtProt; NX_Q9NVV4; -.
DR OpenTargets; ENSG00000107951; -.
DR Orphanet; 254343; Autosomal recessive spastic ataxia-optic atrophy-dysarthria syndrome.
DR PharmGKB; PA164723192; -.
DR VEuPathDB; HostDB:ENSG00000107951; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000158582; -.
DR HOGENOM; CLU_018757_3_1_1; -.
DR InParanoid; Q9NVV4; -.
DR OMA; RTVLIKC; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; Q9NVV4; -.
DR TreeFam; TF354308; -.
DR BRENDA; 2.7.7.19; 2681.
DR PathwayCommons; Q9NVV4; -.
DR SABIO-RK; Q9NVV4; -.
DR SignaLink; Q9NVV4; -.
DR BioGRID-ORCS; 55149; 501 hits in 1093 CRISPR screens.
DR ChiTaRS; MTPAP; human.
DR EvolutionaryTrace; Q9NVV4; -.
DR GenomeRNAi; 55149; -.
DR Pharos; Q9NVV4; Tbio.
DR PRO; PR:Q9NVV4; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NVV4; protein.
DR Bgee; ENSG00000107951; Expressed in oocyte and 197 other tissues.
DR ExpressionAtlas; Q9NVV4; baseline and differential.
DR Genevisible; Q9NVV4; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0002134; F:UTP binding; IDA:UniProtKB.
DR GO; GO:0071044; P:histone mRNA catabolic process; IMP:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA: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; IPR002058; PAP_assoc.
DR InterPro; IPR041252; RL.
DR InterPro; IPR045100; TUTase_dom.
DR Pfam; PF03828; PAP_assoc; 1.
DR Pfam; PF17797; RL; 1.
DR Pfam; PF19088; TUTase; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding; Cytoplasm;
KW Disease variant; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW mRNA processing; Neurodegeneration; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; RNA-binding; Transcription;
KW Transferase; Transit peptide.
FT TRANSIT 1..37
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 38..582
FT /note="Poly(A) RNA polymerase, mitochondrial"
FT /id="PRO_0000250689"
FT DOMAIN 437..483
FT /note="PAP-associated"
FT BINDING 107..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 241..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 243
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..52
FT /note="MAVPGVGLLTRLNLCARRRTRVQRPIVRLLSCPGTVAKDLRRDEQPSGSVET
FT -> MAWAKKVGGRAGQGRSLSRCDPIILDPEWLYGPPEGEGGPEGVGGETRASIHPPLR
FT TGRHHQKVNHNIRGPEGSAKDAAPGGGGHHQAGPGQRGDEDGALQHLCGGGGGVGVSVG
FT RGTGTSVAAEHPSLQVKLLELQELVLRLAGDHNEGHGKFLAAAQNPADDPAPGAPAPQE
FT LGAADKQG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_020724"
FT VARIANT 162
FT /note="R -> C (in dbSNP:rs1047991)"
FT /id="VAR_027601"
FT VARIANT 221
FT /note="Y -> H (in dbSNP:rs17855118)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027602"
FT VARIANT 419
FT /note="C -> R (in dbSNP:rs17857517)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027603"
FT VARIANT 478
FT /note="N -> D (in SPAX4; dbSNP:rs267606900)"
FT /evidence="ECO:0000269|PubMed:20970105"
FT /id="VAR_064907"
FT VARIANT 546
FT /note="S -> N (in dbSNP:rs17855116)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_027604"
FT MUTAGEN 221..222
FT /note="YF->AA: Reduces dimerization."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 230
FT /note="F->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 259..261
FT /note="HKI->AAA: No effect on dimerization. Loss of
FT dimerization and of enzyme activity; when associated with
FT 294-AAAA-297."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 294..297
FT /note="HFGP->AAGA: Reduced dimerization. Loss of
FT dimerization and of enzyme activity; when associated with
FT 259-AAA-261."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 312
FT /note="L->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 325
FT /note="D->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:21292163"
FT MUTAGEN 378
FT /note="F->A: Reduced enzyme activity."
FT /evidence="ECO:0000269|PubMed:21292163"
FT CONFLICT 507
FT /note="W -> L (in Ref. 4; BAB13981)"
FT /evidence="ECO:0000305"
FT CONFLICT 554
FT /note="V -> A (in Ref. 4; BAB13981)"
FT /evidence="ECO:0000305"
FT HELIX 64..75
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 201..218
FT /evidence="ECO:0007829|PDB:3PQ1"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 231..233
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 277..294
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:3PQ1"
FT TURN 318..320
FT /evidence="ECO:0007829|PDB:3PQ1"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 333..344
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 377..389
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 403..406
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:3PQ1"
FT TURN 482..484
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 492..510
FT /evidence="ECO:0007829|PDB:3PQ1"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:3PQ1"
SQ SEQUENCE 582 AA; 66172 MW; EBA5BECEA39A5090 CRC64;
MAVPGVGLLT RLNLCARRRT RVQRPIVRLL SCPGTVAKDL RRDEQPSGSV ETGFEDKIPK
RRFSEMQNER REQAQRTVLI HCPEKISENK FLKYLSQFGP INNHFFYESF GLYAVVEFCQ
KESIGSLQNG THTPSTAMET AIPFRSRFFN LKLKNQTSER SRVRSSNQLP RSNKQLFELL
CYAESIDDQL NTLLKEFQLT EENTKLRYLT CSLIEDMAAA YFPDCIVRPF GSSVNTFGKL
GCDLDMFLDL DETRNLSAHK ISGNFLMEFQ VKNVPSERIA TQKILSVLGE CLDHFGPGCV
GVQKILNARC PLVRFSHQAS GFQCDLTTNN RIALTSSELL YIYGALDSRV RALVFSVRCW
ARAHSLTSSI PGAWITNFSL TMMVIFFLQR RSPPILPTLD SLKTLADAED KCVIEGNNCT
FVRDLSRIKP SQNTETLELL LKEFFEYFGN FAFDKNSINI RQGREQNKPD SSPLYIQNPF
ETSLNISKNV SQSQLQKFVD LARESAWILQ QEDTDRPSIS SNRPWGLVSL LLPSAPNRKS
FTKKKSNKFA IETVKNLLES LKGNRTENFT KTSGKRTIST QT
