PAPD1_DROME
ID PAPD1_DROME Reviewed; 612 AA.
AC O46102; O46103; Q8MRT1;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Poly(A) RNA polymerase, mitochondrial {ECO:0000303|PubMed:27176048};
DE Short=DmMTPAP {ECO:0000303|PubMed:27176048};
DE EC=2.7.7.19 {ECO:0000250|UniProtKB:Q9NVV4};
DE Flags: Precursor;
GN Name=MTPAP {ECO:0000303|PubMed:27176048};
GN ORFNames=CG11418 {ECO:0000312|FlyBase:FBgn0024360};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:CAA17688.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000312|EMBL:CAA17688.2};
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAM51142.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM51142.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAM51142.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:AEW48257.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AEW48257.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=27176048; DOI=10.1371/journal.pgen.1006028;
RA Bratic A., Clemente P., Calvo-Garrido J., Maffezzini C., Felser A.,
RA Wibom R., Wedell A., Freyer C., Wredenberg A.;
RT "Mitochondrial polyadenylation is a one-step process required for mRNA
RT integrity and tRNA maturation.";
RL PLoS Genet. 12:E1006028-E1006028(2016).
CC -!- FUNCTION: Polymerase that creates the 3' poly(A) tail of mitochondrial
CC transcripts. This is not required for transcript stability or
CC translation but may maintain mRNA integrity by protecting 3' termini
CC from degradation. {ECO:0000269|PubMed:27176048}.
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:0000250|UniProtKB:Q9NVV4};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9NVV4};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:27176048}.
CC -!- DISRUPTION PHENOTYPE: Mutant male larvae die at the third instar larval
CC stage with a severe reduction in polyadenylation and increased
CC mitochondrial tRNA levels except for tRNA(Cys) which shows a marked
CC reduction and an accumulation of shortened RNAs. Mutant male larvae
CC show de novo translation of some peptides, suggesting that
CC polyadenylation is not required for translation. They also show reduced
CC assembly and activity of repiratory chain complexes I and V.
CC Heterozygous females are viable and fertile as the gene is X-linked.
CC RNAi-mediated knockdown results in reduced larval body weight, death at
CC the ferrate stage or soon after eclosion and severely reduced
CC polyadenylation in larvae. {ECO:0000269|PubMed:27176048}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B-like family.
CC {ECO:0000305}.
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DR EMBL; AL022018; CAA17688.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF45607.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB94975.1; -; Genomic_DNA.
DR EMBL; AY119282; AAM51142.1; -; mRNA.
DR EMBL; BT132966; AEW48257.1; -; mRNA.
DR PIR; T13616; T13616.
DR RefSeq; NP_001259129.1; NM_001272200.1.
DR RefSeq; NP_569904.1; NM_130548.3.
DR AlphaFoldDB; O46102; -.
DR SMR; O46102; -.
DR IntAct; O46102; 4.
DR STRING; 7227.FBpp0070227; -.
DR PaxDb; O46102; -.
DR PRIDE; O46102; -.
DR EnsemblMetazoa; FBtr0070236; FBpp0070227; FBgn0024360.
DR EnsemblMetazoa; FBtr0332288; FBpp0304567; FBgn0024360.
DR GeneID; 31081; -.
DR KEGG; dme:Dmel_CG11418; -.
DR UCSC; CG11418-RA; d. melanogaster.
DR CTD; 55149; -.
DR FlyBase; FBgn0024360; MTPAP.
DR VEuPathDB; VectorBase:FBgn0024360; -.
DR eggNOG; KOG2277; Eukaryota.
DR GeneTree; ENSGT00940000158582; -.
DR HOGENOM; CLU_018757_2_0_1; -.
DR InParanoid; O46102; -.
DR OMA; RTVLIKC; -.
DR OrthoDB; 1188122at2759; -.
DR PhylomeDB; O46102; -.
DR SignaLink; O46102; -.
DR BioGRID-ORCS; 31081; 0 hits in 1 CRISPR screen.
DR ChiTaRS; CG11418; fly.
DR GenomeRNAi; 31081; -.
DR PRO; PR:O46102; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0024360; Expressed in secondary oocyte and 27 other tissues.
DR ExpressionAtlas; O46102; baseline and differential.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central.
DR GO; GO:1990817; F:RNA adenylyltransferase activity; IMP:FlyBase.
DR GO; GO:0003723; F:RNA binding; ISS:FlyBase.
DR GO; GO:0000958; P:mitochondrial mRNA catabolic process; IMP:FlyBase.
DR GO; GO:0097222; P:mitochondrial mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; ISS:FlyBase.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR GO; GO:0036416; P:tRNA stabilization; IMP:UniProtKB.
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 2: Evidence at transcript level;
KW ATP-binding; Magnesium; Manganese; Metal-binding; Mitochondrion;
KW mRNA processing; Nucleotide-binding; Nucleotidyltransferase;
KW Reference proteome; RNA-binding; Transferase; Transit peptide.
FT TRANSIT 1..57
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 58..612
FT /note="Poly(A) RNA polymerase, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000437484"
FT DOMAIN 427..463
FT /note="PAP-associated"
FT /evidence="ECO:0000255"
FT REGION 555..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 83..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 228..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13833"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:O13833"
FT CONFLICT 90
FT /note="T -> A (in Ref. 4; AAM51142)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 68546 MW; 5153F4D627F67E1A CRC64;
MNSLVRRSAQ QLSLWRTYCI KHNASEAASP GRNAGRPNYE EFIGRHQRQA QCSIVVQVSS
EKSYEELYNY CSSFGSIMGA HHYCVRQDET LHYILLEYAT SDEAAAAIGA GVTNGELSGV
PVRSPFLWFR AAGGGRRSPK LVANTAPALL SLDGTRQVDQ RHLLGLLRGA ADIEEQVQQL
YEHTRLNELG IRMRFLAALQ VQQAIAGMFP AAQAQPFGSS VNGFGRMGCD LDLILRFDSD
MGAKIPLEAA VPSRLVYHTK ENLSNGRSQT QRHMECFGDM LHLFLPGVCH VRRILQARVP
IIKYHHEHLD LEVDLSMSNL TGFYMSELLY MFGEMDPRVR PLTFTIRRWA QTCGLTNPSP
GRWISNFSLT CLVMFFLQQL RQPILPTIGA LAKAAEPGDS RVTEDGINCT FTRNVDRLGF
RSRNQSSLSE LLLQFFEFYS QFDFHNRAIS LNEGKPLSKP DHSAMYIVNP LEQLLNVSKN
VSLEECERLR IEVRNAAWVL ESEVENASVP EGDGQELSCG LLNLFKHPEK AVIRPNMFFK
PRMVEVSDLF EQKEAGATSS STPPTPAITY KSASVRQQVQ SIKAATRSEL KQLRGSGSSV
PTSSPNNRRR SR
