ID   RPOM_MOUSE              Reviewed;        1207 AA.
AC   Q8BKF1; Q8BJE0;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   24-JAN-2024, entry version 155.
DE   RecName: Full=DNA-directed RNA polymerase, mitochondrial {ECO:0000305};
DE            Short=MtRPOL;
DE            EC=2.7.7.6;
DE   Flags: Precursor;
GN   Name=Polrmt {ECO:0000312|MGI:MGI:1915843};
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=Eye, and Mammary gland;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, and Heart;
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).
RN   [3]
RP   IDENTIFICATION IN A COMPLEX WITH SIRT3 AND FOXO3, AND SUBCELLULAR LOCATION.
RX   PubMed=23283301; DOI=10.1007/s00018-012-1244-6;
RA   Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D.,
RA   Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G.,
RA   Puri P.L., Sartorelli V., Simone C.;
RT   "A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing
RT   glucose levels.";
RL   Cell. Mol. Life Sci. 70:2015-2029(2013).
CC   -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC       mitochondrial DNA into RNA using the four ribonucleoside triphosphates
CC       as substrates. Component of the mitochondrial transcription initiation
CC       complex, composed at least of TFB2M, TFAM and POLRMT that is required
CC       for basal transcription of mitochondrial DNA. In this complex, TFAM
CC       recruits POLRMT to a specific promoter whereas TFB2M induces structural
CC       changes in POLRMT to enable promoter opening and trapping of the DNA
CC       non-template strand. Has DNA primase activity. Catalyzes the synthesis
CC       of short RNA primers that are necessary for the initiation of lagging-
CC       strand DNA synthesis from the origin of light-strand DNA replication
CC       (OriL). {ECO:0000250|UniProtKB:O00411}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC         RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC         COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC         EC=2.7.7.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10031,
CC         ECO:0000255|PROSITE-ProRule:PRU10032};
CC   -!- SUBUNIT: Homodimer. Component of the mitochondrial transcription
CC       initiation complex, composed at least of TFB2M, TFAM and POLRMT. In
CC       this complex TFAM recruits POLRMT to the promoter whereas TFB2M induces
CC       structural changes in POLRMT to enable promoter opening and trapping of
CC       the DNA non-template strand (By similarity). Upon metabolic stress,
CC       forms a complex composed of FOXO3, SIRT3 and mitochondrial RNA
CC       polymerase POLRMT; the complex is recruited to mtDNA in a SIRT3-
CC       dependent manner (PubMed:23283301). Also forms a complex composed of
CC       FOXO3, SIRT3, TFAM and POLRMT. Interacts with TFB1M and TFB2M, leading
CC       to the stimulation of transcription. Interacts with TEFM. Interacts
CC       with MTRES1 (By similarity). {ECO:0000250|UniProtKB:O00411,
CC       ECO:0000269|PubMed:23283301}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23283301}.
CC   -!- SIMILARITY: Belongs to the phage and mitochondrial RNA polymerase
CC       family. {ECO:0000305}.
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DR   EMBL; AK053356; BAC35360.1; -; mRNA.
DR   EMBL; AK085666; BAC39500.1; -; mRNA.
DR   CCDS; CCDS23987.1; -.
DR   RefSeq; NP_766139.2; NM_172551.3.
DR   AlphaFoldDB; Q8BKF1; -.
DR   SMR; Q8BKF1; -.
DR   BioGRID; 229707; 3.
DR   STRING; 10090.ENSMUSP00000020580; -.
DR   iPTMnet; Q8BKF1; -.
DR   PhosphoSitePlus; Q8BKF1; -.
DR   EPD; Q8BKF1; -.
DR   MaxQB; Q8BKF1; -.
DR   PaxDb; 10090-ENSMUSP00000020580; -.
DR   ProteomicsDB; 299927; -.
DR   Pumba; Q8BKF1; -.
DR   Antibodypedia; 1270; 128 antibodies from 29 providers.
DR   DNASU; 216151; -.
DR   Ensembl; ENSMUST00000020580.13; ENSMUSP00000020580.7; ENSMUSG00000020329.13.
DR   GeneID; 216151; -.
DR   KEGG; mmu:216151; -.
DR   UCSC; uc007fzo.2; mouse.
DR   AGR; MGI:1915843; -.
DR   CTD; 5442; -.
DR   MGI; MGI:1915843; Polrmt.
DR   VEuPathDB; HostDB:ENSMUSG00000020329; -.
DR   eggNOG; KOG1038; Eukaryota.
DR   GeneTree; ENSGT00390000008060; -.
DR   InParanoid; Q8BKF1; -.
DR   OMA; WWAKSDE; -.
DR   OrthoDB; 143789at2759; -.
DR   PhylomeDB; Q8BKF1; -.
DR   TreeFam; TF105700; -.
DR   Reactome; R-MMU-163282; Mitochondrial transcription initiation.
DR   BioGRID-ORCS; 216151; 23 hits in 79 CRISPR screens.
DR   ChiTaRS; Polrmt; mouse.
DR   PRO; PR:Q8BKF1; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q8BKF1; Protein.
DR   Bgee; ENSMUSG00000020329; Expressed in heart right ventricle and 268 other cell types or tissues.
DR   ExpressionAtlas; Q8BKF1; baseline and differential.
DR   GO; GO:0034245; C:mitochondrial DNA-directed RNA polymerase complex; IBA:GO_Central.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; ISO:MGI.
DR   GO; GO:0003896; F:DNA primase activity; ISS:UniProtKB.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISO:MGI.
DR   GO; GO:0001018; F:mitochondrial promoter sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0006390; P:mitochondrial transcription; ISO:MGI.
DR   GO; GO:0006391; P:transcription initiation at mitochondrial promoter; ISO:MGI.
DR   Gene3D; 1.10.287.280; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 1.10.1320.10; DNA-directed RNA polymerase, N-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR046950; DNA-dir_Rpol_C_phage-type.
DR   InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR037159; RNA_POL_N_sf.
DR   InterPro; IPR029262; RPOL_N.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
DR   PANTHER; PTHR10102; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR10102:SF0; DNA-DIRECTED RNA POLYMERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00940; RNA_pol; 1.
DR   Pfam; PF14700; RPOL_N; 1.
DR   SMART; SM01311; RPOL_N; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   PROSITE; PS51375; PPR; 2.
DR   PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR   PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
DR   Genevisible; Q8BKF1; MM.
PE   1: Evidence at protein level;
KW   DNA-directed RNA polymerase; Mitochondrion; Nucleotidyltransferase;
KW   Reference proteome; Repeat; Transcription; Transferase; Transit peptide.
FT   TRANSIT         1..41
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           42..1207
FT                   /note="DNA-directed RNA polymerase, mitochondrial"
FT                   /id="PRO_0000031069"
FT   REPEAT          232..266
FT                   /note="PPR 1"
FT   REPEAT          267..302
FT                   /note="PPR 2"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          82..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..724
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..1207
FT                   /note="Mediates interaction with TEFM"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        893
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        962
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1121
FT                   /evidence="ECO:0000250"
FT   CONFLICT        23
FT                   /note="H -> Q (in Ref. 1; BAC39500)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1207 AA;  136705 MW;  674601A6BC001CE4 CRC64;
     MSALRWTRSA AGLGRVLRSP GPHRPPSEEG TFGGFCSSRR SSAASPREQH VLREWGHAEL
     LEVLEARVRQ LRAEGTPEMR VKKVQVDRPP QGHSSRWAQK LEAEKRVKQR RQKEVDQQKQ
     ALTQEFWTLH KEPKIWNKKL AGYLQPSKKG TPTNSEEKQL AQALQAALGR LSSREAEALA
     RKKAKAVEAQ ILVLQQKFLA FFECCVCTGQ VPLAHHVLVT HHNNGDRQQV LTLHMYNTVM
     LGWARKGSFR ELVYVFLMLK DAGLSPDLCS YAAALQCMGR RDQDVRTIQR CLKQMMEEGF
     QPQLLFTDLV LEEEDRAALL RAVVKAEPAF RPPPQAPSPV NTSTLLKDIY SKEGPVSYPK
     LHLPLDTLQD LFYQQLHVEL SSSVCVQSVE KAPVMSKEVI EARKTLQALR EQWEVELLRV
     LRETKATMGR QAYEGQPTLY PFLCLLSEGE FVSILMQVLK VLPAQGEPLI QLAHNLGLRV
     LNRHLVKQKQ VTNHVQKLGQ RYSQYLQLLA SDTQVAPCLP REYWESLGPL EAPAQQPWSV
     PVLLQLGKQL AELLVQAVQM PRSLAARQGA QRSIPVLYHV YSFRSYRQVG ILKPHPAFTH
     LLETAAEPTL TFETTEVPML CPPLPWTSLH SGAYLLSSTK LMRATEGTTQ HQRLLEQCPP
     AQLHGPLDAL TQLGNCAWRV NGHLLDLVLQ IFRDKGCMPL GVPPPRSEAP RPARYQLPPG
     STPVHKSELR KELARCLKVA REMHSLRSEA LYRLSLAQHL RHRVFWLPHN MDFRGRTYPC
     PPHFNHLGSD LARALLEFAE GRPLGPRGLD WLKIHLINLT GLKKGDSLRM RLAFADEVME
     EILDSADNPL TGRKWWMEAD EPWQTLACCM EVAHAVRSPD PAAYISHLPV HQDGSCNGLQ
     HYAALGRDSV GAASVNLTPS DLPQDVYREV ATQVEEFRQQ DAKEGLRVAQ VLEGFISRKV
     VKQTVMTVVY GVTRYGGRLQ IEKRLRELSD FPQEFVWEAS HYLVRQVFKS LQEMFTSTRA
     IQHWLTESAN LISHAGWPVE WVTPLGIPII QPYHRESKVQ VKGGLQSITL TSSVDESQKP
     NTLKQKNGFP PNFIHSLDSS HMMLTALHCY RKGLIFVSVH DCFWTHAADI PTMNEVCREQ
     FVRLHSQPIL EDLAKFLKKR FCSVSSIKSL KSSERALVTK LQETLQSLPK TGTFDLGQVI
     RSTYFFS
//