RPOM_MOUSE
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 03-AUG-2022, entry version 147.
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. {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; Q8BKF1; -.
DR PRIDE; Q8BKF1; -.
DR ProteomicsDB; 299927; -.
DR Antibodypedia; 1270; 110 antibodies from 29 providers.
DR DNASU; 216151; -.
DR Ensembl; ENSMUST00000020580; ENSMUSP00000020580; ENSMUSG00000020329.
DR GeneID; 216151; -.
DR KEGG; mmu:216151; -.
DR UCSC; uc007fzo.2; mouse.
DR CTD; 5442; -.
DR MGI; MGI:1915843; Polrmt.
DR VEuPathDB; HostDB:ENSMUSG00000020329; -.
DR eggNOG; KOG1038; Eukaryota.
DR GeneTree; ENSGT00390000008060; -.
DR InParanoid; Q8BKF1; -.
DR OMA; YAEEIMP; -.
DR OrthoDB; 135329at2759; -.
DR PhylomeDB; Q8BKF1; -.
DR TreeFam; TF105700; -.
DR Reactome; R-MMU-163282; Mitochondrial transcription initiation.
DR BioGRID-ORCS; 216151; 23 hits in 75 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 264 other tissues.
DR ExpressionAtlas; Q8BKF1; baseline and differential.
DR Genevisible; Q8BKF1; MM.
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: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 from mitochondrial promoter; ISO:MGI.
DR Gene3D; 1.10.1320.10; -; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR002092; DNA-dir_Rpol_phage-type.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002885; Pentatricopeptide_repeat.
DR InterPro; IPR037159; RNA_POL_N_sf.
DR InterPro; IPR029262; RPOL_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR10102; PTHR10102; 1.
DR Pfam; PF00940; RNA_pol; 1.
DR Pfam; PF14700; RPOL_N; 1.
DR SMART; SM01311; RPOL_N; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR TIGRFAMs; TIGR00756; PPR; 1.
DR PROSITE; PS51375; PPR; 2.
DR PROSITE; PS00900; RNA_POL_PHAGE_1; 1.
DR PROSITE; PS00489; RNA_POL_PHAGE_2; 1.
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
