ID RPC2_HUMAN Reviewed; 1133 AA. AC Q9NW08; A8K6H0; B3KV73; F5H1E6; Q9NW59; DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2003, sequence version 2. DT 27-MAR-2024, entry version 196. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC2; DE Short=RNA polymerase III subunit C2; DE EC=2.7.7.6 {ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218}; DE AltName: Full=C128; DE AltName: Full=DNA-directed RNA polymerase III 127.6 kDa polypeptide; DE AltName: Full=DNA-directed RNA polymerase III subunit B; GN Name=POLR3B {ECO:0000312|HGNC:HGNC:30348}; 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), IDENTIFICATION IN THE RNA POL III RP COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002; RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.; RT "Characterization of human RNA polymerase III identifies orthologues for RT Saccharomyces cerevisiae RNA polymerase III subunits."; RL Mol. Cell. Biol. 22:8044-8055(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Placenta, Teratocarcinoma, and Tongue; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [4] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Muscle; 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 [6] RP FUNCTION, AND SUBUNIT. RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015; RA Chiu Y.-H., Macmillan J.B., Chen Z.J.; RT "RNA polymerase III detects cytosolic DNA and induces type I interferons RT through the RIG-I pathway."; RL Cell 138:576-591(2009). RN [7] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19609254; DOI=10.1038/ni.1779; RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., RA Hornung V.; RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA RT polymerase III-transcribed RNA intermediate."; RL Nat. Immunol. 10:1065-1072(2009). RN [8] RP FUNCTION OF POL III. RX PubMed=20413673; DOI=10.1101/gr.101337.109; RA Canella D., Praz V., Reina J.H., Cousin P., Hernandez N.; RT "Defining the RNA polymerase III transcriptome: Genome-wide localization of RT the RNA polymerase III transcription machinery in human cells."; RL Genome Res. 20:710-721(2010). RN [9] 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 [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [11] RP FUNCTION OF POL III, AND SUBUNIT. RX PubMed=35637192; DOI=10.1038/s41467-022-30323-6; RA Van Bortle K., Marciano D.P., Liu Q., Chou T., Lipchik A.M., Gollapudi S., RA Geller B.S., Monte E., Kamakaka R.T., Snyder M.P.; RT "A cancer-associated RNA polymerase III identity drives robust RT transcription and expression of snaR-A non-coding RNA."; RL Nat. Commun. 13:3007-3007(2022). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=33335104; DOI=10.1038/s41467-020-20262-5; RA Ramsay E.P., Abascal-Palacios G., Daiss J.L., King H., Gouge J., Pilsl M., RA Beuron F., Morris E., Gunkel P., Engel C., Vannini A.; RT "Structure of human RNA polymerase III."; RL Nat. Commun. 11:6409-6421(2020). RN [13] RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH DNA-RNA RP HYBRID AND ZN(2+), FUNCTION, AND SUBUNIT. RX PubMed=33674783; DOI=10.1038/s41422-021-00472-2; RA Li L., Yu Z., Zhao D., Ren Y., Hou H., Xu Y.; RT "Structure of human RNA polymerase III elongation complex."; RL Cell Res. 31:791-800(2021). RN [14] RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) IN COMPLEX WITH DNA-RNA RP HYBRID AND ZN(2+), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SITE. RX PubMed=34675218; DOI=10.1038/s41467-021-26402-9; RA Hou H., Li Y., Wang M., Liu A., Yu Z., Chen K., Zhao D., Xu Y.; RT "Structural insights into RNA polymerase III-mediated transcription RT termination through trapping poly-deoxythymidine."; RL Nat. Commun. 12:6135-6146(2021). RN [15] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH DNA-RNA RP HYBRID AND ZN(2+), FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=33558764; DOI=10.1038/s41594-020-00555-5; RA Girbig M., Misiaszek A.D., Vorlander M.K., Lafita A., Grotsch H., RA Baudin F., Bateman A., Muller C.W.; RT "Cryo-EM structures of human RNA polymerase III in its unbound and RT transcribing states."; RL Nat. Struct. Mol. Biol. 28:210-219(2021). RN [16] RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH DNA-RNA RP HYBRID AND ZN(2+), FUNCTION, AND SUBUNIT. RX PubMed=33558766; DOI=10.1038/s41594-021-00557-x; RA Wang Q., Li S., Wan F., Xu Y., Wu Z., Cao M., Lan P., Lei M., Wu J.; RT "Structural insights into transcriptional regulation of human RNA RT polymerase III."; RL Nat. Struct. Mol. Biol. 28:220-227(2021). RN [17] RP VARIANTS HLD8 620-ASN--LYS-652 DEL; HIS-768 AND GLU-926, AND INVOLVEMENT IN RP HLD8. RX PubMed=22036171; DOI=10.1016/j.ajhg.2011.10.003; RA Saitsu H., Osaka H., Sasaki M., Takanashi J., Hamada K., Yamashita A., RA Shibayama H., Shiina M., Kondo Y., Nishiyama K., Tsurusaki Y., Miyake N., RA Doi H., Ogata K., Inoue K., Matsumoto N.; RT "Mutations in POLR3A and POLR3B encoding RNA Polymerase III subunits cause RT an autosomal-recessive hypomyelinating leukoencephalopathy."; RL Am. J. Hum. Genet. 89:644-651(2011). RN [18] RP VARIANTS HLD8 LYS-503 AND GLU-523. RX PubMed=22036172; DOI=10.1016/j.ajhg.2011.10.006; RA Tetreault M., Choquet K., Orcesi S., Tonduti D., Balottin U., Teichmann M., RA Fribourg S., Schiffmann R., Brais B., Vanderver A., Bernard G.; RT "Recessive mutations in POLR3B, encoding the second largest subunit of Pol RT III, cause a rare hypomyelinating leukodystrophy."; RL Am. J. Hum. Genet. 89:652-655(2011). RN [19] RP VARIANTS HLD8 PHE-104; GLY-268; CYS-442; GLU-523 AND ARG-527. RX PubMed=23355746; DOI=10.1136/jmedgenet-2012-101357; RA Daoud H., Tetreault M., Gibson W., Guerrero K., Cohen A., RA Gburek-Augustat J., Synofzik M., Brais B., Stevens C.A., RA Sanchez-Carpintero R., Goizet C., Naidu S., Vanderver A., Bernard G.; RT "Mutations in POLR3A and POLR3B are a major cause of hypomyelinating RT leukodystrophies with or without dental abnormalities and/or RT hypogonadotropic hypogonadism."; RL J. Med. Genet. 50:194-197(2013). RN [20] RP VARIANTS CMT1I LYS-363; VAL-365; VAL-375; SER-426; ARG-462 AND HIS-1046, RP CHARACTERIZATION OF VARIANTS CMT1I LYS-363; VAL-365; VAL-375; SER-426; RP ARG-462 AND HIS-1046, INVOLVEMENT IN CMT1I, AND SUBCELLULAR LOCATION. RX PubMed=33417887; DOI=10.1016/j.ajhg.2020.12.002; RA Djordjevic D., Pinard M., Gauthier M.S., Smith-Hicks C., Hoffman T.L., RA Wolf N.I., Oegema R., van Binsbergen E., Baskin B., Bernard G., RA Fribourg S., Coulombe B., Yoon G.; RT "De novo variants in POLR3B cause ataxia, spasticity, and demyelinating RT neuropathy."; RL Am. J. Hum. Genet. 108:186-193(2021). RN [21] RP VARIANT CMT1I HIS-1046, AND INVOLVEMENT IN CMT1I. RX PubMed=34666706; DOI=10.1186/s12883-021-02399-y; RA Xue Y.Y., Cheng H.L., Dong H.L., Yin H.M., Yuan Y., Meng L.C., Wu Z.Y., RA Yu H.; RT "A de novo variant of POLR3B causes demyelinating Charcot-Marie-Tooth RT disease in a Chinese patient: a case report."; RL BMC Neurol. 21:402-402(2021). CC -!- FUNCTION: Catalytic core component of RNA polymerase III (Pol III), a CC DNA-dependent RNA polymerase which synthesizes small non-coding RNAs CC using the four ribonucleoside triphosphates as substrates. Synthesizes CC 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic CC loci (PubMed:20413673, PubMed:33558766). Pol III-mediated transcription CC cycle proceeds through transcription initiation, transcription CC elongation and transcription termination stages. During transcription CC initiation, Pol III is recruited to DNA promoters type I, II or III CC with the help of general transcription factors and other specific CC initiation factors. Once the polymerase has escaped from the promoter CC it enters the elongation phase during which RNA is actively CC polymerized, based on complementarity with the template DNA strand. CC Transcription termination involves the release of the RNA transcript CC and polymerase from the DNA (PubMed:20413673, PubMed:33335104, CC PubMed:33674783, PubMed:34675218, PubMed:33558764, PubMed:33558766). CC Forms Pol III active center together with the largest subunit CC POLR3A/RPC1. A single-stranded DNA template strand of the promoter is CC positioned within the central active site cleft of Pol III. Appends one CC nucleotide at a time to the 3' end of the nascent RNA, with POLR3A/RPC1 CC contributing a Mg(2+)-coordinating DxDGD motif, and POLR3B/RPC2 CC participating in the coordination of a second Mg(2+) ion and providing CC lysine residues believed to facilitate Watson-Crick base pairing CC between the incoming nucleotide and template base. Typically, Mg(2+) CC ions direct a 5' nucleoside triphosphate to form a phosphodiester bond CC with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, CC with the elimination of pyrophosphate (PubMed:19609254, CC PubMed:33335104, PubMed:33674783, PubMed:34675218, PubMed:33558764, CC PubMed:20413673). Pol III plays a key role in sensing and limiting CC infection by intracellular bacteria and DNA viruses. Acts as a nuclear CC and cytosolic DNA sensor involved in innate immune response. Can sense CC non-self dsDNA that serves as template for transcription into dsRNA. CC The non-self RNA polymerase III transcripts, such as Epstein-Barr CC virus-encoded RNAs (EBERs) induce type I interferon and NF-kappa-B CC through the RIG-I pathway. {ECO:0000250, ECO:0000269|PubMed:19609254, CC ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20413673, CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, CC ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, CC ECO:0000269|PubMed:34675218}. 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:0000269|PubMed:19609254, CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, CC ECO:0000269|PubMed:34675218}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; CC Evidence={ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:33335104, CC ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:34675218}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P08518, CC ECO:0000250|UniProtKB:P30876}; CC Note=Two Mg(2+) ions are coordinated by both the catalytic residues and CC the nucleic acid substrate to enhance substrate recognition and CC catalytic efficiency. {ECO:0000250|UniProtKB:P08518, CC ECO:0000250|UniProtKB:P30876}; CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex CC consisting of 17 subunits: a ten-subunit catalytic core composed of CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and CC CRCP/RPC9, protruding from the core and functioning primarily in CC transcription initiation; and additional subunits homologous to general CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3- CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both CC transcription initiation and termination. {ECO:0000269|PubMed:19631370, CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, CC ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, CC ECO:0000269|PubMed:34675218}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104, CC ECO:0000269|PubMed:33417887}. Cytoplasm, cytosol CC {ECO:0000269|PubMed:33335104}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NW08-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NW08-2; Sequence=VSP_045286; CC -!- DISEASE: Leukodystrophy, hypomyelinating, 8, with or without CC oligodontia and/or hypogonadotropic hypogonadism (HLD8) [MIM:614381]: CC An autosomal recessive neurodegenerative disorder characterized by CC early childhood onset of cerebellar ataxia and mild intellectual CC disabilities associated with diffuse hypomyelination apparent on brain CC MRI. Variable features include oligodontia and/or hypogonadotropic CC hypogonadism. {ECO:0000269|PubMed:22036171, CC ECO:0000269|PubMed:22036172, ECO:0000269|PubMed:23355746}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Charcot-Marie-Tooth disease, demyelinating, 1I (CMT1I) CC [MIM:619742]: An autosomal dominant demyelinating form of Charcot- CC Marie-Tooth disease, a disorder of the peripheral nervous system, CC characterized by progressive weakness and atrophy, initially of the CC peroneal muscles and later of the distal muscles of the arms. Charcot- CC Marie-Tooth disease is classified in two main groups on the basis of CC electrophysiologic properties and histopathology: primary peripheral CC demyelinating neuropathies (designated CMT1 when they are dominantly CC inherited) and primary peripheral axonal neuropathies (CMT2). CC Demyelinating neuropathies are characterized by severely reduced nerve CC conduction velocities (less than 38 m/sec), segmental demyelination and CC remyelination with onion bulb formations on nerve biopsy, slowly CC progressive distal muscle atrophy and weakness, absent deep tendon CC reflexes, and hollow feet. CMT1I is characterized predominantly by CC delayed motor development in the first years of life associated with CC gait abnormalities, sensory ataxia, hyporeflexia, and distal sensory CC impairment due to a sensorimotor peripheral neuropathy that mainly CC affects the lower limbs. The disorder is progressive, and some may have CC upper limb involvement. A subset of patients has central nervous system CC involvement that manifests as global developmental delay with impaired CC intellectual development and speech difficulties. CC {ECO:0000269|PubMed:33417887, ECO:0000269|PubMed:34666706}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA91527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAA91581.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY092084; AAM18214.1; -; mRNA. DR EMBL; AK001161; BAA91527.1; ALT_INIT; mRNA. DR EMBL; AK001250; BAA91581.1; ALT_INIT; mRNA. DR EMBL; AK122713; BAG53685.1; -; mRNA. DR EMBL; AK291635; BAF84324.1; -; mRNA. DR EMBL; AC009721; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC078992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC080012; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW97780.1; -; Genomic_DNA. DR EMBL; BC046238; AAH46238.1; -; mRNA. DR CCDS; CCDS53824.1; -. [Q9NW08-2] DR CCDS; CCDS9105.1; -. [Q9NW08-1] DR RefSeq; NP_001154180.1; NM_001160708.1. [Q9NW08-2] DR RefSeq; NP_060552.4; NM_018082.5. [Q9NW08-1] DR PDB; 7A6H; EM; 3.30 A; B=1-1133. DR PDB; 7AE1; EM; 2.80 A; B=1-1133. DR PDB; 7AE3; EM; 3.10 A; B=1-1133. DR PDB; 7AEA; EM; 3.40 A; B=1-1133. DR PDB; 7AST; EM; 4.00 A; M=1-1133. DR PDB; 7D58; EM; 2.90 A; B=1-1133. DR PDB; 7D59; EM; 3.10 A; B=1-1133. DR PDB; 7DN3; EM; 3.50 A; B=1-1133. DR PDB; 7DU2; EM; 3.35 A; B=1-1133. DR PDB; 7FJI; EM; 3.60 A; B=1-1133. DR PDB; 7FJJ; EM; 3.60 A; B=1-1133. DR PDB; 8ITY; EM; 3.90 A; B=1-1133. DR PDB; 8IUE; EM; 4.10 A; B=1-1133. DR PDB; 8IUH; EM; 3.40 A; B=1-1133. DR PDBsum; 7A6H; -. DR PDBsum; 7AE1; -. DR PDBsum; 7AE3; -. DR PDBsum; 7AEA; -. DR PDBsum; 7AST; -. DR PDBsum; 7D58; -. DR PDBsum; 7D59; -. DR PDBsum; 7DN3; -. DR PDBsum; 7DU2; -. DR PDBsum; 7FJI; -. DR PDBsum; 7FJJ; -. DR PDBsum; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR AlphaFoldDB; Q9NW08; -. DR EMDB; EMD-11673; -. DR EMDB; EMD-11736; -. DR EMDB; EMD-11738; -. DR EMDB; EMD-11742; -. DR EMDB; EMD-11904; -. DR EMDB; EMD-30577; -. DR EMDB; EMD-30578; -. DR EMDB; EMD-30779; -. DR EMDB; EMD-30865; -. DR EMDB; EMD-31621; -. DR EMDB; EMD-31622; -. DR EMDB; EMD-35712; -. DR EMDB; EMD-35719; -. DR EMDB; EMD-35722; -. DR SMR; Q9NW08; -. DR BioGRID; 120828; 127. DR ComplexPortal; CPX-2393; DNA-directed RNA polymerase III complex, POLR3G variant. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR IntAct; Q9NW08; 25. DR MINT; Q9NW08; -. DR STRING; 9606.ENSP00000228347; -. DR GlyGen; Q9NW08; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NW08; -. DR MetOSite; Q9NW08; -. DR PhosphoSitePlus; Q9NW08; -. DR BioMuta; POLR3B; -. DR DMDM; 29428029; -. DR EPD; Q9NW08; -. DR jPOST; Q9NW08; -. DR MassIVE; Q9NW08; -. DR MaxQB; Q9NW08; -. DR PaxDb; 9606-ENSP00000228347; -. DR PeptideAtlas; Q9NW08; -. DR ProteomicsDB; 25631; -. DR ProteomicsDB; 82885; -. [Q9NW08-1] DR Pumba; Q9NW08; -. DR Antibodypedia; 30662; 198 antibodies from 28 providers. DR DNASU; 55703; -. DR Ensembl; ENST00000228347.9; ENSP00000228347.4; ENSG00000013503.10. [Q9NW08-1] DR Ensembl; ENST00000539066.5; ENSP00000445721.1; ENSG00000013503.10. [Q9NW08-2] DR GeneID; 55703; -. DR KEGG; hsa:55703; -. DR MANE-Select; ENST00000228347.9; ENSP00000228347.4; NM_018082.6; NP_060552.4. DR UCSC; uc001tlp.3; human. [Q9NW08-1] DR AGR; HGNC:30348; -. DR CTD; 55703; -. DR DisGeNET; 55703; -. DR GeneCards; POLR3B; -. DR GeneReviews; POLR3B; -. DR HGNC; HGNC:30348; POLR3B. DR HPA; ENSG00000013503; Low tissue specificity. DR MalaCards; POLR3B; -. DR MIM; 614366; gene. DR MIM; 614381; phenotype. DR MIM; 619742; phenotype. DR neXtProt; NX_Q9NW08; -. DR OpenTargets; ENSG00000013503; -. DR Orphanet; 85186; Endosteal sclerosis-cerebellar hypoplasia syndrome. DR Orphanet; 88637; Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome. DR PharmGKB; PA134867680; -. DR VEuPathDB; HostDB:ENSG00000013503; -. DR eggNOG; KOG0215; Eukaryota. DR GeneTree; ENSGT00950000183132; -. DR HOGENOM; CLU_000524_5_1_1; -. DR InParanoid; Q9NW08; -. DR OMA; LAYCSWC; -. DR OrthoDB; 5476750at2759; -. DR PhylomeDB; Q9NW08; -. DR TreeFam; TF103047; -. DR PathwayCommons; Q9NW08; -. DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA. DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation. DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter. DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter. DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR SignaLink; Q9NW08; -. DR SIGNOR; Q9NW08; -. DR BioGRID-ORCS; 55703; 834 hits in 1173 CRISPR screens. DR ChiTaRS; POLR3B; human. DR GenomeRNAi; 55703; -. DR Pharos; Q9NW08; Tbio. DR PRO; PR:Q9NW08; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9NW08; Protein. DR Bgee; ENSG00000013503; Expressed in secondary oocyte and 165 other cell types or tissues. DR ExpressionAtlas; Q9NW08; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC. DR GO; GO:0071667; F:DNA/RNA hybrid binding; IDA:UniProtKB. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB. DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IDA:UniProtKB. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1100.10; -; 2. DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1. DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom. DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF8; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC2; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. DR Genevisible; Q9NW08; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Antiviral defense; KW Charcot-Marie-Tooth disease; Cytoplasm; Disease variant; KW DNA-directed RNA polymerase; Immunity; Innate immunity; Leukodystrophy; KW Magnesium; Metal-binding; Neurodegeneration; Neuropathy; KW Nucleotidyltransferase; Nucleus; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1..1133 FT /note="DNA-directed RNA polymerase III subunit RPC2" FT /id="PRO_0000048092" FT ZN_FING 1080..1095 FT /note="C4-type" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 186 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7FJJ" FT BINDING 195 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="nontemplate strand" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0007744|PDB:7AE1" FT BINDING 213 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7FJJ" FT BINDING 432 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="nontemplate strand" FT /evidence="ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7FJJ" FT BINDING 438 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:33674783, FT ECO:0007744|PDB:7DN3" FT BINDING 692 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7FJJ" FT BINDING 753 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with POLR3A/RPC1" FT /evidence="ECO:0000250|UniProtKB:P08518, FT ECO:0000250|UniProtKB:P30876" FT BINDING 896 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:33674783, FT ECO:0000269|PubMed:34675218, ECO:0007744|PDB:7DN3, FT ECO:0007744|PDB:7FJJ" FT BINDING 904 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0007744|PDB:7AE1, FT ECO:0007744|PDB:7D58" FT BINDING 1019 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7FJJ" FT BINDING 1039 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000269|PubMed:33558766, FT ECO:0000269|PubMed:33674783, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 1040 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0007744|PDB:7AE1" FT BINDING 1046 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7FJJ" FT BINDING 1080 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 1083 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33674783, ECO:0000269|PubMed:34675218, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7DN3, FT ECO:0007744|PDB:7FJJ" FT BINDING 1092 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, FT ECO:0000269|PubMed:34675218, ECO:0007744|PDB:7AE1, FT ECO:0007744|PDB:7D58, ECO:0007744|PDB:7DN3, FT ECO:0007744|PDB:7FJJ" FT BINDING 1095 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, FT ECO:0000269|PubMed:34675218, ECO:0007744|PDB:7AE1, FT ECO:0007744|PDB:7D58, ECO:0007744|PDB:7DN3, FT ECO:0007744|PDB:7FJJ" FT SITE 429 FT /note="Critical in trapping poly(dT) in Pol III-mediated FT transcription termination" FT /evidence="ECO:0000305|PubMed:34675218" FT VAR_SEQ 1..58 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045286" FT VARIANT 104 FT /note="L -> F (in HLD8)" FT /evidence="ECO:0000269|PubMed:23355746" FT /id="VAR_072344" FT VARIANT 268 FT /note="S -> G (in HLD8)" FT /evidence="ECO:0000269|PubMed:23355746" FT /id="VAR_072345" FT VARIANT 363 FT /note="E -> K (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization)" FT /evidence="ECO:0000269|PubMed:33417887" FT /id="VAR_086912" FT VARIANT 365 FT /note="A -> V (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization; FT dbSNP:rs2037218302)" FT /evidence="ECO:0000269|PubMed:33417887" FT /id="VAR_086913" FT VARIANT 375 FT /note="D -> V (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization; FT dbSNP:rs2037451945)" FT /evidence="ECO:0000269|PubMed:33417887" FT /id="VAR_086914" FT VARIANT 426 FT /note="L -> S (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization; FT dbSNP:rs2037490138)" FT /evidence="ECO:0000269|PubMed:33417887" FT /id="VAR_086915" FT VARIANT 442 FT /note="R -> C (in HLD8; dbSNP:rs1442212683)" FT /evidence="ECO:0000269|PubMed:23355746" FT /id="VAR_072346" FT VARIANT 462 FT /note="T -> R (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization; FT dbSNP:rs2037492289)" FT /evidence="ECO:0000269|PubMed:33417887" FT /id="VAR_086916" FT VARIANT 503 FT /note="T -> K (in HLD8; dbSNP:rs267608683)" FT /evidence="ECO:0000269|PubMed:22036172" FT /id="VAR_067005" FT VARIANT 523 FT /note="V -> E (in HLD8; dbSNP:rs138249161)" FT /evidence="ECO:0000269|PubMed:22036172, FT ECO:0000269|PubMed:23355746" FT /id="VAR_067006" FT VARIANT 527 FT /note="C -> R (in HLD8)" FT /evidence="ECO:0000269|PubMed:23355746" FT /id="VAR_072347" FT VARIANT 620..652 FT /note="Missing (in HLD8)" FT /evidence="ECO:0000269|PubMed:22036171" FT /id="VAR_067007" FT VARIANT 740 FT /note="T -> A (in dbSNP:rs17038460)" FT /id="VAR_057255" FT VARIANT 768 FT /note="R -> H (in HLD8; dbSNP:rs267608687)" FT /evidence="ECO:0000269|PubMed:22036171" FT /id="VAR_067008" FT VARIANT 926 FT /note="D -> E (in HLD8; dbSNP:rs267608689)" FT /evidence="ECO:0000269|PubMed:22036171" FT /id="VAR_067009" FT VARIANT 1046 FT /note="R -> H (in CMT1I; affects RNA polymerase III FT assembly; no effect on nuclear localization; FT dbSNP:rs2038648611)" FT /evidence="ECO:0000269|PubMed:33417887, FT ECO:0000269|PubMed:34666706" FT /id="VAR_086917" FT CONFLICT 258 FT /note="E -> A (in Ref. 1; AAM18214)" FT /evidence="ECO:0000305" FT CONFLICT 607 FT /note="T -> I (in Ref. 2; BAG53685)" FT /evidence="ECO:0000305" FT CONFLICT 978 FT /note="R -> C (in Ref. 2; BAA91527)" FT /evidence="ECO:0000305" FT HELIX 26..28 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 29..34 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 37..40 FT /evidence="ECO:0007829|PDB:7AE3" FT HELIX 41..52 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 54..60 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 64..66 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 68..70 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 86..88 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 90..92 FT /evidence="ECO:0007829|PDB:7D58" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 99..105 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 110..119 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 121..124 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 126..137 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 142..145 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 146..149 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 152..155 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 156..159 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 174..178 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 180..184 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 190..193 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 194..196 FT /evidence="ECO:0007829|PDB:7DU2" FT STRAND 199..204 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:7D58" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 224..226 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 230..232 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 236..242 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 248..255 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 259..272 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 273..276 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 280..288 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 307..315 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 316..320 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 329..346 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 357..359 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 360..363 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 365..391 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 396..398 FT /evidence="ECO:0007829|PDB:7D58" FT HELIX 402..405 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 409..421 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 427..429 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 431..433 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 437..439 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 445..451 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 454..456 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 461..463 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 467..470 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 473..475 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 476..478 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 488..492 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 493..496 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 509..515 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 516..519 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 523..525 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 529..532 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 533..535 FT /evidence="ECO:0007829|PDB:7D59" FT STRAND 537..541 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 544..550 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 552..564 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 566..568 FT /evidence="ECO:0007829|PDB:7D58" FT STRAND 573..577 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 578..581 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 582..586 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 592..600 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 603..605 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 608..615 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 621..626 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 629..634 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 635..640 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 643..646 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 647..649 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 661..664 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 669..671 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 672..674 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 675..677 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 680..692 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 699..702 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 707..714 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 719..721 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 723..727 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 730..732 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 737..744 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 751..753 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 755..758 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 759..764 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 765..767 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 769..779 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 783..785 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 797..799 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 800..802 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 804..806 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 807..809 FT /evidence="ECO:0007829|PDB:7D59" FT STRAND 813..815 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 825..828 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 830..833 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 851..853 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 856..858 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 864..873 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 879..889 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 896..898 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 900..902 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 905..911 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 913..915 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 920..922 FT /evidence="ECO:0007829|PDB:7AE3" FT STRAND 926..929 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 933..937 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 940..953 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 954..956 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 969..978 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 983..987 FT /evidence="ECO:0007829|PDB:7D58" FT TURN 992..994 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 995..997 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1002..1013 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 1016..1018 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1021..1025 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1030..1032 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 1039..1042 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1045..1047 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 1049..1057 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 1061..1068 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 1069..1072 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1074..1080 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 1081..1083 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1086..1088 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 1093..1096 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1097..1107 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 1108..1119 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 1123..1130 FT /evidence="ECO:0007829|PDB:7AE1" SQ SEQUENCE 1133 AA; 127785 MW; F0B3AFF892DDED7D CRC64; MDVLAEEFGN LTPEQLAAPI PTVEEKWRLL PAFLKVKGLV KQHIDSFNYF INVEIKKIMK ANEKVTSDAD PMWYLKYLNI YVGLPDVEES FNVTRPVSPH ECRLRDMTYS APITVDIEYT RGSQRIIRNA LPIGRMPIML RSSNCVLTGK TPAEFAKLNE CPLDPGGYFI VKGVEKVILI QEQLSKNRII VEADRKGAVG ASVTSSTHEK KSRTNMAVKQ GRFYLRHNTL SEDIPIVIIF KAMGVESDQE IVQMIGTEEH VMAAFGPSLE ECQKAQIFTQ MQALKYIGNK VRRQRMWGGG PKKTKIEEAR ELLASTILTH VPVKEFNFRA KCIYTAVMVR RVILAQGDNK VDDRDYYGNK RLELAGQLLS LLFEDLFKKF NSEMKKIADQ VIPKQRAAQF DVVKHMRQDQ ITNGMVNAIS TGNWSLKRFK MDRQGVTQVL SRLSYISALG MMTRISSQFE KTRKVSGPRS LQPSQWGMLC PSDTPEGEAC GLVKNLALMT HITTDMEDGP IVKLASNLGV EDVNLLCGEE LSYPNVFLVF LNGNILGVIR DHKKLVNTFR LMRRAGYINE FVSISTNLTD RCVYISSDGG RLCRPYIIVK KQKPAVTNKH MEELAQGYRN FEDFLHESLV EYLDVNEEND CNIALYEHTI NKDTTHLEIE PFTLLGVCAG LIPYPHHNQS PRNTYQCAMG KQAMGTIGYN QRNRIDTLMY LLAYPQKPMV KTKTIELIEF EKLPAGQNAT VAVMSYSGYD IEDALVLNKA SLDRGFGRCL VYKNAKCTLK RYTNQTFDKV MGPMLDAATR KPIWRHEILD ADGICSPGEK VENKQVLVNK SMPTVTQIPL EGSNVPQQPQ YKDVPITYKG ATDSYIEKVM ISSNAEDAFL IKMLLRQTRR PEIGDKFSSR HGQKGVCGLI VPQEDMPFCD SGICPDIIMN PHGFPSRMTV GKLIELLAGK AGVLDGRFHY GTAFGGSKVK DVCEDLVRHG YNYLGKDYVT SGITGEPLEA YIYFGPVYYQ KLKHMVLDKM HARARGPRAV LTRQPTEGRS RDGGLRLGEM ERDCLIGYGA SMLLLERLMI SSDAFEVDVC GQCGLLGYSG WCHYCKSSCH VSSLRIPYAC KLLFQELQSM NIIPRLKLSK YNE //