ID RPA2_HUMAN Reviewed; 1135 AA. AC Q9H9Y6; B7Z6Y7; B7Z823; F5GZX4; F8W898; Q2TAM4; Q585T5; Q6ZRR2; Q9H9D3; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=DNA-directed RNA polymerase I subunit RPA2; DE Short=RNA polymerase I subunit 2; DE EC=2.7.7.6 {ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}; DE AltName: Full=DNA-directed RNA polymerase I 135 kDa polypeptide; DE Short=RPA135; GN Name=POLR1B {ECO:0000303|PubMed:31649276, GN ECO:0000312|HGNC:HGNC:20454}; 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 [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4), AND RP VARIANTS LEU-295 AND ARG-887 (ISOFORM 4). RC TISSUE=Spleen, and Testis; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5), AND VARIANT LEU-295. RC TISSUE=Pancreas; 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 [4] RP FUNCTION OF POL I PIC, AND SUBUNIT. RX PubMed=11250903; DOI=10.1093/emboj/20.6.1373; RA Miller G., Panov K.I., Friedrich J.K., Trinkle-Mulcahy L., Lamond A.I., RA Zomerdijk J.C.B.M.; RT "hRRN3 is essential in the SL1-mediated recruitment of RNA polymerase I to RT rRNA gene promoters."; RL EMBO J. 20:1373-1382(2001). RN [5] RP FUNCTION OF POL I PIC, AND SUBUNIT. RX PubMed=11283244; DOI=10.1128/mcb.21.8.2641-2649.2001; RA Panov K.I., Friedrich J.K., Zomerdijk J.C.; RT "A step subsequent to preinitiation complex assembly at the ribosomal RNA RT gene promoter is rate limiting for human RNA polymerase I-dependent RT transcription."; RL Mol. Cell. Biol. 21:2641-2649(2001). RN [6] RP FUNCTION OF POL I PIC, AND SUBUNIT. RX PubMed=16858408; DOI=10.1038/sj.emboj.7601221; RA Panov K.I., Friedrich J.K., Russell J., Zomerdijk J.C.; RT "UBF activates RNA polymerase I transcription by stimulating promoter RT escape."; RL EMBO J. 25:3310-3322(2006). RN [7] RP IDENTIFICATION IN THE RNA POL I COMPLEX, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16809778; DOI=10.1128/mcb.00230-06; RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., RA Zomerdijk J.C.B.M.; RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation RT of transcription by upstream binding factor."; RL Mol. Cell. Biol. 26:5436-5448(2006). RN [8] 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1051, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [10] RP STRUCTURE BY ELECTRON MICROSCOPY (2.81 ANGSTROMS) OF 1-1719 IN COMPLEX WITH RP DNA-RNA HYBRID AND ZN(2+), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, DOMAIN, RP AND SITE. RX PubMed=34671025; DOI=10.1038/s41421-021-00335-5; RA Zhao D., Liu W., Chen K., Wu Z., Yang H., Xu Y.; RT "Structure of the human RNA polymerase I elongation complex."; RL Cell Discov. 7:97-109(2021). RN [11] RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS) IN COMPLEX WITH DNA-RNA RP HYBRID AND ZN(2+), FUNCTION OF POL I, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=34887565; DOI=10.1038/s41594-021-00693-4; RA Misiaszek A.D., Girbig M., Grotsch H., Baudin F., Murciano B., Lafita A., RA Muller C.W.; RT "Cryo-EM structures of human RNA polymerase I."; RL Nat. Struct. Mol. Biol. 28:997-1008(2021). RN [12] RP STRUCTURE BY ELECTRON MICROSCOPY (4.09 ANGSTROMS), FUNCTION, CATALYTIC RP ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=36271492; DOI=10.26508/lsa.202201568; RA Daiss J.L., Pilsl M., Straub K., Bleckmann A., Hocherl M., Heiss F.B., RA Abascal-Palacios G., Ramsay E.P., Tluckova K., Mars J.C., Furtges T., RA Bruckmann A., Rudack T., Bernecky C., Lamour V., Panov K., Vannini A., RA Moss T., Engel C.; RT "The human RNA polymerase I structure reveals an HMG-like docking domain RT specific to metazoans."; RL Life. Sci Alliance 5:1-20(2022). RN [13] RP INVOLVEMENT IN TCS4, AND VARIANTS TCS4 ARG-682; CYS-1003 AND SER-1003. RX PubMed=31649276; DOI=10.1038/s41436-019-0669-9; RA Sanchez E., Laplace-Builhe B., Mau-Them F.T., Richard E., Goldenberg A., RA Toler T.L., Guignard T., Gatinois V., Vincent M., Blanchet C., Boland A., RA Bihoreau M.T., Deleuze J.F., Olaso R., Nephi W., Luedecke H.J., RA Verheij J.B.G.M., Moreau-Lenoir F., Denoyelle F., Riviere J.B., RA Laplanche J.L., Willing M., Captier G., Apparailly F., Wieczorek D., RA Collet C., Djouad F., Genevieve D.; RT "POLR1B and neural crest cell anomalies in Treacher Collins syndrome type RT 4."; RL Genet. Med. 22:547-556(2020). CC -!- FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA- CC dependent RNA polymerase which synthesizes ribosomal RNA precursors CC using the four ribonucleoside triphosphates as substrates. Transcribes CC 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, CC 18S and 28S ribosomal RNAs (PubMed:34671025, PubMed:34887565, CC PubMed:36271492, PubMed:11250903, PubMed:11283244, PubMed:16858408). CC Pol I-mediated transcription cycle proceeds through transcription CC initiation, transcription elongation and transcription termination CC stages. During transcription initiation, Pol I pre-initiation complex CC (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex CC bound to the core promoter that precedes an rDNA repeat unit. The PIC CC assembly bends the promoter favoring the formation of the transcription CC bubble and promoter escape. Once the polymerase has escaped from the CC promoter it enters the elongation phase during which RNA is actively CC polymerized, based on complementarity with the template DNA strand. CC Highly processive, assembles in structures referred to as 'Miller CC trees' where many elongating Pol I complexes queue and transcribe the CC same rDNA coding regions. At terminator sequences downstream of the CC rDNA gene, PTRF interacts with Pol I and halts Pol I transcription CC leading to the release of the RNA transcript and polymerase from the CC DNA (PubMed:34671025, PubMed:34887565, PubMed:36271492, CC PubMed:11250903, PubMed:11283244, PubMed:16858408). Forms Pol I active CC center together with the largest subunit POLR1A/RPA1. Appends one CC nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 CC contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 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 the template base. Typically, CC Mg(2+) ions direct a 5' nucleoside triphosphate to form a CC phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of CC the nascent RNA, with the elimination of pyrophosphate. Has CC proofreading activity: Pauses and backtracks to allow the cleavage of a CC missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity CC is associated with decreased transcription fidelity (PubMed:34671025, CC PubMed:34887565, PubMed:36271492, PubMed:11250903, PubMed:11283244, CC PubMed:16858408, PubMed:16809778) (By similarity). CC {ECO:0000250|UniProtKB:P10964, ECO:0000269|PubMed:11250903, CC ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16809778, CC ECO:0000269|PubMed:16858408, ECO:0000269|PubMed:34671025, CC ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}. 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:16809778, CC ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, CC ECO:0000269|PubMed:36271492}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; CC Evidence={ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:34671025, CC ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}; 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 I (Pol I) complex consisting CC of 13 subunits: a ten-subunit catalytic core composed of POLR1A/RPA1, CC POLR1B/RPA2, POLR1C/RPAC1, POLR1D/RPAC2, POLR1H/RPA12, POLR2E/RPABC1, CC POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile CC stalk subunit POLR1F/RPA43 protruding from the core and additional CC subunits homologous to general transcription factors POLR1E/RPA49 and CC POLR1G/RPA34 (PubMed:16809778, PubMed:34671025, PubMed:34887565, CC PubMed:36271492). Part of Pol I pre-initiation complex (PIC), in which CC Pol I core assembles with RRN3 and promoter-bound UTBF and SL1/TIF-IB CC complex (PubMed:11283244, PubMed:16809778, PubMed:11250903, CC PubMed:16858408). {ECO:0000269|PubMed:11250903, CC ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16809778, CC ECO:0000269|PubMed:16858408, ECO:0000269|PubMed:34671025, CC ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}. CC -!- INTERACTION: CC Q9H9Y6; O95602: POLR1A; NbExp=3; IntAct=EBI-355441, EBI-359472; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000305|PubMed:34887565, CC ECO:0000305|PubMed:36271492}. Chromosome CC {ECO:0000250|UniProtKB:P70700}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9H9Y6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H9Y6-2; Sequence=VSP_017823; CC Name=3; CC IsoId=Q9H9Y6-3; Sequence=VSP_056750; CC Name=4; CC IsoId=Q9H9Y6-4; Sequence=VSP_056749; CC Name=5; CC IsoId=Q9H9Y6-5; Sequence=VSP_056751; CC -!- DOMAIN: The active site comprises the fork loops, the loops and the CC rudder that stabilize the transcription bubble and assist polymerase CC translocation. {ECO:0000303|PubMed:34671025}. CC -!- DISEASE: Treacher Collins syndrome 4 (TCS4) [MIM:618939]: A form of CC Treacher Collins syndrome, a disorder of craniofacial development. CC Treacher Collins syndrome is characterized by a combination of CC bilateral downward slanting of the palpebral fissures, colobomas of the CC lower eyelids with a paucity of eyelashes medial to the defect, CC hypoplasia of the facial bones, cleft palate, malformation of the CC external ears, atresia of the external auditory canals, and bilateral CC conductive hearing loss. TCS4 inheritance pattern is autosomal CC dominant. {ECO:0000269|PubMed:31649276}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {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; AK022533; BAB14082.1; -; mRNA. DR EMBL; AK022890; BAB14296.1; -; mRNA. DR EMBL; AK128044; BAC87247.1; -; mRNA. DR EMBL; AK301178; BAH13423.1; -; mRNA. DR EMBL; AK302814; BAH13809.1; -; mRNA. DR EMBL; AC012442; AAX81999.1; -; Genomic_DNA. DR EMBL; BC110833; AAI10834.1; -; mRNA. DR CCDS; CCDS2097.1; -. [Q9H9Y6-1] DR CCDS; CCDS46395.1; -. [Q9H9Y6-2] DR CCDS; CCDS62988.1; -. [Q9H9Y6-3] DR CCDS; CCDS62989.1; -. [Q9H9Y6-5] DR CCDS; CCDS62990.1; -. [Q9H9Y6-4] DR RefSeq; NP_001131076.1; NM_001137604.2. [Q9H9Y6-2] DR RefSeq; NP_001269701.1; NM_001282772.1. [Q9H9Y6-3] DR RefSeq; NP_001269703.1; NM_001282774.1. [Q9H9Y6-5] DR RefSeq; NP_001269705.1; NM_001282776.1. [Q9H9Y6-4] DR RefSeq; NP_001269706.1; NM_001282777.1. DR RefSeq; NP_001269708.1; NM_001282779.1. DR RefSeq; NP_061887.2; NM_019014.5. [Q9H9Y6-1] DR PDB; 7OB9; EM; 2.70 A; B=1-1135. DR PDB; 7OBA; EM; 3.10 A; B=1-1135. DR PDB; 7OBB; EM; 3.30 A; B=1-1135. DR PDB; 7VBA; EM; 2.89 A; B=1-1135. DR PDB; 7VBB; EM; 2.81 A; B=1-1135. DR PDB; 7VBC; EM; 3.01 A; B=1-1135. DR PDB; 8A43; EM; 4.09 A; B=1-1135. DR PDBsum; 7OB9; -. DR PDBsum; 7OBA; -. DR PDBsum; 7OBB; -. DR PDBsum; 7VBA; -. DR PDBsum; 7VBB; -. DR PDBsum; 7VBC; -. DR PDBsum; 8A43; -. DR AlphaFoldDB; Q9H9Y6; -. DR EMDB; EMD-12795; -. DR EMDB; EMD-12796; -. DR EMDB; EMD-12797; -. DR EMDB; EMD-15135; -. DR EMDB; EMD-31876; -. DR EMDB; EMD-31877; -. DR EMDB; EMD-31878; -. DR SMR; Q9H9Y6; -. DR BioGRID; 123926; 165. DR ComplexPortal; CPX-2386; DNA-directed RNA polymerase I complex. DR CORUM; Q9H9Y6; -. DR DIP; DIP-27538N; -. DR IntAct; Q9H9Y6; 36. DR MINT; Q9H9Y6; -. DR STRING; 9606.ENSP00000444136; -. DR GlyGen; Q9H9Y6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9H9Y6; -. DR PhosphoSitePlus; Q9H9Y6; -. DR SwissPalm; Q9H9Y6; -. DR BioMuta; POLR1B; -. DR DMDM; 92090637; -. DR EPD; Q9H9Y6; -. DR jPOST; Q9H9Y6; -. DR MassIVE; Q9H9Y6; -. DR MaxQB; Q9H9Y6; -. DR PaxDb; 9606-ENSP00000444136; -. DR PeptideAtlas; Q9H9Y6; -. DR ProteomicsDB; 25159; -. DR ProteomicsDB; 30108; -. DR ProteomicsDB; 81369; -. [Q9H9Y6-1] DR ProteomicsDB; 81370; -. [Q9H9Y6-2] DR Pumba; Q9H9Y6; -. DR Antibodypedia; 18109; 139 antibodies from 24 providers. DR DNASU; 84172; -. DR Ensembl; ENST00000263331.10; ENSP00000263331.5; ENSG00000125630.16. [Q9H9Y6-1] DR Ensembl; ENST00000409894.7; ENSP00000387143.3; ENSG00000125630.16. [Q9H9Y6-5] DR Ensembl; ENST00000417433.6; ENSP00000405358.2; ENSG00000125630.16. [Q9H9Y6-2] DR Ensembl; ENST00000537335.5; ENSP00000437914.1; ENSG00000125630.16. [Q9H9Y6-4] DR Ensembl; ENST00000541869.5; ENSP00000444136.1; ENSG00000125630.16. [Q9H9Y6-3] DR GeneID; 84172; -. DR KEGG; hsa:84172; -. DR MANE-Select; ENST00000263331.10; ENSP00000263331.5; NM_019014.6; NP_061887.2. DR UCSC; uc002thw.4; human. [Q9H9Y6-1] DR AGR; HGNC:20454; -. DR CTD; 84172; -. DR DisGeNET; 84172; -. DR GeneCards; POLR1B; -. DR GeneReviews; POLR1B; -. DR HGNC; HGNC:20454; POLR1B. DR HPA; ENSG00000125630; Low tissue specificity. DR MalaCards; POLR1B; -. DR MIM; 602000; gene. DR MIM; 618939; phenotype. DR neXtProt; NX_Q9H9Y6; -. DR OpenTargets; ENSG00000125630; -. DR Orphanet; 861; Treacher-Collins syndrome. DR PharmGKB; PA130601182; -. DR VEuPathDB; HostDB:ENSG00000125630; -. DR eggNOG; KOG0216; Eukaryota. DR GeneTree; ENSGT00950000183132; -. DR HOGENOM; CLU_000524_5_1_1; -. DR InParanoid; Q9H9Y6; -. DR OMA; FFGVVHY; -. DR OrthoDB; 5476750at2759; -. DR PhylomeDB; Q9H9Y6; -. DR TreeFam; TF103055; -. DR PathwayCommons; Q9H9Y6; -. DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression. DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression. DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation. DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape. DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination. DR SignaLink; Q9H9Y6; -. DR SIGNOR; Q9H9Y6; -. DR BioGRID-ORCS; 84172; 815 hits in 1146 CRISPR screens. DR ChiTaRS; POLR1B; human. DR GeneWiki; POLR1B; -. DR GenomeRNAi; 84172; -. DR Pharos; Q9H9Y6; Tbio. DR PRO; PR:Q9H9Y6; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9H9Y6; Protein. DR Bgee; ENSG00000125630; Expressed in buccal mucosa cell and 207 other cell types or tissues. DR ExpressionAtlas; Q9H9Y6; baseline and differential. DR GO; GO:0005694; C:chromosome; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005736; C:RNA polymerase I 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:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl. DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB. DR GO; GO:0017126; P:nucleologenesis; IEA:Ensembl. DR GO; GO:0009303; P:rRNA transcription; IEA:Ensembl. DR GO; GO:0006360; P:transcription by RNA polymerase I; IEA:GOC. DR CDD; cd00653; RNA_pol_B_RPB2; 1. DR Gene3D; 2.40.50.150; -; 1. DR Gene3D; 3.90.1070.20; -; 1. DR Gene3D; 3.90.1100.10; -; 1. 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 Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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; IPR037034; RNA_pol_Rpb2_2_sf. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR InterPro; IPR009674; Rpa2_dom_4. DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1. DR PANTHER; PTHR20856:SF5; DNA-DIRECTED RNA POLYMERASE I SUBUNIT RPA2; 1. DR Pfam; PF06883; RNA_pol_Rpa2_4; 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; 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 SWISS-2DPAGE; Q9H9Y6; -. DR Genevisible; Q9H9Y6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosome; Disease variant; KW DNA-directed RNA polymerase; Magnesium; Metal-binding; KW Nucleotidyltransferase; Nucleus; Phosphoprotein; Reference proteome; KW Transcription; Transferase; Zinc; Zinc-finger. FT CHAIN 1..1135 FT /note="DNA-directed RNA polymerase I subunit RPA2" FT /id="PRO_0000048072" FT ZN_FING 1070..1101 FT /note="C4-type" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..208 FT /note="Loop B" FT /evidence="ECO:0000269|PubMed:34671025" FT REGION 236..247 FT /note="Loop A" FT /evidence="ECO:0000269|PubMed:34671025" FT REGION 439..453 FT /note="Fork loop 1" FT /evidence="ECO:0000269|PubMed:34671025" FT REGION 474..489 FT /note="Fork loop 2" FT /evidence="ECO:0000269|PubMed:34671025" FT BINDING 180 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT BINDING 367 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34887565, FT ECO:0007744|PDB:7OB9" FT BINDING 755 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_note="ligand shared with POLR1A/RPA1" FT /evidence="ECO:0000250|UniProtKB:P08518, FT ECO:0000250|UniProtKB:P30876" FT BINDING 890 FT /ligand="RNA" FT /ligand_id="ChEBI:CHEBI:33697" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0007744|PDB:7VBA" FT BINDING 1020 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="nontemplate strand" FT /evidence="ECO:0000269|PubMed:34887565, FT ECO:0007744|PDB:7OB9" FT BINDING 1036 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_label="template strand" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT BINDING 1070 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT BINDING 1073 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT BINDING 1098 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT BINDING 1101 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:34671025, FT ECO:0000269|PubMed:34887565, ECO:0007744|PDB:7OB9, FT ECO:0007744|PDB:7VBA" FT SITE 687 FT /note="Active site gating; blocks backward movement of FT nascent RNA" FT /evidence="ECO:0000269|PubMed:34671025" FT MOD_RES 1051 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..211 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056749" FT VAR_SEQ 1 FT /note="M -> MRAKEAAETGLRPLLPACTERLASGVYRETGVRCAGGHM (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056750" FT VAR_SEQ 61..116 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_017823" FT VAR_SEQ 387..582 FT /note="EKLEGWLVSIKIAFDKKAQKTSVSMNTDNLMRIFTMGIDLTKPFEYLFATGN FT LRSKTGLGLLQDSGLCVVADKLNFIRYLSHFRCVHRGADFAKMRTTTVRRLLPESWGFL FT CPVHTPDGEPCGLMNHLTAVCEVVTQFVYTASIPALLCNLGVTPIDGAPHRSYSECYPV FT LLDGVMVGWVDKDLAPGIADSLRHFK -> GSLPLMELPTDHT (in isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056751" FT VARIANT 295 FT /note="S -> L (in dbSNP:rs1545133)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_034476" FT VARIANT 682 FT /note="S -> R (in TCS4; uncertain significance; FT dbSNP:rs1684443250)" FT /evidence="ECO:0000269|PubMed:31649276" FT /id="VAR_084557" FT VARIANT 887 FT /note="H -> R" FT /id="VAR_071195" FT VARIANT 1003 FT /note="R -> C (in TCS4; dbSNP:rs1684813071)" FT /evidence="ECO:0000269|PubMed:31649276" FT /id="VAR_084558" FT VARIANT 1003 FT /note="R -> S (in TCS4)" FT /evidence="ECO:0000269|PubMed:31649276" FT /id="VAR_084559" FT CONFLICT 247 FT /note="L -> R (in Ref. 1; BAB14082)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="E -> G (in Ref. 3; AAI10834)" FT /evidence="ECO:0000305" FT CONFLICT 746 FT /note="I -> T (in Ref. 1; BAB14296)" FT /evidence="ECO:0000305" FT CONFLICT 800 FT /note="D -> G (in Ref. 1; BAC87247)" FT /evidence="ECO:0000305" FT CONFLICT 868 FT /note="C -> R (in Ref. 1; BAB14082)" FT /evidence="ECO:0000305" FT CONFLICT 889 FT /note="Q -> R (in Ref. 1; BAB14082)" FT /evidence="ECO:0000305" FT CONFLICT 1039 FT /note="E -> G (in Ref. 1; BAH13809)" FT /evidence="ECO:0000305" FT STRAND 6..9 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 18..20 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 22..25 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 33..36 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:7OBB" FT HELIX 40..60 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 64..67 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 69..83 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 100..105 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 113..122 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 125..135 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 143..146 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 147..150 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 153..158 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 170..172 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 175..178 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 187..189 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 191..194 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 196..200 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 201..216 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 221..229 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 234..242 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 244..248 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 249..256 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 261..268 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 276..291 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 297..307 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 310..312 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 320..330 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 339..357 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 366..368 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 372..375 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 377..405 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 419..422 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 428..436 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 454..456 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 462..465 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 466..468 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 470..473 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 477..480 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 485..487 FT /evidence="ECO:0007829|PDB:7OBA" FT HELIX 491..493 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 494..496 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 506..510 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 511..514 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 530..536 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 540..544 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 553..560 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 568..570 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 571..584 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 594..598 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 602..604 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 609..613 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 619..625 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 626..629 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 630..635 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 636..639 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 646..648 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 653..655 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 658..662 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 663..666 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 671..673 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 677..679 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 682..691 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 693..695 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 712..716 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 721..723 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 726..729 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 732..734 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 739..741 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 743..745 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 749..751 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 757..760 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 761..765 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 766..769 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 771..780 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 781..784 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 788..790 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 792..794 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 801..803 FT /evidence="ECO:0007829|PDB:7OBA" FT TURN 804..806 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 811..813 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 823..830 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 831..833 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 836..840 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 847..855 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 858..860 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 866..873 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 882..884 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 886..888 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 890..897 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 899..901 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 905..908 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 912..915 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 917..919 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 921..923 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 927..941 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 954..956 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 958..968 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 975..977 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 982..984 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 992..994 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 997..1003 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 1006..1008 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1011..1015 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1020..1022 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1029..1032 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1034..1037 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 1039..1046 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1047..1049 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 1051..1059 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1065..1070 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1071..1074 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1075..1081 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1088..1091 FT /evidence="ECO:0007829|PDB:7OBA" FT STRAND 1096..1098 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1099..1101 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1104..1112 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 1114..1124 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 1125..1127 FT /evidence="ECO:0007829|PDB:7OB9" FT STRAND 1128..1135 FT /evidence="ECO:0007829|PDB:7OB9" SQ SEQUENCE 1135 AA; 128229 MW; 1F019E07F866C22E CRC64; MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA IPPFEFAFKD ERISFTILDA VISPPTVPKG TICKEANVYP AECRGRRSTY RGKLTADINW AVNGISKGII KQFLGYVPIM VKSKLCNLRN LPPQALIEHH EEAEEMGGYF IINGIEKVIR MLIMPRRNFP IAMIRPKWKT RGPGYTQYGV SMHCVREEHS AVNMNLHYLE NGTVMLNFIY RKELFFLPLG FALKALVSFS DYQIFQELIK GKEDDSFLRN SVSQMLRIVM EEGCSTQKQV LNYLGECFRV KLNVPDWYPN EQAAEFLFNQ CICIHLKSNT EKFYMLCLMT RKLFALAKGE CMEDNPDSLV NQEVLTPGQL FLMFLKEKLE GWLVSIKIAF DKKAQKTSVS MNTDNLMRIF TMGIDLTKPF EYLFATGNLR SKTGLGLLQD SGLCVVADKL NFIRYLSHFR CVHRGADFAK MRTTTVRRLL PESWGFLCPV HTPDGEPCGL MNHLTAVCEV VTQFVYTASI PALLCNLGVT PIDGAPHRSY SECYPVLLDG VMVGWVDKDL APGIADSLRH FKVLREKRIP PWMEVVLIPM TGKPSLYPGL FLFTTPCRLV RPVQNLALGK EELIGTMEQI FMNVAIFEDE VFAGVTTHQE LFPHSLLSVI ANFIPFSDHN QSPRNMYQCQ MGKQTMGFPL LTYQDRSDNK LYRLQTPQSP LVRPSMYDYY DMDNYPIGTN AIVAVISYTG YDMEDAMIVN KASWERGFAH GSVYKSEFID LSEKIKQGDS SLVFGIKPGD PRVLQKLDDD GLPFIGAKLQ YGDPYYSYLN LNTGESFVMY YKSKENCVVD NIKVCSNDTG SGKFKCVCIT MRVPRNPTIG DKFASRHGQK GILSRLWPAE DMPFTESGMV PDILFNPHGF PSRMTIGMLI ESMAGKSAAL HGLCHDATPF IFSEENSALE YFGEMLKAAG YNFYGTERLY SGISGLELEA DIFIGVVYYQ RLRHMVSDKF QVRTTGARDR VTNQPIGGRN VQGGIRFGEM ERDALLAHGT SFLLHDRLFN CSDRSVAHVC VKCGSLLSPL LEKPPPSWSA MRNRKYNCTL CSRSDTIDTV SVPYVFRYFV AELAAMNIKV KLDVV //