RPC1_HUMAN
ID RPC1_HUMAN Reviewed; 1390 AA.
AC O14802; Q8IW34; Q8TCW5;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC1;
DE Short=RNA polymerase III subunit C1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
DE AltName: Full=DNA-directed RNA polymerase III subunit A;
DE AltName: Full=RNA polymerase III 155 kDa subunit;
DE Short=RPC155;
DE AltName: Full=RNA polymerase III subunit C160;
GN Name=POLR3A;
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].
RX PubMed=9331371; DOI=10.1101/gr.7.10.1006;
RA Sepehri S., Hernandez N.;
RT "The largest subunit of human RNA polymerase III is closely related to the
RT largest subunit of yeast and trypanosome RNA polymerase III.";
RL Genome Res. 7:1006-1019(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-374.
RX PubMed=12384934; DOI=10.1002/art.10521;
RA Kuwana M., Kimura K., Kawakami Y.;
RT "Identification of an immunodominant epitope on RNA polymerase III
RT recognized by systemic sclerosis sera: application to enzyme-linked
RT immunosorbent assay.";
RL Arthritis Rheum. 46:2742-2747(2002).
RN [6]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP 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 [7]
RP FUNCTION.
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 [8]
RP FUNCTION.
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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-445, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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 [11]
RP VARIANTS HLD7 ASN-372; LEU-558; TYR-636; GLU-672; TYR-724; ILE-775; VAL-852
RP AND THR-1247 INS, INVOLVEMENT IN HLD7, AND TISSUE SPECIFICITY.
RX PubMed=21855841; DOI=10.1016/j.ajhg.2011.07.014;
RA Bernard G., Chouery E., Putorti M.L., Tetreault M., Takanohashi A.,
RA Carosso G., Clement I., Boespflug-Tanguy O., Rodriguez D., Delague V.,
RA Abou Ghoch J., Jalkh N., Dorboz I., Fribourg S., Teichmann M.,
RA Megarbane A., Schiffmann R., Vanderver A., Brais B.;
RT "Mutations of POLR3A encoding a catalytic subunit of RNA polymerase Pol III
RT cause a recessive hypomyelinating leukodystrophy.";
RL Am. J. Hum. Genet. 89:415-423(2011).
RN [12]
RP VARIANTS HLD7 ASN-897 AND CYS-1005.
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 [13]
RP VARIANTS HLD7 LEU-91; GLY-387; ARG-602; VAL-852; CYS-1005 AND LYS-1261.
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 [14]
RP VARIANTS HLD7 CYS-310 AND THR-804.
RX PubMed=23694757; DOI=10.1016/j.braindev.2013.04.011;
RA Shimojima K., Shimada S., Tamasaki A., Akaboshi S., Komoike Y., Saito A.,
RA Furukawa T., Yamamoto T.;
RT "Novel compound heterozygous mutations of POLR3A revealed by whole-exome
RT sequencing in a patient with hypomyelination.";
RL Brain Dev. 36:315-321(2014).
RN [15]
RP VARIANT WDRTS 873-ARG--THR-1390 DEL, AND INVOLVEMENT IN WDRTS.
RX PubMed=27612211; DOI=10.1002/ajmg.a.37960;
RA Jay A.M., Conway R.L., Thiffault I., Saunders C., Farrow E., Adams J.,
RA Toriello H.V.;
RT "Neonatal progeriod syndrome associated with biallelic truncating variants
RT in POLR3A.";
RL Am. J. Med. Genet. A 170:3343-3346(2016).
RN [16]
RP VARIANTS WDRTS 254-ARG--THR-1390 DEL AND 669-ARG--THR-1390 DEL, AND
RP INVOLVEMENT IN WDRTS.
RX PubMed=30414627; DOI=10.1016/j.ajhg.2018.10.010;
RA Wambach J.A., Wegner D.J., Patni N., Kircher M., Willing M.C.,
RA Baldridge D., Xing C., Agarwal A.K., Vergano S.A.S., Patel C., Grange D.K.,
RA Kenney A., Najaf T., Nickerson D.A., Bamshad M.J., Cole F.S., Garg A.;
RT "Bi-allelic POLR3A loss-of-function variants cause autosomal-recessive
RT Wiedemann-Rautenstrauch syndrome.";
RL Am. J. Hum. Genet. 103:968-975(2018).
RN [17]
RP VARIANT WDRTS 254-ARG--THR-1390 DEL, AND INVOLVEMENT IN WDRTS.
RX PubMed=30450527; DOI=10.1007/s00439-018-1957-1;
RA Lessel D., Ozel A.B., Campbell S.E., Saadi A., Arlt M.F., McSweeney K.M.,
RA Plaiasu V., Szakszon K., Szollos A., Rusu C., Rojas A.J., Lopez-Valdez J.,
RA Thiele H., Nuernberg P., Nickerson D.A., Bamshad M.J., Li J.Z., Kubisch C.,
RA Glover T.W., Gordon L.B.;
RT "Analyses of LMNA-negative juvenile progeroid cases confirms biallelic
RT POLR3A mutations in Wiedemann-Rautenstrauch-like syndrome and expands the
RT phenotypic spectrum of PYCR1 mutations.";
RL Hum. Genet. 137:921-939(2018).
RN [18]
RP VARIANTS WDRTS 825-SER--THR-1390 DEL; ARG-903; GLN-1069; ARG-1131; ASN-1292
RP AND ARG-1335, AND INVOLVEMENT IN WDRTS.
RX PubMed=30323018; DOI=10.1136/jmedgenet-2018-105528;
RA Paolacci S., Li Y., Agolini E., Bellacchio E., Arboleda-Bustos C.E.,
RA Carrero D., Bertola D., Al-Gazali L., Alders M., Altmueller J.,
RA Arboleda G., Beleggia F., Bruselles A., Ciolfi A., Gillessen-Kaesbach G.,
RA Krieg T., Mohammed S., Mueller C., Novelli A., Ortega J., Sandoval A.,
RA Velasco G., Yigit G., Arboleda H., Lopez-Otin C., Wollnik B., Tartaglia M.,
RA Hennekam R.C.;
RT "Specific combinations of biallelic POLR3A variants cause Wiedemann-
RT Rautenstrauch syndrome.";
RL J. Med. Genet. 55:837-846(2018).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Largest and catalytic core component of RNA polymerase III which
CC synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase
CC active center together with the second largest subunit. A single-
CC stranded DNA template strand of the promoter is positioned within the
CC central active site cleft of Pol III. A bridging helix emanates from
CC RPC1 and crosses the cleft near the catalytic site and is thought to
CC promote translocation of Pol III by acting as a ratchet that moves the
CC RNA-DNA hybrid through the active site by switching from straight to
CC bent conformations at each step of nucleotide addition (By similarity).
CC Plays a key role in sensing and limiting infection by intracellular
CC bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor
CC involved in innate immune response. Can sense non-self dsDNA that
CC serves as template for transcription into dsRNA. The non-self RNA
CC polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs
CC (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I
CC pathway. {ECO:0000250, ECO:0000269|PubMed:19609254,
CC ECO:0000269|PubMed:19631370}.
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;
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, in the cortex and the white
CC matter (at protein level). {ECO:0000269|PubMed:21855841}.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 7, with or without
CC oligodontia and/or hypogonadotropic hypogonadism (HLD7) [MIM:607694]:
CC An autosomal recessive neurodegenerative disorder characterized by
CC childhood onset of progressive motor decline manifest as spasticity,
CC ataxia, tremor, and cerebellar signs, as well as mild cognitive
CC regression. Other features may include hypodontia or oligodontia and
CC hypogonadotropic hypogonadism. There is considerable inter- and
CC intrafamilial variability. {ECO:0000269|PubMed:21855841,
CC ECO:0000269|PubMed:22036171, ECO:0000269|PubMed:23355746,
CC ECO:0000269|PubMed:23694757}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Wiedemann-Rautenstrauch syndrome (WDRTS) [MIM:264090]: An
CC autosomal recessive, neonatal progeroid disorder characterized by
CC intrauterine growth retardation, failure to thrive, short stature,
CC hypotonia, variable mental impairment, and a progeroid appearance.
CC Clinical features include apparent macrocephaly, sparse hair, prominent
CC scalp veins, entropion, greatly widened anterior fontanelles, malar
CC hypoplasia, and generalized lipoatrophy. Death usually occurs in early
CC childhood but survival to third decade has been reported.
CC {ECO:0000269|PubMed:27612211, ECO:0000269|PubMed:30323018,
CC ECO:0000269|PubMed:30414627, ECO:0000269|PubMed:30450527}. 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}.
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DR EMBL; AF021351; AAB86536.1; -; mRNA.
DR EMBL; AL512628; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54617.1; -; Genomic_DNA.
DR EMBL; BC041089; AAH41089.1; -; mRNA.
DR EMBL; AY091459; AAM12029.1; -; mRNA.
DR CCDS; CCDS7354.1; -.
DR RefSeq; NP_008986.2; NM_007055.3.
DR PDB; 7A6H; EM; 3.30 A; A=1-1390.
DR PDB; 7AE1; EM; 2.80 A; A=1-1390.
DR PDB; 7AE3; EM; 3.10 A; A=1-1390.
DR PDB; 7AEA; EM; 3.40 A; A=1-1390.
DR PDB; 7AST; EM; 4.00 A; N=1-1390.
DR PDB; 7D58; EM; 2.90 A; A=1-1390.
DR PDB; 7D59; EM; 3.10 A; A=1-1390.
DR PDB; 7DN3; EM; 3.50 A; A=1-1390.
DR PDB; 7DU2; EM; 3.35 A; A=1-1390.
DR PDB; 7FJI; EM; 3.60 A; A=1-1390.
DR PDB; 7FJJ; EM; 3.60 A; A=1-1390.
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 AlphaFoldDB; O14802; -.
DR SMR; O14802; -.
DR BioGRID; 116301; 149.
DR IntAct; O14802; 49.
DR MINT; O14802; -.
DR STRING; 9606.ENSP00000361446; -.
DR ChEMBL; CHEMBL4665582; -.
DR GlyGen; O14802; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14802; -.
DR MetOSite; O14802; -.
DR PhosphoSitePlus; O14802; -.
DR SwissPalm; O14802; -.
DR BioMuta; POLR3A; -.
DR EPD; O14802; -.
DR jPOST; O14802; -.
DR MassIVE; O14802; -.
DR MaxQB; O14802; -.
DR PaxDb; O14802; -.
DR PeptideAtlas; O14802; -.
DR PRIDE; O14802; -.
DR ProteomicsDB; 48248; -.
DR Antibodypedia; 29822; 165 antibodies from 29 providers.
DR DNASU; 11128; -.
DR Ensembl; ENST00000372371.8; ENSP00000361446.3; ENSG00000148606.14.
DR GeneID; 11128; -.
DR KEGG; hsa:11128; -.
DR MANE-Select; ENST00000372371.8; ENSP00000361446.3; NM_007055.4; NP_008986.2.
DR UCSC; uc001jzn.4; human.
DR CTD; 11128; -.
DR DisGeNET; 11128; -.
DR GeneCards; POLR3A; -.
DR GeneReviews; POLR3A; -.
DR HGNC; HGNC:30074; POLR3A.
DR HPA; ENSG00000148606; Low tissue specificity.
DR MalaCards; POLR3A; -.
DR MIM; 264090; phenotype.
DR MIM; 607694; phenotype.
DR MIM; 614258; gene.
DR neXtProt; NX_O14802; -.
DR OpenTargets; ENSG00000148606; -.
DR Orphanet; 137639; Hypomyelinating leukodystrophy-ataxia-hypodontia-hypomyelination syndrome.
DR Orphanet; 447893; Hypomyelination-cerebellar atrophy-hypoplasia of the corpus callosum syndrome.
DR Orphanet; 88637; Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome.
DR Orphanet; 77295; Odontoleukodystrophy.
DR Orphanet; 447896; Tremor-ataxia-central hypomyelination syndrome.
DR Orphanet; 3455; Wiedemann-Rautenstrauch syndrome.
DR PharmGKB; PA134900426; -.
DR VEuPathDB; HostDB:ENSG00000148606; -.
DR eggNOG; KOG0261; Eukaryota.
DR GeneTree; ENSGT00930000151028; -.
DR HOGENOM; CLU_000487_3_0_1; -.
DR InParanoid; O14802; -.
DR OMA; AVCPPYN; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; O14802; -.
DR TreeFam; TF103054; -.
DR PathwayCommons; O14802; -.
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; O14802; -.
DR SIGNOR; O14802; -.
DR BioGRID-ORCS; 11128; 817 hits in 1094 CRISPR screens.
DR ChiTaRS; POLR3A; human.
DR GenomeRNAi; 11128; -.
DR Pharos; O14802; Tbio.
DR PRO; PR:O14802; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O14802; protein.
DR Bgee; ENSG00000148606; Expressed in buccal mucosa cell and 183 other tissues.
DR ExpressionAtlas; O14802; baseline and differential.
DR Genevisible; O14802; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd02736; RNAP_III_Rpc1_C; 1.
DR CDD; cd02583; RNAP_III_RPC1_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR035698; RNAP_III_Rpc1_C.
DR InterPro; IPR035697; RNAP_III_RPC1_N.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Antiviral defense; Disease variant;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Leukodystrophy;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1390
FT /note="DNA-directed RNA polymerase III subunit RPC1"
FT /id="PRO_0000073947"
FT REGION 844..856
FT /note="Bridging helix"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT MOD_RES 445
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 91
FT /note="P -> L (in HLD7; dbSNP:rs1375717376)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072338"
FT VARIANT 254..1390
FT /note="Missing (in WDRTS)"
FT /evidence="ECO:0000269|PubMed:30414627,
FT ECO:0000269|PubMed:30450527"
FT /id="VAR_081999"
FT VARIANT 310
FT /note="W -> C (in HLD7; dbSNP:rs1217230904)"
FT /evidence="ECO:0000269|PubMed:23694757"
FT /id="VAR_072339"
FT VARIANT 372
FT /note="D -> N (in HLD7; dbSNP:rs267608673)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066516"
FT VARIANT 387
FT /note="A -> G (in HLD7; dbSNP:rs1307896663)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072340"
FT VARIANT 558
FT /note="F -> L (in HLD7; dbSNP:rs267608668)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066517"
FT VARIANT 582
FT /note="R -> L (in dbSNP:rs34588967)"
FT /id="VAR_051873"
FT VARIANT 602
FT /note="S -> R (in HLD7; dbSNP:rs762708292)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072341"
FT VARIANT 636
FT /note="S -> Y (in HLD7; dbSNP:rs267608676)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066518"
FT VARIANT 669..1390
FT /note="Missing (in WDRTS)"
FT /evidence="ECO:0000269|PubMed:30414627"
FT /id="VAR_082000"
FT VARIANT 672
FT /note="G -> E (in HLD7; dbSNP:rs267608670)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066519"
FT VARIANT 713
FT /note="K -> N (in dbSNP:rs35354908)"
FT /id="VAR_051874"
FT VARIANT 724
FT /note="C -> Y (in HLD7; dbSNP:rs267608679)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066520"
FT VARIANT 775
FT /note="N -> I (in HLD7; dbSNP:rs267608672)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066521"
FT VARIANT 804
FT /note="I -> T (in HLD7)"
FT /evidence="ECO:0000269|PubMed:23694757"
FT /id="VAR_072342"
FT VARIANT 825..1390
FT /note="Missing (in WDRTS)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082001"
FT VARIANT 852
FT /note="M -> V (in HLD7; dbSNP:rs267608671)"
FT /evidence="ECO:0000269|PubMed:21855841,
FT ECO:0000269|PubMed:23355746"
FT /id="VAR_066522"
FT VARIANT 873..1390
FT /note="Missing (in WDRTS)"
FT /evidence="ECO:0000269|PubMed:27612211"
FT /id="VAR_082002"
FT VARIANT 897
FT /note="I -> N (in HLD7; dbSNP:rs267608681)"
FT /evidence="ECO:0000269|PubMed:22036171"
FT /id="VAR_067004"
FT VARIANT 903
FT /note="G -> R (in WDRTS; unknown pathological significance;
FT dbSNP:rs1399429058)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082003"
FT VARIANT 1005
FT /note="R -> C (in HLD7; dbSNP:rs267608682)"
FT /evidence="ECO:0000269|PubMed:22036171,
FT ECO:0000269|PubMed:23355746"
FT /id="VAR_066523"
FT VARIANT 1069
FT /note="R -> Q (in WDRTS; unknown pathological significance;
FT dbSNP:rs778985686)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082004"
FT VARIANT 1131
FT /note="K -> R (in WDRTS; unknown pathological significance;
FT dbSNP:rs138305578)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082005"
FT VARIANT 1247
FT /note="T -> TT (in HLD7)"
FT /evidence="ECO:0000269|PubMed:21855841"
FT /id="VAR_066524"
FT VARIANT 1261
FT /note="E -> K (in HLD7; dbSNP:rs371703979)"
FT /evidence="ECO:0000269|PubMed:23355746"
FT /id="VAR_072343"
FT VARIANT 1292
FT /note="D -> N (in WDRTS; unknown pathological significance;
FT dbSNP:rs757209071)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082006"
FT VARIANT 1335
FT /note="G -> R (in WDRTS; unknown pathological significance;
FT dbSNP:rs768222183)"
FT /evidence="ECO:0000269|PubMed:30323018"
FT /id="VAR_082007"
FT CONFLICT 15
FT /note="I -> T (in Ref. 1; AAB86536)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="I -> F (in Ref. 1; AAB86536)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="L -> P (in Ref. 5; AAM12029)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="A -> G (in Ref. 1; AAB86536)"
FT /evidence="ECO:0000305"
FT CONFLICT 1275
FT /note="M -> MV (in Ref. 1; AAB86536)"
FT /evidence="ECO:0000305"
FT STRAND 12..21
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 98..107
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 119..128
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:7AE3"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 198..203
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 207..210
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 236..238
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 247..250
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:7D58"
FT TURN 269..272
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 278..299
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 303..321
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:7DU2"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 358..371
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 390..395
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 418..422
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 424..426
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 429..435
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 437..442
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 473..488
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 490..492
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 504..508
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 513..523
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 525..527
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 532..534
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:7AE3"
FT TURN 543..545
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 547..552
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 553..555
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 574..578
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 590..592
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 594..596
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 616..620
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 627..631
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 637..641
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 652..655
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 656..661
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 663..671
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 673..694
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 707..732
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 739..741
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 744..770
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 776..782
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:7DU2"
FT HELIX 789..796
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:7D59"
FT STRAND 812..815
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 829..831
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 838..840
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 844..879
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 893..895
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 897..901
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 902..905
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 909..911
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 913..918
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 921..931
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 935..937
FT /evidence="ECO:0007829|PDB:7D59"
FT HELIX 942..952
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 956..960
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 963..987
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 991..993
FT /evidence="ECO:0007829|PDB:7D59"
FT HELIX 998..1002
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1008..1023
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1033..1047
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1056..1059
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1067..1075
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1085..1091
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1095..1105
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1110..1112
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1114..1121
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1126..1132
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1134..1140
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1146..1152
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1153..1157
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1162..1164
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 1165..1169
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1172..1175
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1181..1183
FT /evidence="ECO:0007829|PDB:7D58"
FT TURN 1186..1188
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1189..1195
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1196..1198
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 1199..1203
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1209..1214
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1223..1230
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1232..1235
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1243..1245
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1247..1249
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1251..1258
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1260..1277
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1284..1295
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1296..1299
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 1305..1311
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1315..1318
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 1319..1321
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1324..1334
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1337..1339
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1343..1349
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1356..1358
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1359..1364
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 1378..1380
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 1382..1384
FT /evidence="ECO:0007829|PDB:7AE1"
SQ SEQUENCE 1390 AA; 155641 MW; 56F30900848E3DB9 CRC64;
MVKEQFRETD VAKKISHICF GMKSPEEMRQ QAHIQVVSKN LYSQDNQHAP LLYGVLDHRM
GTSEKDRPCE TCGKNLADCL GHYGYIDLEL PCFHVGYFRA VIGILQMICK TCCHIMLSQE
EKKQFLDYLK RPGLTYLQKR GLKKKISDKC RKKNICHHCG AFNGTVKKCG LLKIIHEKYK
TNKKVVDPIV SNFLQSFETA IEHNKEVEPL LGRAQENLNP LVVLNLFKRI PAEDVPLLLM
NPEAGKPSDL ILTRLLVPPL CIRPSVVSDL KSGTNEDDLT MKLTEIIFLN DVIKKHRISG
AKTQMIMEDW DFLQLQCALY INSELSGIPL NMAPKKWTRG FVQRLKGKQG RFRGNLSGKR
VDFSGRTVIS PDPNLRIDEV AVPVHVAKIL TFPEKVNKAN INFLRKLVQN GPEVHPGANF
IQQRHTQMKR FLKYGNREKM AQELKYGDIV ERHLIDGDVV LFNRQPSLHK LSIMAHLARV
KPHRTFRFNE CVCTPYNADF DGDEMNLHLP QTEEAKAEAL VLMGTKANLV TPRNGEPLIA
AIQDFLTGAY LLTLKDTFFD RAKACQIIAS ILVGKDEKIK VRLPPPTILK PVTLWTGKQI
FSVILRPSDD NPVRANLRTK GKQYCGKGED LCANDSYVTI QNSELMSGSM DKGTLGSGSK
NNIFYILLRD WGQNEAADAM SRLARLAPVY LSNRGFSIGI GDVTPGQGLL KAKYELLNAG
YKKCDEYIEA LNTGKLQQQP GCTAEETLEA LILKELSVIR DHAGSACLRE LDKSNSPLTM
ALCGSKGSFI NISQMIACVG QQAISGSRVP DGFENRSLPH FEKHSKLPAA KGFVANSFYS
GLTPTEFFFH TMAGREGLVD TAVKTAETGY MQRRLVKSLE DLCSQYDLTV RSSTGDIIQF
IYGGDGLDPA AMEGKDEPLE FKRVLDNIKA VFPCPSEPAL SKNELILTTE SIMKKSEFLC
CQDSFLQEIK KFIKGVSEKI KKTRDKYGIN DNGTTEPRVL YQLDRITPTQ VEKFLETCRD
KYMRAQMEPG SAVGALCAQS IGEPGTQMTL KTFHFAGVAS MNITLGVPRI KEIINASKAI
STPIITAQLD KDDDADYARL VKGRIEKTLL GEISEYIEEV FLPDDCFILV KLSLERIRLL
RLEVNAETVR YSICTSKLRV KPGDVAVHGE AVVCVTPREN SKSSMYYVLQ FLKEDLPKVV
VQGIPEVSRA VIHIDEQSGK EKYKLLVEGD NLRAVMATHG VKGTRTTSNN TYEVEKTLGI
EAARTTIINE IQYTMVNHGM SIDRRHVMLL SDLMTYKGEV LGITRFGLAK MKESVLMLAS
FEKTADHLFD AAYFGQKDSV CGVSECIIMG IPMNIGTGLF KLLHKADRDP NPPKRPLIFD
TNEFHIPLVT
