RPB1_CAEEL
ID RPB1_CAEEL Reviewed; 1856 AA.
AC P16356; Q20090;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
DE Short=RNA polymerase II subunit B1;
DE EC=2.7.7.6;
DE AltName: Full=DNA-directed RNA polymerase III largest subunit;
GN Name=ama-1 {ECO:0000312|WormBase:F36A4.7};
GN Synonyms=rpb-1 {ECO:0000312|WormBase:F36A4.7};
GN ORFNames=F36A4.7 {ECO:0000312|WormBase:F36A4.7};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RX PubMed=2586513; DOI=10.1128/mcb.9.10.4119-4130.1989;
RA Bird D.M., Riddle D.L.;
RT "Molecular cloning and sequencing of ama-1, the gene encoding the largest
RT subunit of Caenorhabditis elegans RNA polymerase II.";
RL Mol. Cell. Biol. 9:4119-4130(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP PHOSPHORYLATION.
RX PubMed=11960010; DOI=10.1073/pnas.082618399;
RA Wallenfang M.R., Seydoux G.;
RT "cdk-7 is required for mRNA transcription and cell cycle progression in
RT Caenorhabditis elegans embryos.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5527-5532(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, PHOSPHORYLATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=14726532; DOI=10.1074/jbc.m310731200;
RA Walker A.K., Shi Y., Blackwell T.K.;
RT "An extensive requirement for transcription factor IID-specific TAF-1 in
RT Caenorhabditis elegans embryonic transcription.";
RL J. Biol. Chem. 279:15339-15347(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=17291483; DOI=10.1016/j.ydbio.2006.12.039;
RA Walker A.K., Boag P.R., Blackwell T.K.;
RT "Transcription reactivation steps stimulated by oocyte maturation in C.
RT elegans.";
RL Dev. Biol. 304:382-393(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=23903194; DOI=10.1242/dev.095778;
RA Bowman E.A., Bowman C.R., Ahn J.H., Kelly W.G.;
RT "Phosphorylation of RNA polymerase II is independent of P-TEFb in the C.
RT elegans germline.";
RL Development 140:3703-3713(2013).
RN [7]
RP DEPHOSPHORYLATION BY SSUP-72.
RX PubMed=26588990; DOI=10.1101/gad.266650.115;
RA Chen F., Zhou Y., Qi Y.B., Khivansara V., Li H., Chun S.Y., Kim J.K.,
RA Fu X.D., Jin Y.;
RT "Context-dependent modulation of Pol II CTD phosphatase SSUP-72 regulates
RT alternative polyadenylation in neuronal development.";
RL Genes Dev. 29:2377-2390(2015).
RN [8]
RP FUNCTION, INTERACTION WITH SIG-7, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=27541139; DOI=10.1371/journal.pgen.1006227;
RA Ahn J.H., Rechsteiner A., Strome S., Kelly W.G.;
RT "A conserved nuclear cyclophilin is required for both RNA polymerase II
RT elongation and co-transcriptional splicing in Caenorhabditis elegans.";
RL PLoS Genet. 12:E1006227-E1006227(2016).
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 component of RNA polymerase II which synthesizes
CC mRNA precursors and many functional non-coding RNAs. Forms the
CC polymerase active center together with the second largest subunit. Pol
CC II is the central component of the basal RNA polymerase II
CC transcription machinery. It is composed of mobile elements that move
CC relative to each other. RPB1 is part of the core element with the
CC central large cleft, the clamp element that moves to open and close the
CC cleft and the jaws that are thought to grab the incoming DNA template.
CC At the start of transcription, a single-stranded DNA template strand of
CC the promoter is positioned within the central active site cleft of Pol
CC II. A bridging helix emanates from RPB1 and crosses the cleft near the
CC catalytic site and is thought to promote translocation of Pol II by
CC acting as a ratchet that moves the RNA-DNA hybrid through the active
CC site by switching from straight to bent conformations at each step of
CC nucleotide addition. During transcription elongation, Pol II moves on
CC the template as the transcript elongates. Elongation is influenced by
CC the phosphorylation status of the C-terminal domain (CTD) of Pol II
CC largest subunit (RPB1), which serves as a platform for assembly of
CC factors that regulate transcription initiation, elongation, termination
CC and mRNA processing (By similarity). Involved in the transcription of
CC several genes including those involved in embryogenesis
CC (PubMed:14726532, PubMed:27541139). {ECO:0000250|UniProtKB:P24928,
CC ECO:0000269|PubMed:14726532, ECO:0000269|PubMed:27541139}.
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 II (Pol II) complex consisting
CC of 12 subunits (By similarity). Interacts with sig-7 (PubMed:27541139).
CC {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:27541139}.
CC -!- INTERACTION:
CC P16356; Q9N337: mdt-6; NbExp=2; IntAct=EBI-1533906, EBI-1533827;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14726532,
CC ECO:0000269|PubMed:17291483, ECO:0000269|PubMed:23903194}. Chromosome
CC {ECO:0000269|PubMed:27541139}. Note=Localizes to punctate nucleoplasmic
CC structures in the nuclei of interphase somatic cells when
CC phosphorylated at 'Ser-5' of the C-terminal heptapeptide repeat
CC (PubMed:14726532). A similar localization occurs in early developing
CC oocytes when phosphorylated at 'Ser-2' and 'Ser-5' of the C-terminal
CC heptapeptide repeat (PubMed:17291483). Localizes to the nucleus of
CC embryonic somatic and germline cells when phosphorylated at 'Ser-2' of
CC the C-terminal heptapeptide repeat (PubMed:23903194). Localizes to two
CC discrete foci in the transcriptionally silent germ line nucleus
CC (PubMed:14726532, PubMed:17291483). Co-localizes with transcriptionally
CC active chromatin in all autosomes of mitotic and meiotic nuclei in germ
CC cells (PubMed:27541139). {ECO:0000269|PubMed:14726532,
CC ECO:0000269|PubMed:17291483, ECO:0000269|PubMed:23903194,
CC ECO:0000269|PubMed:27541139}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo. During embryonic development,
CC the form phosphorylated at 'Ser-2' of the C-terminal heptapeptide
CC repeats is present only in transcriptionally active somatic cells.
CC {ECO:0000269|PubMed:14726532}.
CC -!- DOMAIN: The C-terminal domain (CTD) serves as a platform for assembly
CC of factors that regulate transcription initiation, elongation,
CC termination and mRNA processing. {ECO:0000305}.
CC -!- PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can
CC be highly phosphorylated. The phosphorylation activates Pol II (By
CC similarity). Phosphorylation occurs mainly at residues 'Ser-2' and
CC 'Ser-5' of the heptapeptide repeat and starts at the 3- to 4-cell
CC embryonic stage (PubMed:14726532, PubMed:17291483). This
CC phosphorylation also occurs in the early stages of oocyte development
CC and is not detected in oocytes arrested at the meiotic diakinesis stage
CC (PubMed:17291483). In the somatic lineage, phosphorylation at 'Ser-2'
CC is mediated by cdk-12 downstream of cdk-9 whereas in the germline
CC lineage cdk-12 phosphorylates 'Ser-2' independently of cdk-9
CC (PubMed:23903194). Phosphorylation is likely mediated by cdk-7
CC (PubMed:11960010). May be dephosphorylated by fcp-1 in diakinetic
CC oocytes and in 1-cell and 2-cell embryos (PubMed:17291483).
CC Dephosphorylated at 'Ser-5' of the heptapeptide repeats by ssup-72
CC (PubMed:26588990). The phosphorylation state is believed to result from
CC the balanced action of site-specific CTD kinases and phosphatase, and a
CC 'CTD code' that specifies the position of Pol II within the
CC transcription cycle has been proposed (By similarity).
CC {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:14726532,
CC ECO:0000269|PubMed:17291483, ECO:0000269|PubMed:23903194,
CC ECO:0000269|PubMed:26588990, ECO:0000303|PubMed:11960010}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in embryonic
CC arrest at the 100-cell stage and prevents the embryonic transcription
CC of several genes (PubMed:14726532). Surviving embryos exhibit
CC gastrulation defects with decreased expression of genes involved in
CC gastrulation (PubMed:27541139). {ECO:0000269|PubMed:14726532,
CC ECO:0000269|PubMed:27541139}.
CC -!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the RNA
CC polymerase II transcribing complex probably involves a two-step
CC mechanism. The initial binding seems to occur at the entry (E) site and
CC involves a magnesium ion temporarily coordinated by three conserved
CC aspartate residues of the two largest RNA Pol II subunits. The
CC ribonucleoside triphosphate is transferred by a rotation to the
CC nucleotide addition (A) site for pairing with the template DNA. The
CC catalytic A site involves three conserved aspartate residues of the RNA
CC Pol II largest subunit which permanently coordinate a second magnesium
CC ion.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; M29235; AAA28126.1; -; mRNA.
DR EMBL; BX284604; CCD69532.1; -; Genomic_DNA.
DR PIR; A34092; A34092.
DR PIR; T29959; T29959.
DR RefSeq; NP_500523.4; NM_068122.6.
DR AlphaFoldDB; P16356; -.
DR SMR; P16356; -.
DR BioGRID; 42323; 37.
DR IntAct; P16356; 5.
DR STRING; 6239.F36A4.7; -.
DR iPTMnet; P16356; -.
DR EPD; P16356; -.
DR PaxDb; P16356; -.
DR PeptideAtlas; P16356; -.
DR EnsemblMetazoa; F36A4.7.1; F36A4.7.1; WBGene00000123.
DR GeneID; 177190; -.
DR KEGG; cel:CELE_F36A4.7; -.
DR UCSC; F36A4.7; c. elegans.
DR CTD; 247749; -.
DR WormBase; F36A4.7; CE46402; WBGene00000123; ama-1.
DR eggNOG; KOG0260; Eukaryota.
DR GeneTree; ENSGT00930000151033; -.
DR HOGENOM; CLU_000487_0_2_1; -.
DR InParanoid; P16356; -.
DR OMA; SLLHICM; -.
DR OrthoDB; 591636at2759; -.
DR PhylomeDB; P16356; -.
DR Reactome; R-CEL-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-CEL-113418; Formation of the Early Elongation Complex.
DR Reactome; R-CEL-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-CEL-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-CEL-6803529; FGFR2 alternative splicing.
DR Reactome; R-CEL-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-CEL-72086; mRNA Capping.
DR Reactome; R-CEL-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-CEL-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-CEL-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-CEL-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-CEL-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-CEL-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-CEL-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-CEL-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-CEL-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P16356; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00000123; Expressed in embryo and 7 other tissues.
DR GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:WormBase.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; ISS:WormBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007369; P:gastrulation; IMP:WormBase.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:2000543; P:positive regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IMP:WormBase.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 3.30.1360.140; -; 1.
DR Gene3D; 4.10.860.120; -; 2.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR000684; RNA_pol_II_repeat_euk.
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; IPR007075; RNA_pol_Rpb1_6.
DR InterPro; IPR007073; RNA_pol_Rpb1_7.
DR InterPro; IPR038593; RNA_pol_Rpb1_7_sf.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
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 Pfam; PF04992; RNA_pol_Rpb1_6; 1.
DR Pfam; PF04990; RNA_pol_Rpb1_7; 1.
DR Pfam; PF05001; RNA_pol_Rpb1_R; 22.
DR SMART; SM00663; RPOLA_N; 1.
DR PROSITE; PS00115; RNA_POL_II_REPEAT; 26.
PE 1: Evidence at protein level;
KW Chromosome; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transferase; Zinc.
FT CHAIN 1..1856
FT /note="DNA-directed RNA polymerase II subunit RPB1"
FT /id="PRO_0000073935"
FT REPEAT 1593..1599
FT /note="1"
FT REPEAT 1600..1606
FT /note="2"
FT REPEAT 1616..1622
FT /note="3"
FT REPEAT 1623..1629
FT /note="4"
FT REPEAT 1630..1636
FT /note="5"
FT REPEAT 1637..1643
FT /note="6"
FT REPEAT 1644..1650
FT /note="7"
FT REPEAT 1651..1657
FT /note="8"
FT REPEAT 1658..1664
FT /note="9"
FT REPEAT 1665..1671
FT /note="10"
FT REPEAT 1672..1678
FT /note="11"
FT REPEAT 1679..1685
FT /note="12"
FT REPEAT 1686..1692
FT /note="13"
FT REPEAT 1693..1699
FT /note="14"
FT REPEAT 1700..1706
FT /note="15"
FT REPEAT 1707..1713
FT /note="16"
FT REPEAT 1720..1726
FT /note="17"
FT REPEAT 1727..1733
FT /note="18"
FT REPEAT 1734..1740
FT /note="19"
FT REPEAT 1741..1747
FT /note="20"
FT REPEAT 1748..1754
FT /note="21"
FT REPEAT 1755..1761
FT /note="22"
FT REPEAT 1769..1775
FT /note="23"
FT REPEAT 1782..1788
FT /note="24"
FT REPEAT 1789..1795
FT /note="25"
FT REPEAT 1796..1802
FT /note="26"
FT REPEAT 1803..1809
FT /note="27"
FT REPEAT 1810..1816
FT /note="28; approximate"
FT REGION 256..268
FT /note="Lid loop"
FT REGION 314..331
FT /note="Rudder loop"
FT REGION 827..839
FT /note="Bridging helix"
FT REGION 1523..1856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1593..1816
FT /note="C-terminal domain (CTD); 28 X 7 AA approximate
FT tandem repeats of Y-[ST]-P-[ST]-S-P-[AGKNQRST]"
FT COMPBIAS 1575..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1856
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 76
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 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
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 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 489
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 491
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="ligand shared with RPB2"
FT /evidence="ECO:0000250"
FT BINDING 493
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 215
FT /note="V -> D (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..415
FT /note="Missing (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="R -> RVSVAQNAIKL (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 963
FT /note="I -> D (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 978
FT /note="Q -> L (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 994..995
FT /note="KP -> NA (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 1160..1162
FT /note="Missing (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
FT CONFLICT 1406..1407
FT /note="IT -> YS (in Ref. 1; AAA28126)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1856 AA; 204525 MW; 379BB183B957D2D5 CRC64;
MALVGVDFQA PLRIVSRVQF GILGPEEIKR MSVAHVEFPE VYENGKPKLG GLMDPRQGVI
DRRGRCMTCA GNLTDCPGHF GHLELAKPVF HIGFLTKTLK ILRCVCFYCG RLLIDKSAPR
VLEILKKTGT NSKKRLTMIY DLCKAKSVCE GAAEKEEGMP DDPDDPMNDG KKVAGGCGRY
QPSYRRVGID INAEWKKNVN EDTQERKIML TAERVLEVFQ QITDEDILVI GMDPQFARPE
WMICTVLPVP PLAVRPAVVT FGSAKNQDDL THKLSDIIKT NQQLQRNEAN GAAAHVLTDD
VRLLQFHVAT LVDNCIPGLP TATQKGGRPL KSIKQRLKGK EGRIRGNLMG KRVDFSARTV
ITADPNLPID TVGVPRTIAQ NLTFPEIVTP FNVDKLQELV NRGDTQYPGA KYIIRENGAR
VDLRYHPRAA DLHLQPGYRV ERHMKDGDII VFNRQPTLHK MSMMGHRVKI LPWSTFRMNL
SVTSPYNADF DGDEMNLHLP QSLETRAEIE EIAMVPRQLI TPQANKPVMG IVQDTLCAVR
MMTKRDVFID WPFMMDLLMY LPTWDGKVPQ PAILKPKPLW TGKQVFSLII PGNVNVLRTH
STHPDSEDSG PYKWISPGDT KVIIEHGELL SGIVCSKTVG KSAGNLLHVV TLELGYEIAA
NFYSHIQTVI NAWLIREGHT IGIGDTIADQ ATYLDIQNTI RKAKQDVVDV IEKAHNDDLE
PTPGNTLRQT FENKVNQILN DARDRTGSSA QKSLSEFNNF KSMVVSGSKG SKINISQVIA
CVGQQNVEGK RIPFGFRHRT LPHFIKDDYG PESKGFVENS YLAGLTPSEF FFHAMGGREG
LIDTAVKTAE TGYIQRRLIK AMESVMVNYD GTVRNSLAQM VQLRYGEDGL DGMWVENQNM
PTMKPNNAVF ERDFRMDLTD NKFLRKNYSE DVVREIQESE DGISLVESEW SQLEEDRRLL
RKIFPRGDAK IVLPCNLQRL IWNAQKIFKV DLRKPVNLSP LHVISGVREL SKKLIIVSGN
DEISKQAQYN ATLLMNILLR STLCTKNMCT KSKLNSEAFD WLLGEIESRF QQAIAQPGEM
VGALAAQSLG EPATQMTLNT FHYAGVSAKN VTLGVPRLKE IINVSKTLKT PSLTVFLTGA
AAKDPEKAKD VLCKLEHTTL KKVTCNTAIY YDPDPKNTVI AEDEEWVSIF YEMPDHDLSR
TSPWLLRIEL DRKRMVDKKL TMEMIADRIH GGFGNDVHTI YTDDNAEKLV FRLRIAGEDK
GEAQEEQVDK MEDDVFLRCI EANMLSDLTL QGIPAISKVY MNQPNTDDKK RIIITPEGGF
KSVADWILET DGTALLRVLS ERQIDPVRTT SNDICEIFEV LGIEAVRKAI EREMDNVISF
DGSYVNYRHL ALLCDVMTAK GHLMAITRHG INRQEVGALM RCSFEETVDI LMEAAVHAEE
DPVKGVSENI MLGQLARCGT GCFDLVLDVE KCKYGMEIPQ NVVMGGGFYG SFAGSPSNRE
FSPAHSPWNS GVTPTYAGAA WSPTTGGMSP GAGFSPAGNT DGGASPFNEG GWSPASPGDP
LGALSPRTPS YGGMSPGVYS PSSPQFSMTS PHYSPTSPSY SPTSPAAGQS PVSPSYSPTS
PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP SSPSYSPSSP SYSPSSPRYS
PTSPTYSPTS PTYSPTSPTY SPTSPTYSPT SPSYESGGGY SPSSPKYSPS SPTYSPTSPS
YSPTSPQYSP TSPQYSPSSP TYTPSSPTYN PTSPRGFSSP QYSPTSPTYS PTSPSYTPSS
PQYSPTSPTY TPSPSEQPGT SAQYSPTSPT YSPSSPTYSP ASPSYSPSSP TYDPNS
