SEN1_YEAST
ID SEN1_YEAST Reviewed; 2231 AA.
AC Q00416; D6VZ65; E9P9Z4; Q06448;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Helicase SEN1;
DE EC=3.6.4.-;
DE AltName: Full=tRNA-splicing endonuclease positive effector;
GN Name=SEN1; OrderedLocusNames=YLR430W; ORFNames=L9576.1;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-2231, AND MUTAGENESIS OF GLY-1747.
RX PubMed=1569945; DOI=10.1128/mcb.12.5.2154-2164.1992;
RA Demarini D.J., Winey M., Ursic D., Webb F., Culbertson M.R.;
RT "SEN1, a positive effector of tRNA-splicing endonuclease in Saccharomyces
RT cerevisiae.";
RL Mol. Cell. Biol. 12:2154-2164(1992).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=8544822; DOI=10.1007/bf00418026;
RA Ursic D., DeMarini D.J., Culbertson M.R.;
RT "Inactivation of the yeast Sen1 protein affects the localization of
RT nucleolar proteins.";
RL Mol. Gen. Genet. 249:571-584(1995).
RN [5]
RP FUNCTION.
RX PubMed=8943355; DOI=10.1128/mcb.16.12.6993;
RA Steinmetz E.J., Brow D.A.;
RT "Repression of gene expression by an exogenous sequence element acting in
RT concert with a heterogeneous nuclear ribonucleoprotein-like protein, Nrd1,
RT and the putative helicase Sen1.";
RL Mol. Cell. Biol. 16:6993-7003(1996).
RN [6]
RP FUNCTION.
RX PubMed=9365256; DOI=10.1093/nar/25.23.4778;
RA Ursic D., Himmel K.L., Gurley K.A., Webb F., Culbertson M.R.;
RT "The yeast SEN1 gene is required for the processing of diverse RNA
RT classes.";
RL Nucleic Acids Res. 25:4778-4785(1997).
RN [7]
RP FUNCTION.
RX PubMed=9819377; DOI=10.1128/mcb.18.12.6885;
RA Rasmussen T.P., Culbertson M.R.;
RT "The putative nucleic acid helicase Sen1p is required for formation and
RT stability of termini and for maximal rates of synthesis and levels of
RT accumulation of small nucleolar RNAs in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 18:6885-6896(1998).
RN [8]
RP FUNCTION.
RX PubMed=11565036; DOI=10.1038/35095090;
RA Steinmetz E.J., Conrad N.K., Brow D.A., Corden J.L.;
RT "RNA-binding protein Nrd1 directs poly(A)-independent 3'-end formation of
RT RNA polymerase II transcripts.";
RL Nature 413:327-331(2001).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION, AND INTERACTION WITH RAD2; RNT1 AND RPB1.
RX PubMed=15121901; DOI=10.1093/nar/gkh561;
RA Ursic D., Chinchilla K., Finkel J.S., Culbertson M.R.;
RT "Multiple protein/protein and protein/RNA interactions suggest roles for
RT yeast DNA/RNA helicase Sen1p in transcription, transcription-coupled DNA
RT repair and RNA processing.";
RL Nucleic Acids Res. 32:2441-2452(2004).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF GLU-1597.
RX PubMed=17157256; DOI=10.1016/j.molcel.2006.10.023;
RA Steinmetz E.J., Warren C.L., Kuehner J.N., Panbehi B., Ansari A.Z.,
RA Brow D.A.;
RT "Genome-wide distribution of yeast RNA polymerase II and its control by
RT Sen1 helicase.";
RL Mol. Cell 24:735-746(2006).
CC -!- FUNCTION: ATP-dependent 5'->3' DNA/RNA helicase required for the
CC expression and maturation of diverse classes of non-protein-coding RNAs
CC like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar
CC (snoRNA) RNAs. Directs RNA polymerase II transcription termination on
CC snoRNAs as well as on several short protein-coding genes. May also play
CC a role in transcription-coupled nucleotide excision repair.
CC {ECO:0000269|PubMed:11565036, ECO:0000269|PubMed:15121901,
CC ECO:0000269|PubMed:17157256, ECO:0000269|PubMed:8943355,
CC ECO:0000269|PubMed:9365256, ECO:0000269|PubMed:9819377}.
CC -!- SUBUNIT: Interacts with RAD2, RNT1 and RPB1. Binds to multiple snoRNAs.
CC {ECO:0000269|PubMed:15121901}.
CC -!- INTERACTION:
CC Q00416; P32598: GLC7; NbExp=8; IntAct=EBI-16945, EBI-13715;
CC Q00416; P38996: NAB3; NbExp=5; IntAct=EBI-16945, EBI-11776;
CC Q00416; P07276: RAD2; NbExp=3; IntAct=EBI-16945, EBI-14757;
CC Q00416; Q02555: RNT1; NbExp=2; IntAct=EBI-16945, EBI-15673;
CC Q00416; P04050: RPO21; NbExp=4; IntAct=EBI-16945, EBI-15760;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:8544822}.
CC -!- MISCELLANEOUS: Present with 125 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB63976.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U20939; AAB67502.1; -; Genomic_DNA.
DR EMBL; U21094; AAB67523.1; -; Genomic_DNA.
DR EMBL; M74589; AAB63976.1; ALT_FRAME; mRNA.
DR EMBL; BK006945; DAA09731.1; -; Genomic_DNA.
DR PIR; S53416; S53416.
DR RefSeq; NP_013534.3; NM_001182318.3.
DR PDB; 5MZN; X-ray; 1.79 A; A=1095-1470, A=1525-1902.
DR PDB; 6GC3; NMR; -; B=2052-2063.
DR PDB; 6I59; X-ray; 2.95 A; A=1095-1470, A=1539-1904.
DR PDB; 6O3W; X-ray; 2.10 A; C/D=1882-1895.
DR PDB; 6O3X; X-ray; 1.99 A; D/E/F=2053-2064.
DR PDB; 6O3Y; X-ray; 2.80 A; D/E/F=2181-2193.
DR PDBsum; 5MZN; -.
DR PDBsum; 6GC3; -.
DR PDBsum; 6I59; -.
DR PDBsum; 6O3W; -.
DR PDBsum; 6O3X; -.
DR PDBsum; 6O3Y; -.
DR AlphaFoldDB; Q00416; -.
DR SMR; Q00416; -.
DR BioGRID; 31689; 473.
DR ComplexPortal; CPX-1316; NRD1 snoRNA termination complex.
DR ComplexPortal; CPX-1604; Small ribosomal subunit processome, variant 1.
DR ComplexPortal; CPX-1607; Small ribosomal subunit processome, variant 2.
DR ComplexPortal; CPX-1608; Small ribosomal subunit processome, variant 3.
DR DIP; DIP-881N; -.
DR IntAct; Q00416; 105.
DR MINT; Q00416; -.
DR STRING; 4932.YLR430W; -.
DR iPTMnet; Q00416; -.
DR MaxQB; Q00416; -.
DR PaxDb; Q00416; -.
DR PRIDE; Q00416; -.
DR TopDownProteomics; Q00416; -.
DR EnsemblFungi; YLR430W_mRNA; YLR430W; YLR430W.
DR GeneID; 851150; -.
DR KEGG; sce:YLR430W; -.
DR SGD; S000004422; SEN1.
DR VEuPathDB; FungiDB:YLR430W; -.
DR eggNOG; KOG1801; Eukaryota.
DR GeneTree; ENSGT00940000174323; -.
DR HOGENOM; CLU_000459_2_0_1; -.
DR InParanoid; Q00416; -.
DR OMA; YGCSKCI; -.
DR BioCyc; YEAST:G3O-32489-MON; -.
DR BRENDA; 3.6.4.12; 984.
DR PRO; PR:Q00416; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q00416; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0035649; C:Nrd1 complex; IDA:SGD.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005657; C:replication fork; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IPI:ComplexPortal.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IDA:SGD.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; IDA:SGD.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; ISS:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0019904; F:protein domain specific binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0045454; P:cell redox homeostasis; IMP:SGD.
DR GO; GO:0045005; P:DNA-templated DNA replication maintenance of fidelity; IMP:SGD.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IMP:SGD.
DR GO; GO:0030490; P:maturation of SSU-rRNA; IC:ComplexPortal.
DR GO; GO:0031124; P:mRNA 3'-end processing; IMP:SGD.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:SGD.
DR GO; GO:0060257; P:negative regulation of flocculation; IMP:CACAO.
DR GO; GO:1990248; P:regulation of transcription from RNA polymerase II promoter in response to DNA damage; IMP:SGD.
DR GO; GO:0006364; P:rRNA processing; IMP:SGD.
DR GO; GO:0031126; P:sno(s)RNA 3'-end processing; IMP:SGD.
DR GO; GO:0016180; P:snRNA processing; IMP:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IGI:SGD.
DR GO; GO:0008033; P:tRNA processing; IMP:SGD.
DR CDD; cd21408; 1B_Sen1p-like; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR044340; Helicase_Sen1_1B_dom.
DR InterPro; IPR024481; Helicase_Sen1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026121; Sen1.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF487; PTHR10887:SF487; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF12726; SEN1_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; mRNA processing;
KW Nucleotide-binding; Nucleus; Reference proteome; rRNA processing;
KW tRNA processing.
FT CHAIN 1..2231
FT /note="Helicase SEN1"
FT /id="PRO_0000080722"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1032..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1491..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1894..1993
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2032..2231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1909..1927
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1045..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1899..1924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1934..1949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2061..2162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2190..2220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1360..1364
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1619
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1787
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 1597
FT /note="E->K: Causes read-through of both a snoRNA gene
FT terminator and the poly(A) site of a protein-coding gene."
FT /evidence="ECO:0000269|PubMed:17157256"
FT MUTAGEN 1747
FT /note="G->A: In SEN1-1; gives rise to a temperature-
FT sensitive mutant."
FT /evidence="ECO:0000269|PubMed:1569945"
FT HELIX 1100..1109
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1114..1120
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1129..1133
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1137..1139
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1150..1174
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1181..1191
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1194..1202
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1203..1208
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1215..1220
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1233..1237
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1240..1252
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1256..1265
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1269..1273
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1279..1287
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1289..1300
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1301..1303
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1307..1312
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1323..1333
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1337..1348
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1351..1356
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1363..1379
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1406..1412
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1413..1423
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1439..1441
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1450..1453
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1457..1465
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1466..1469
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1544..1561
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1563..1568
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1570..1573
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1575..1578
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1586..1591
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1597..1601
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1602..1606
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1610..1615
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1617..1619
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1627..1631
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1632..1635
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1638..1643
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1653..1657
FT /evidence="ECO:0007829|PDB:6I59"
FT HELIX 1659..1669
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1680..1683
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1687..1690
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1696..1702
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1719..1736
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1737..1739
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1746..1751
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1753..1767
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1768..1771
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1772..1774
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1775..1779
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1780..1785
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1788..1794
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1804..1817
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1820..1829
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1831..1834
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1838..1849
FT /evidence="ECO:0007829|PDB:5MZN"
FT STRAND 1853..1856
FT /evidence="ECO:0007829|PDB:5MZN"
FT TURN 1858..1861
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1866..1873
FT /evidence="ECO:0007829|PDB:5MZN"
FT HELIX 1891..1893
FT /evidence="ECO:0007829|PDB:6O3W"
SQ SEQUENCE 2231 AA; 252497 MW; 88F0FF95B3A8BD89 CRC64;
MNSNNPDNNN SNNINNNNKD KDIAPNSDVQ LATVYTKAKS YIPQIEQVYQ GTNPNIQEAK
LLGELLQVLA EVPKGTHLFC DPILEPISIF SLTIFSFNEE ATATWLKNHF NPILSVCDKC
ILNFARGKCK MLQHFAIQRH VPHEHVAKFN DIVCQWRVEA VFPILRNISV NDNTGINITN
EIETAMYECL CNPHMLRLNK QLKATFEAIF KFFYDTKHRL LDVTNPLSIK TFISGVIFCW
CEGSKEENEW SRAFLKDLYS RNFHINLSNL TPDIIEEVYI HILFLQNPAN WTEIVVSQFW
SRLLPVFNLF DKDVFIEYFQ VPKNVESLKK TFKFPLEPIF KMWYNHLSKS YHDKPLDFLL
RGLTMFLNKF GSEFWSKIEP FTFHSILDII FNRDSFPIKL IKIQDNPIVE HQTEVYFQLT
GSVTDLLSWT LPFYHALSPS KRIQMVRKVS MAFLRIIANY PSLKSIPKAC LMNSATALLR
AVLTIKENER AMLYKNDEFE TVLLTKTDSR ALLNNPLIQD IIIRSASNPN DFYPGLGAAS
ASVATSTMMV LAECIDFDIL LLCHRTFKLY SGKPISEIPI STNVLENVTN KIDLRSFHDG
PLLAKQLLVS LKNINGLLIV PSNTAVAEAH NALNQKFLLL STRLMEKFAD ILPGQLSKIL
ADEDASQGFW SCIFSSDKHL YQAATNILYN TFDVEGRLEG ILAILNSNLT VNLKNINVML
QRLINCEFYE PCPRAVRVLM DVVSAFVDPI SGVFANFQTL KSQNTEKEFL KFWESCWLFL
DTIYKFTLKW ASKYDYSELE NFTKDTLDLS RSLVDSFREF SDILHDQTKN LLLNVLETFK
NMLYWLRLSD EVLLESCVRL IISTSDLAHE KHVKVDDSLV EMMAKYASKA KRFSNKLTEQ
QASEILQKAK IFNKALTEEV ATEAENYRKE KELSRLGKVI DLTDSVPASP SLSPSLSSTI
ASSSAESRAD YLQRKALSSS ITGRPRVAQP KITSFGTFQS SANAKLHRTK PVKPLSKMEL
ARMQLLNNRV VHPPSAPAFH TKSRGLSNKN DDSSSEESDN DIESARELFA IAKAKGKGIQ
TVDINGKVVK RQTAAELAKQ ELEHMRKRLN VDMNPLYEII LQWDYTRNSE YPDDEPIGNY
SDVKDFFNSP ADYQKVMKPL LLLESWQGLC SSRDREDYKP FSIIVGNRTA VSDFYDVYAS
VAKQVIQDCG ISESDLIVMA YLPDFRPDKR LSSDDFKKAQ HTCLAKVRTL KNTKGGNVDV
TLRIHRNHSF SKFLTLRSEI YCVKVMQMTT IEREYSTLEG LEYYDLVGQI LQAKPSPPVN
VDAAEIETVK KSYKLNTSQA EAIVNSVSKE GFSLIQGPPG TGKTKTILGI IGYFLSTKNA
SSSNVIKVPL EKNSSNTEQL LKKQKILICA PSNAAVDEIC LRLKSGVYDK QGHQFKPQLV
RVGRSDVVNV AIKDLTLEEL VDKRIGERNY EIRTDPELER KFNNAVTKRR ELRGKLDSES
GNPESPMSTE DISKLQLKIR ELSKIINELG RDRDEMREKN SVNYRNRDLD RRNAQAHILA
VSDIICSTLS GSAHDVLATM GIKFDTVIID EACQCTELSS IIPLRYGGKR CIMVGDPNQL
PPTVLSGAAS NFKYNQSLFV RMEKNSSPYL LDVQYRMHPS ISKFPSSEFY QGRLKDGPGM
DILNKRPWHQ LEPLAPYKFF DIISGRQEQN AKTMSYTNME EIRVAIELVD YLFRKFDNKI
DFTGKIGIIS PYREQMQKMR KEFARYFGGM INKSIDFNTI DGFQGQEKEI ILISCVRADD
TKSSVGFLKD FRRMNVALTR AKTSIWVLGH QRSLAKSKLW RDLIEDAKDR SCLAYACSGF
LDPRNNRAQS ILRKFNVPVP SEQEDDYKLP MEYITQGPDE VKSNKDTKKR RVVDEGEEAD
KAVKKKKKEK KKEKKKSKAD DKKKNNKKAE SPSTSSGTKK KSSIFGGMSV PSAVVPKTFP
DVDSNKKAAA VVGKKKNNKH VCFSDDVSFI PRNDEPEIKV TRSLSSVLKE KQLGLKETRT
ISPPEISNNE DDDDEDDYTP SISDSSLMKS EANGRNNRVA SHNQNFSASI YDDPQVSQAK
QTQVPAAITK HRSSNSVLSG GSSRILTASD YGEPNQNGQN GANRTLSQHV GNANQYSTAP
VGTGELHETL PAHPQDSYPA EAEDPYDLNP HPQPQSSAFK GPGSGPTGTR NSSRRNASSS
PFIPKKRKPR S
