ISW1_YEAST
ID ISW1_YEAST Reviewed; 1129 AA.
AC P38144; D6VQP1;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW1;
DE EC=3.6.4.-;
GN Name=ISW1; OrderedLocusNames=YBR245C; ORFNames=YBR1633;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP SEQUENCE REVISION.
RA Aljinovic G., Pohl F.M., Pohl T.M.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP FUNCTION, IDENTIFICATION IN AN ISW1-TYPE COMPLEX, AND MUTAGENESIS OF
RP LYS-227.
RX PubMed=10090725; DOI=10.1101/gad.13.6.686;
RA Tsukiyama T., Palmer J., Landel C.C., Shiloach J., Wu C.;
RT "Characterization of the imitation switch subfamily of ATP-dependent
RT chromatin-remodeling factors in Saccharomyces cerevisiae.";
RL Genes Dev. 13:686-697(1999).
RN [5]
RP FUNCTION.
RX PubMed=11238381; DOI=10.1101/gad.190301;
RA Kent N.A., Karabetsou N., Politis P.K., Mellor J.;
RT "In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p.";
RL Genes Dev. 15:619-626(2001).
RN [6]
RP FUNCTION OF THE ISW1A COMPLEX, AND FUNCTION OF THE ISW1B COMPLEX.
RX PubMed=14622597; DOI=10.1016/s0092-8674(03)00880-8;
RA Morillon A., Karabetsou N., O'Sullivan J., Kent N., Proudfoot N.,
RA Mellor J.;
RT "Isw1 chromatin remodeling ATPase coordinates transcription elongation and
RT termination by RNA polymerase II.";
RL Cell 115:425-435(2003).
RN [7]
RP IDENTIFICATION IN ISW1-TYPE COMPLEXES, FUNCTION OF THE ISW1A COMPLEX, AND
RP FUNCTION OF THE ISW1B COMPLEX.
RX PubMed=12482963; DOI=10.1128/mcb.23.1.80-91.2003;
RA Vary J.C. Jr., Gangaraju V.K., Qin J., Landel C.C., Kooperberg C.,
RA Bartholomew B., Tsukiyama T.;
RT "Yeast Isw1p forms two separable complexes in vivo.";
RL Mol. Cell. Biol. 23:80-91(2003).
RN [8]
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 [9]
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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-694 AND SER-846, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Catalytic component of ISW1-type complexes, which act by
CC remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC the structure of nucleosomal DNA. They are involved in coordinating
CC transcriptional repression, activation and elongation phases. The ISW1A
CC complex represses gene expression at initiation through specific
CC positioning of a promoter proximal dinucleosome. The ISW1B complex acts
CC within coding regions to control the amount of RNA polymerase II
CC released into productive elongation and to coordinate elongation with
CC termination and pre-mRNA processing. {ECO:0000269|PubMed:10090725,
CC ECO:0000269|PubMed:11238381, ECO:0000269|PubMed:12482963,
CC ECO:0000269|PubMed:14622597}.
CC -!- SUBUNIT: Component of the ISW1A complex, which at least consists of
CC ISW1 and IOC3. Component of the ISW1B complex, which at least consists
CC of ISW1, IOC2 and IOC4. {ECO:0000269|PubMed:10090725,
CC ECO:0000269|PubMed:12482963}.
CC -!- INTERACTION:
CC P38144; Q12072: IOC2; NbExp=6; IntAct=EBI-21087, EBI-30191;
CC P38144; P43596: IOC3; NbExp=11; IntAct=EBI-21087, EBI-22944;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 1500 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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DR EMBL; Z36114; CAA85208.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07361.1; -; Genomic_DNA.
DR PIR; S46122; S46122.
DR RefSeq; NP_009804.1; NM_001178593.1.
DR PDB; 2Y9Y; X-ray; 3.25 A; A=763-1129.
DR PDB; 2Y9Z; X-ray; 3.60 A; A=763-1129.
DR PDB; 6IRO; EM; 3.40 A; L=69-1129.
DR PDB; 6JYL; EM; 3.37 A; K=69-1129.
DR PDB; 6K1P; EM; 3.87 A; K=69-1129.
DR PDBsum; 2Y9Y; -.
DR PDBsum; 2Y9Z; -.
DR PDBsum; 6IRO; -.
DR PDBsum; 6JYL; -.
DR PDBsum; 6K1P; -.
DR AlphaFoldDB; P38144; -.
DR SMR; P38144; -.
DR BioGRID; 32940; 1887.
DR ComplexPortal; CPX-636; ISW1b chromatin remodeling complex.
DR ComplexPortal; CPX-637; ISW1a chromatin remodeling complex.
DR DIP; DIP-6601N; -.
DR IntAct; P38144; 71.
DR MINT; P38144; -.
DR STRING; 4932.YBR245C; -.
DR iPTMnet; P38144; -.
DR MaxQB; P38144; -.
DR PaxDb; P38144; -.
DR PRIDE; P38144; -.
DR EnsemblFungi; YBR245C_mRNA; YBR245C; YBR245C.
DR GeneID; 852547; -.
DR KEGG; sce:YBR245C; -.
DR SGD; S000000449; ISW1.
DR VEuPathDB; FungiDB:YBR245C; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000176603; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; P38144; -.
DR OMA; REINRWT; -.
DR BioCyc; YEAST:G3O-29174-MON; -.
DR EvolutionaryTrace; P38144; -.
DR PRO; PR:P38144; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38144; protein.
DR GO; GO:0016587; C:Isw1 complex; IPI:ComplexPortal.
DR GO; GO:0036436; C:Isw1a complex; IDA:SGD.
DR GO; GO:0036437; C:Isw1b complex; IDA:SGD.
DR GO; GO:0030874; C:nucleolar chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006354; P:DNA-templated transcription, elongation; IDA:SGD.
DR GO; GO:1900050; P:negative regulation of histone exchange; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:SGD.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0009408; P:response to heat; IC:ComplexPortal.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IGI:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IGI:SGD.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1129
FT /note="ISWI chromatin-remodeling complex ATPase ISW1"
FT /id="PRO_0000074330"
FT DOMAIN 208..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 506..657
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 882..935
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 988..1052
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 144..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1073..1129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 324..327
FT /note="DEAH box"
FT COMPBIAS 1073..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 221..228
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 694
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 227
FT /note="K->A: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:10090725"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 198..212
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 227..240
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 282..288
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 289..294
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 297..301
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 311..315
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 335..340
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 360..368
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 390..392
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:6IRO"
FT HELIX 398..405
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:6JYL"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 425..431
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 435..445
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 468..477
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 496..500
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 503..517
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 521..524
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 528..540
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 555..564
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 575..577
FT /evidence="ECO:0007829|PDB:6IRO"
FT TURN 578..581
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 582..584
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 592..597
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 602..609
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:6JYL"
FT STRAND 622..628
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 632..656
FT /evidence="ECO:0007829|PDB:6JYL"
FT HELIX 814..827
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT TURN 828..830
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 835..838
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT TURN 839..841
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT TURN 848..850
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 851..862
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT STRAND 866..868
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 870..882
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 889..902
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 907..911
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT STRAND 917..919
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 920..932
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT TURN 941..943
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 944..968
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 974..977
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 994..1007
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 1015..1024
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 1027..1029
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 1032..1035
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT HELIX 1039..1054
FT /evidence="ECO:0007829|PDB:2Y9Y"
FT TURN 1055..1058
FT /evidence="ECO:0007829|PDB:2Y9Y"
SQ SEQUENCE 1129 AA; 131102 MW; 2CF86BAF553E6695 CRC64;
MAYMLAIANF HFFKFYTRMR KKHENNSCNE KDKDENLFKI ILAIFLQEKK KYDCISSGSI
MTASEEYLEN LKPFQVGLPP HDPESNKKRY LLKDANGKKF DLEGTTKRFE HLLSLSGLFK
HFIESKAAKD PKFRQVLDVL EENKANGKGK GKHQDVRRRK TEHEEDAELL KEEDSDDDES
IEFQFRESPA YVNGQLRPYQ IQGVNWLVSL HKNKIAGILA DEMGLGKTLQ TISFLGYLRY
IEKIPGPFLV IAPKSTLNNW LREINRWTPD VNAFILQGDK EERAELIQKK LLGCDFDVVI
ASYEIIIREK SPLKKINWEY IIIDEAHRIK NEESMLSQVL REFTSRNRLL ITGTPLQNNL
HELWALLNFL LPDIFSDAQD FDDWFSSEST EEDQDKIVKQ LHTVLQPFLL RRIKSDVETS
LLPKKELNLY VGMSSMQKKW YKKILEKDLD AVNGSNGSKE SKTRLLNIMM QLRKCCNHPY
LFDGAEPGPP YTTDEHLVYN AAKLQVLDKL LKKLKEEGSR VLIFSQMSRL LDILEDYCYF
RNYEYCRIDG STAHEDRIQA IDDYNAPDSK KFVFLLTTRA GGLGINLTSA DVVVLYDSDW
NPQADLQAMD RAHRIGQKKQ VKVFRLVTDN SVEEKILERA TQKLRLDQLV IQQNRTSLKK
KENKADSKDA LLSMIQHGAA DVFKSGTSTG SAGTPEPGSG EKGDDIDLDE LLLKSENKTK
SLNAKYETLG LDDLQKFNQD SAYEWNGQDF KKKIQRDIIS PLLLNPTKRE RKENYSIDNY
YKDVLNTGRS STPSHPRMPK PHVFHSHQLQ PPQLKVLYEK ERMWTAKKTG YVPTMDDVKA
AYGDISDEEE KKQKLELLKL SVNNSQPLTE EEEKMKADWE SEGFTNWNKL EFRKFITVSG
KYGRNSIQAI ARELAPGKTL EEVRAYAKAF WSNIERIEDY EKYLKIIENE EEKIKRVKMQ
QEALRRKLSE YKNPFFDLKL KHPPSSNNKR TYSEEEDRFI LLMLFKYGLD RDDVYELVRD
EIRDCPLFEL DFYFRSRTPV ELARRGNTLL QCLEKEFNAG IVLDDATKDR MKKEDENGKR
IREEFADQTA NEKENVDGVE SKKAKIEDTS NVGTEQLVAE KIPENETTH
