INO80_MOUSE
ID INO80_MOUSE Reviewed; 1559 AA.
AC Q6ZPV2; A2AQP8; Q6P7V0; Q6PCP1; Q8C9T7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Chromatin-remodeling ATPase INO80 {ECO:0000305};
DE EC=3.6.4.- {ECO:0000250|UniProtKB:Q9ULG1};
DE AltName: Full=DNA helicase-related INO80 complex homolog 1 {ECO:0000305};
DE AltName: Full=DNA helicase-related protein INO80 {ECO:0000305};
GN Name=Ino80; Synonyms=Inoc1, Kiaa1259;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-746 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 357-1559 (ISOFORM 2).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 472-1559 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 TISSUE SPECIFICITY.
RX PubMed=16298340; DOI=10.1016/j.bbrc.2005.10.206;
RA Bakshi R., Mehta A.K., Sharma R., Maiti S., Pasha S., Brahmachari V.;
RT "Characterization of a human SWI2/SNF2 like protein hINO80: demonstration
RT of catalytic and DNA binding activity.";
RL Biochem. Biophys. Res. Commun. 339:313-320(2006).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=20971067; DOI=10.1016/j.bbrc.2010.10.066;
RA Kashiwaba S., Kitahashi K., Watanabe T., Onoda F., Ohtsu M., Murakami Y.;
RT "The mammalian INO80 complex is recruited to DNA damage sites in an ARP8
RT dependent manner.";
RL Biochem. Biophys. Res. Commun. 402:619-625(2010).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: ATPase component of the chromatin remodeling INO80 complex
CC which is involved in transcriptional regulation, DNA replication and
CC DNA repair. Binds DNA. As part of the INO80 complex, remodels chromatin
CC by shifting nucleosomes. Regulates transcription upon recruitment by
CC YY1 to YY1-activated genes, where it acts as an essential coactivator.
CC Involved in UV-damage excision DNA repair. The contribution to DNA
CC double-strand break repair appears to be largely indirect through
CC transcriptional regulation. Involved in DNA replication. Required for
CC microtubule assembly during mitosis thereby regulating chromosome
CC segregation cycle. {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9ULG1};
CC -!- ACTIVITY REGULATION: Activated upon binding to double stranded DNA or
CC nucleosomes. {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex; three
CC different complex modules assemble on different domains of INO80.
CC Interacts with DDB1. Interacts with transcriptional repressor protein
CC YY1; the interaction recruits the INO80 complex to YY1 target genes.
CC Interacts with YY1AP1. Interacts with tubulin alpha.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9ULG1}. Nucleus
CC {ECO:0000255|PROSITE-ProRule:PRU00746, ECO:0000269|PubMed:20971067}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9ULG1}.
CC Chromosome {ECO:0000250|UniProtKB:Q9ULG1}. Note=Localizes to the
CC cytoplasm in quiescent cell. Associates with spindle microtubules
CC during mitosis. Colocalizes with PCNA at replication forks during S-
CC phase. Recruited to DNA damage sites in a ACTR8-dependent manner.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZPV2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZPV2-2; Sequence=VSP_020334;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16298340}.
CC -!- DOMAIN: The DBINO region is involved in binding to DNA.
CC {ECO:0000250|UniProtKB:Q9ULG1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AL844862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK040612; BAC30644.1; -; mRNA.
DR EMBL; AK129317; BAC98127.1; -; Transcribed_RNA.
DR EMBL; BC059235; AAH59235.1; -; mRNA.
DR CCDS; CCDS16602.1; -. [Q6ZPV2-1]
DR RefSeq; NP_080850.2; NM_026574.3. [Q6ZPV2-1]
DR AlphaFoldDB; Q6ZPV2; -.
DR SMR; Q6ZPV2; -.
DR BioGRID; 212678; 5.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR CORUM; Q6ZPV2; -.
DR IntAct; Q6ZPV2; 6.
DR MINT; Q6ZPV2; -.
DR STRING; 10090.ENSMUSP00000051845; -.
DR iPTMnet; Q6ZPV2; -.
DR PhosphoSitePlus; Q6ZPV2; -.
DR EPD; Q6ZPV2; -.
DR MaxQB; Q6ZPV2; -.
DR PaxDb; Q6ZPV2; -.
DR PeptideAtlas; Q6ZPV2; -.
DR PRIDE; Q6ZPV2; -.
DR ProteomicsDB; 267339; -. [Q6ZPV2-1]
DR ProteomicsDB; 267340; -. [Q6ZPV2-2]
DR Antibodypedia; 42067; 90 antibodies from 24 providers.
DR DNASU; 68142; -.
DR Ensembl; ENSMUST00000049920; ENSMUSP00000051845; ENSMUSG00000034154. [Q6ZPV2-1]
DR GeneID; 68142; -.
DR KEGG; mmu:68142; -.
DR UCSC; uc008ltt.2; mouse. [Q6ZPV2-1]
DR CTD; 54617; -.
DR MGI; MGI:1915392; Ino80.
DR VEuPathDB; HostDB:ENSMUSG00000034154; -.
DR eggNOG; KOG0388; Eukaryota.
DR GeneTree; ENSGT00900000141110; -.
DR HOGENOM; CLU_000315_19_1_1; -.
DR InParanoid; Q6ZPV2; -.
DR OMA; FWKKNER; -.
DR OrthoDB; 188211at2759; -.
DR PhylomeDB; Q6ZPV2; -.
DR TreeFam; TF324408; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 68142; 18 hits in 114 CRISPR screens.
DR ChiTaRS; Ino80; mouse.
DR PRO; PR:Q6ZPV2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6ZPV2; protein.
DR Bgee; ENSMUSG00000034154; Expressed in inner cell mass derived hypoblast and 229 other tissues.
DR ExpressionAtlas; Q6ZPV2; baseline and differential.
DR Genevisible; Q6ZPV2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0034644; P:cellular response to UV; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0010571; P:positive regulation of nuclear cell cycle DNA replication; ISO:MGI.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0043618; P:regulation of transcription from RNA polymerase II promoter in response to stress; IBA:GO_Central.
DR GO; GO:0051225; P:spindle assembly; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0070914; P:UV-damage excision repair; ISO:MGI.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR031047; Ino80.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45685:SF2; PTHR45685:SF2; 1.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51413; DBINO; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Alternative splicing; ATP-binding; Cell cycle;
KW Cell division; Chromosome; Cytoplasm; Cytoskeleton; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Hydrolase; Microtubule;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1559
FT /note="Chromatin-remodeling ATPase INO80"
FT /id="PRO_0000248830"
FT DOMAIN 282..407
FT /note="DBINO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00746"
FT DOMAIN 532..703
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1108..1263
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..268
FT /note="Assembles INO80 complex module with putative
FT regulatory components INO80E, INO80F, UCHL5, NFRKB, MCRS1
FT and IN80D"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG1"
FT REGION 46..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..528
FT /note="Assembles INO80 complex module consisting of
FT conserved components ACTR8, ACTL6A and YY1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG1"
FT REGION 523..1559
FT /note="Assembles INO80 complex module consisting of
FT conserved components INO80B, INO80C, ACTR5, RVBL1, RVBL2"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG1"
FT REGION 1285..1319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1391..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1504..1559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..230
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 545..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 118
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG1"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULG1"
FT VAR_SEQ 608..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_020334"
SQ SEQUENCE 1559 AA; 176520 MW; A02B780D0B13D08F CRC64;
MASELGAGDD GSSTELAKPL YLQYLERALR LDHFLRQTSA IFNRNISSDD SEDGLDDNNP
LLPESGDPLI QVKEEPPNSL LGETSGASSS GLLNPYSLNG VLQSESKSDK GNLYNFSKLK
KSRKWLKSIL LSDESSEADS QSEDNDDEEE ELSLSREELH NMLRLHKYKK LHQNKYSKDK
ELQQYQYYSA GLLSTYDPFY EQQRHLLGPK KKKFKEDKKL KAKLKKVKKK RRRDEEFSSE
ESPRHHHHQT KVFAKFSHDA PPPGTKKKHL SIEQLNARRR KVWLSIVKKE LPKANKQKSS
ARNLFLTNSR KLAHQCMKEV RRAALQAQKN CKETLPRARR LTKEMLLYWK KYEKVEKEHR
KRAEKEALEQ RKLDEEMREA KRQQRKLNFL ITQTELYAHF MSRKRDMGHD GIQEEILRKL
EDSSTQRQID IGGGVVVNIT QEDYDSNHFK AQALKNAENA YHIHQARTRS FDEDAKESRA
AALRAADKSG SGFGESYSLA NPSIRAGEDI PQPTIFNGKL KGYQLKGMNW LANLYEQGIN
GILADEMGLG KTVQSIALLA HLAERENIWG PFLIISPAST LNNWHQEFTR FVPKFKVLPY
WGNPHDRKVI RRFWSQKTLY TQDAPFHVVI TSYQLVVQDV KYFQRVKWQY MVLDEAQALK
SSSSVRWKIL LQFQCRNRLL LTGTPIQNTM AELWALLHFI MPTLFDSHEE FNEWFSKDIE
SHAENKSAID ENQLSRLHMI LKPFMLRRIK KDVENELSDK IEILTYCQLT SRQKLLYQAL
KNKISIEDLL QSSMGSTQQA QNTTSSLMNL VMQFRKVCNH PELFERQETW SPFHISLKPY
EISKFIYRHG QIRVFNHSRD RWLKVLLSPF APDYIQQSLF HRKGINEGSC FSFLRFIDVS
PAEMANLMLQ GLLARWLALF LSLKASYRLH QLRSWAEPDG TSHQSYLRNK DFLLGVDFPL
SFPNLCSCPL LKSLVFSSHC KAVSGYSDHV VHQRRSATSS LRCCLLTELP SFLCVASPRV
TAVPLDSYCN DRSAEYERGV LKEGGSLAAK QCLLNGAPEL ATDWLSRRSQ FFPEPAGGLL
SIRPQNGWSF IRIPGKESLI TDSGKLYALD VLLTRLKSQG HRVLIYSQMT RMIDLLEEYM
VYRKHTYMRL DGSSKISERR DMVADFQTRN DIFVFLLSTR AGGLGINLTA ADTVIFYDSD
WNPTVDQQAM DRAHRLGQTK QVTVYRLICK GTIEERILQR AKEKSEIQRM VISGGNFKPD
TLKPKEVVSL LLDDEELEKK LRLRQEEKRQ QEESNRVKER KRKREKYAEK KKKEDELDGK
RRKEGVNLVI PFVPSADNSN LSADGDDSFI SVDSAMPSPF SEISISSELH TGSIPPDESS
SDMLVIVDDP ASSAPQSRAT NSPASITGSV SDTVNGISIQ EVPAAGRGHS ARSRGRPKGS
GSTAKGAGKG RSRKSTAGSA AAMAGAKAGA AAASAAAYAA YGYNVSKGIS ASSPLQTSIV
RPAGLADFGP SSASSPLSSP LNKGNNIPGT PKSLHMTSSL ASDSLIRKQG KGTNPSGGR
