TASOR_MOUSE
ID TASOR_MOUSE Reviewed; 1610 AA.
AC Q69ZR9; E9PUH2; Q9CUD3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Protein TASOR {ECO:0000305};
DE AltName: Full=Transgene activation suppressor protein {ECO:0000250|UniProtKB:Q9UK61};
GN Name=Tasor {ECO:0000250|UniProtKB:Q9UK61};
GN Synonyms=D14Abb1e, Fam208a {ECO:0000312|MGI:MGI:1921694},
GN Kiaa1105 {ECO:0000303|PubMed:15368895};
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 1-545 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 764-1610 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1319-1610 (ISOFORM 1).
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
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. 11:205-218(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628; SER-631; SER-836 AND
RP SER-921, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928 (ISOFORM 2), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, Spleen, and Testis;
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).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF LEU-130.
RX PubMed=24781204; DOI=10.1007/s00335-014-9516-0;
RA Harten S.K., Bruxner T.J., Bharti V., Blewitt M., Nguyen T.M., Whitelaw E.,
RA Epp T.;
RT "The first mouse mutants of D14Abb1e (Fam208a) show that it is critical for
RT early development.";
RL Mamm. Genome 25:293-303(2014).
RN [7]
RP FUNCTION, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF LEU-130.
RX PubMed=28839193; DOI=10.1038/s41598-017-09490-w;
RA Bhargava S., Cox B., Polydorou C., Gresakova V., Korinek V., Strnad H.,
RA Sedlacek R., Epp T.A., Chawengsaksophak K.;
RT "The epigenetic modifier Fam208a is required to maintain epiblast cell
RT fitness.";
RL Sci. Rep. 7:9322-9322(2017).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP INPP5A; EML1; SV1L; GPSM2; ITGB3BP; CNTN1; ETFA; PSMD8; S100A10; MPHOSPH8;
RP TMEM100; ALB; PARPBP; HCFC2; NCBP1 AND SETDB1.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: Component of the HUSH complex, a multiprotein complex that
CC mediates epigenetic repression. The HUSH complex is recruited to
CC genomic loci rich in H3K9me3 and is required to maintain
CC transcriptional silencing by promoting recruitment of SETDB1, a histone
CC methyltransferase that mediates further deposition of H3K9me3, as well
CC as MORC2. Also represses L1 retrotransposons in collaboration with
CC MORC2 and, probably, SETDB1, the silencing is dependent of repressive
CC epigenetic modifications, such as H3K9me3 mark. Silencing events often
CC occur within introns of transcriptionally active genes, and lead to the
CC down-regulation of host gene expression. The HUSH complex is also
CC involved in the silencing of unintegrated retroviral DNA by being
CC recruited by ZNF638: some part of the retroviral DNA formed immediately
CC after infection remains unintegrated in the host genome and is
CC transcriptionally repressed (By similarity). Plays a crucial role in
CC early embryonic development (PubMed:31112734, PubMed:24781204,
CC PubMed:28839193). Involved in the organization of spindle poles and
CC spindle apparatus assembly during zygotic division (PubMed:31112734).
CC Plays an important role in maintaining epiblast fitness or potency
CC (PubMed:28839193). {ECO:0000250|UniProtKB:Q9UK61,
CC ECO:0000269|PubMed:24781204, ECO:0000269|PubMed:28839193,
CC ECO:0000269|PubMed:31112734}.
CC -!- SUBUNIT: Component of the HUSH complex; at least composed of TASOR,
CC PPHLN1 and MPHOSPH8 (By similarity). Interacts with MORC2; the
CC interaction associateS MORC2 with the HUSH complex which recruits MORC2
CC to heterochromatic loci (By similarity). Interacts with ZNF638; leading
CC to recruitment of the HUSH complex to unintegrated retroviral DNA (By
CC similarity). Interacts with INPP5A, EML1, SV1L, GPSM2, ITGB3BP, CNTN1,
CC ETFA, PSMD8, S100A10, MPHOSPH8, TMEM100, ALB, PARPBP, HCFC2, NCBP1 and
CC SETDB1 (PubMed:31112734). {ECO:0000250|UniProtKB:Q9UK61,
CC ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24781204}. Chromosome
CC {ECO:0000250|UniProtKB:Q9UK61}. Note=Localizes to chromatin.
CC {ECO:0000250|UniProtKB:Q9UK61}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q69ZR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q69ZR9-2; Sequence=VSP_042114, VSP_042115, VSP_042116,
CC VSP_042117;
CC -!- TISSUE SPECIFICITY: Present in skin, brain and testis (at protein
CC level) (PubMed:24781204). Ubiquitously expressed at low levels in the
CC majority of the organs, expressed at higher levels in kidneys, spleen,
CC thymus, seminal vesicles, uterus, and ovaries and its expression is
CC almost six times higher in male tissues than in females
CC (PubMed:31112734). Highly expressed in seminiferous tubules with a
CC strong signal in Sertoli cells, spermatogonia, and spermatocytes
CC (PubMed:31112734). {ECO:0000269|PubMed:24781204,
CC ECO:0000269|PubMed:31112734}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the epiblast at 5.5 dpc, expression
CC extends into the extraembryonic ectoderm at 6.5 dpc, and at 7.5 dpc
CC expressed in embryonic ectoderm, allantois, amnion and chorion. From
CC 8.5 to 9.5 dpc, ubiquitously expressed in the developing embryo.
CC {ECO:0000269|PubMed:28839193}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethality with robust developmentally
CC delayed phenotype observed at 8.5 dpc, progressing through 9.5 dpc with
CC full lethality by 12.5 dpc (PubMed:24781204, PubMed:28839193). RNAi-
CC mediated knockdown in zygotes results in formation of multipolar
CC spindles and increased ratio of arrested or incorrectly developed
CC embryos (PubMed:28839193). {ECO:0000269|PubMed:24781204,
CC ECO:0000269|PubMed:28839193}.
CC -!- SIMILARITY: Belongs to the TASOR family. {ECO:0000305}.
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DR EMBL; AC154327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154637; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CAAA01054285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT485787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK016751; BAB30409.2; -; mRNA.
DR EMBL; BC037390; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK173099; BAD32377.1; -; mRNA.
DR CCDS; CCDS49432.1; -. [Q69ZR9-2]
DR RefSeq; NP_001108351.1; NM_001114879.1.
DR RefSeq; NP_083221.1; NM_028945.1. [Q69ZR9-2]
DR AlphaFoldDB; Q69ZR9; -.
DR SMR; Q69ZR9; -.
DR BioGRID; 230071; 3.
DR IntAct; Q69ZR9; 1.
DR MINT; Q69ZR9; -.
DR STRING; 10090.ENSMUSP00000022450; -.
DR iPTMnet; Q69ZR9; -.
DR PhosphoSitePlus; Q69ZR9; -.
DR EPD; Q69ZR9; -.
DR jPOST; Q69ZR9; -.
DR MaxQB; Q69ZR9; -.
DR PaxDb; Q69ZR9; -.
DR PeptideAtlas; Q69ZR9; -.
DR PRIDE; Q69ZR9; -.
DR ProteomicsDB; 263251; -. [Q69ZR9-1]
DR ProteomicsDB; 263252; -. [Q69ZR9-2]
DR Antibodypedia; 1875; 29 antibodies from 13 providers.
DR Ensembl; ENSMUST00000022450; ENSMUSP00000022450; ENSMUSG00000040651. [Q69ZR9-2]
DR GeneID; 218850; -.
DR KEGG; mmu:218850; -.
DR UCSC; uc007stt.1; mouse. [Q69ZR9-2]
DR UCSC; uc011zhv.1; mouse. [Q69ZR9-1]
DR CTD; 23272; -.
DR MGI; MGI:1921694; Tasor.
DR VEuPathDB; HostDB:ENSMUSG00000040651; -.
DR eggNOG; ENOG502QUY9; Eukaryota.
DR GeneTree; ENSGT00530000063735; -.
DR HOGENOM; CLU_004573_0_0_1; -.
DR InParanoid; Q69ZR9; -.
DR OMA; CTKIENV; -.
DR OrthoDB; 57214at2759; -.
DR PhylomeDB; Q69ZR9; -.
DR TreeFam; TF336055; -.
DR BioGRID-ORCS; 218850; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Fam208a; mouse.
DR PRO; PR:Q69ZR9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q69ZR9; protein.
DR Bgee; ENSMUSG00000040651; Expressed in manus and 227 other tissues.
DR ExpressionAtlas; Q69ZR9; baseline and differential.
DR Genevisible; Q69ZR9; MM.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0090307; P:mitotic spindle assembly; IMP:MGI.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISS:UniProtKB.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0097355; P:protein localization to heterochromatin; ISS:UniProtKB.
DR InterPro; IPR022188; DUF3715.
DR Pfam; PF12509; DUF3715; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT CHAIN 2..1610
FT /note="Protein TASOR"
FT /id="PRO_0000295729"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 915..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 924..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 793
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1004
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 1059
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT MOD_RES 1508
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT CROSSLNK 581
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT CROSSLNK 825
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT CROSSLNK 866
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UK61"
FT VAR_SEQ 857..867
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042114"
FT VAR_SEQ 935
FT /note="P -> PGMKSPGEQLVCLPPVEAFPNDPRVINRERSCDYQFPSSPST (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042115"
FT VAR_SEQ 1451..1468
FT /note="ALLENDEKDEEDMSLDSG -> DAVLTLTPLELGVGISQH (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042116"
FT VAR_SEQ 1469..1610
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042117"
FT MUTAGEN 130
FT /note="L->P: In MommeD6; severe developmental delay leading
FT to lethality before gastrulation. Mutants exhibit impaired
FT primitive streak elongation, delayed epithelial-to-
FT mesenchymal transition during gastrulation and an increase
FT in p53/TP53-driven apoptosis. Epiblasts show an increased
FT expression of p53 pathway genes as well as several
FT pluripotency-associated long non-coding RNAs."
FT /evidence="ECO:0000269|PubMed:24781204"
FT MOD_RES Q69ZR9-2:928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1610 AA; 181396 MW; B8DDF5E02905CE9F CRC64;
MATAAETEAP STDASWKSRG GGGGDDGMKP ALPELESSLQ NGGGDGGGGA GPEETAAAEA
ARSYGHEQPQ QTSEAAAAAL PKGAEEPERP FRRSFQIPRK SREKKALFQP LTPGSREFED
VLNILHSSYL EPSSVTYFNY RRACLIHNEL LEKEFTEKRR ELKFDGRLDK ELSESYAFLM
VDRYQVQSIC EKGLQVGQSK ITVLGSPSMG IYLCRYADLL QANPLEAGAV GDVVIFKIMK
GKIKSIYDPL SVKSLESMLS KNALDPTPKH ECHVSKNASR ITSLLAYRAY ELTQYYFYEY
GFDEVRRRPR HVCPYAVVSF TYKDDVQTPK FLSPLRSNSF NADRNIDKFN YTLWKGQLLN
KGKLLCYISL RSANRAFLPV KLPEKLDVET VMSIDCLKQK IPPSFFYKDT YVGPNEVLKN
GMYCSLYEVV EKTRIGSNME CLLQKLEKEK LVLVKPLGDR GYLFLLSPFQ MVSPYEHQTV
KSRILHALFL FQEPRCLIIT QKGIMNTTPL EKPENLADIL KITQFLQFSL IQCRKEFKTI
NTINFHSVVE KYVSEFFKRG FGSGKREFFM FSYDSRLDDR KFLYSAPRNK SHIDDCLHTY
IYQPEMYQLS IFKLKELFEE NWRRQQFSPL SDYEGQEEEL NGSKMKFGKR NNSRDETTEP
EQQKSSHSLD YDKDRVKELI NLIQCTKKNV GGDPDPEDTK SKNVLKRKLE DLPENMRKFA
KTSNSTESCH LYEESPQSIG LLGQDPNLRV QQEDSGNTGD IHKLYNWLSE ALANARHSDG
FLTETVNKAL GLSSSGAYEE LKQKCDYELN STLDKKESEQ PACTKIENVH FKDAQSPLLE
VDAASVKYPP LLSSSEVGIN HKLHCKEDPN LINVNNFEGC SLCPTVSIEH GFLRQHSKSN
DDEETEIHWK LIPITGGNAG SPEDQHGKHG EKQTPDTLKG TTEEDTVTAG QAMAVEEQCV
PAAELPRVSE ITENTVLGEF HLFSRKVEEI LKEKNVSYVS AISTPIFSAQ EKMNRLSEFI
HSNTSKAGVE EFVDGLHEKL NTVVITASAK GVSLPPAVSA NHSHAAAALA SLGRRVVSIS
SSDFSAKELF EPLCSEHLKD NNSNEQYSSS VEVEMNRPHH CKELMLTSDH TVPGDTVLEP
TEKEITKSPS DITISAQPAL SNFISQLEPE VFNSLVKIMK DVQKNTVKFY IHEEEESVLC
KEIKEYLTKL GNTECHPDQF LERRSNLDKL LIIIQNEDIA GFIHKVPGLV TLKKLPCVSF
AGVDSLDDVK NHTYNELFVS GGFIVSDESI LNLEVVTIES LKIFLTFLEE LSTPEGKWQW
KIHCKFQKKL KELGRMNTKA LSLLTLLNVY QKKHLVEILS YHSCDSQTRN APEMDCLIRL
QAQNIQQRHI VFLTEKNIKM VSSYTDNGIV VATTEDFMQN FTSLVGYHNS VTEESLPPLL
GANENLESQS ALLENDEKDE EDMSLDSGDE ISHIEVFSNV HSEILAGETK GSSGTDQKKN
IQIELQSSLD VQNSLLEDKT YLIDCEASAP IDRVCSEGES SNSAEQDAYS DFQADQNQLQ
MSHQCSHFNV LTHQTFLGTP YALSSTRSQE NENYFLSAYK NSGTEKSPLS
