TCOF_MOUSE
ID TCOF_MOUSE Reviewed; 1320 AA.
AC O08784; O08857;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Treacle protein;
DE AltName: Full=Treacher Collins syndrome protein homolog;
GN Name=Tcof1;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=9299440; DOI=10.1006/bbrc.1997.7229;
RA Paznekas W.A., Zhang N., Gridley T., Jabs E.W.;
RT "Mouse TCOF1 is expressed widely, has motifs conserved in nucleolar
RT phosphoproteins, and maps to chromosome 18.";
RL Biochem. Biophys. Res. Commun. 238:1-6(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=9158147; DOI=10.1093/hmg/6.5.727;
RA Dixon J., Hovanes K., Shiang R., Dixon M.J.;
RT "Sequence analysis, identification of evolutionary conserved motifs and
RT expression analysis of murine tcof1 provide further evidence for a
RT potential function for the gene and its human homologue, TCOF1.";
RL Hum. Mol. Genet. 6:727-737(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1314.
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169 AND THR-171, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PYROPHOSPHORYLATION.
RX PubMed=17873058; DOI=10.1073/pnas.0707338104;
RA Bhandari R., Saiardi A., Ahmadibeni Y., Snowman A.M., Resnick A.C.,
RA Kristiansen T.Z., Molina H., Pandey A., Werner J.K. Jr., Juluri K.R.,
RA Xu Y., Prestwich G.D., Parang K., Snyder S.H.;
RT "Protein pyrophosphorylation by inositol pyrophosphates is a
RT posttranslational event.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:15305-15310(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1191, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; THR-171; SER-593 AND
RP SER-1216, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-154; SER-169;
RP THR-171; THR-324; SER-413; SER-414; SER-590; SER-593; THR-860; THR-1066;
RP SER-1191; SER-1216; SER-1301 AND SER-1303, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132; LYS-318; LYS-327; LYS-626;
RP LYS-630; LYS-922 AND LYS-976, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Nucleolar protein that acts as a regulator of RNA polymerase
CC I by connecting RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification. Required for neural crest specification:
CC following monoubiquitination by the BCR(KBTBD8) complex, associates
CC with NOLC1 and acts as a platform to connect RNA polymerase I with
CC enzymes responsible for ribosomal processing and modification, leading
CC to remodel the translational program of differentiating cells in favor
CC of neural crest specification. {ECO:0000250|UniProtKB:Q13428}.
CC -!- SUBUNIT: Heterodimer; heterodimerizes with NOLC1 following
CC monoubiquitination. Part of a large pre-ribosomal ribonucleoprotein
CC (RNP) complex, that consists of at least 62 ribosomal proteins, 45
CC nonribosomal proteins and both pre-rRNA and mature rRNA species. Within
CC this complex directly interacts with NOP56 in an RNA-independent
CC manner. {ECO:0000250|UniProtKB:Q13428}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q13428}.
CC -!- TISSUE SPECIFICITY: Ubiquitous in adult and embryonic tissues.
CC {ECO:0000269|PubMed:9299440}.
CC -!- DEVELOPMENTAL STAGE: Expression elevated at 11 dpc when the branchial
CC arches and facial swellings are present. {ECO:0000269|PubMed:9158147}.
CC -!- PTM: Pyrophosphorylated by 5-diphosphoinositol pentakisphosphate (5-
CC IP7) (PubMed:17873058). Serine pyrophosphorylation is achieved by
CC Mg(2+)-dependent, but enzyme independent transfer of a beta-phosphate
CC from a inositol pyrophosphate to a pre-phosphorylated serine residue
CC (PubMed:17873058). {ECO:0000269|PubMed:17873058}.
CC -!- PTM: Ubiquitinated. Monoubiquitination by the BCR(KBTBD8) complex
CC promotes the formation of a NOLC1-TCOF1 complex that acts as a platform
CC to connect RNA polymerase I with enzymes responsible for ribosomal
CC processing and modification, leading to remodel the translational
CC program of differentiating cells in favor of neural crest
CC specification. {ECO:0000250|UniProtKB:Q13428}.
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DR EMBL; AF001794; AAB71347.1; -; mRNA.
DR EMBL; U81030; AAB60933.1; -; mRNA.
DR EMBL; BC060105; AAH60105.1; -; mRNA.
DR CCDS; CCDS37836.1; -.
DR PIR; JC5630; JC5630.
DR RefSeq; NP_035682.1; NM_011552.3.
DR AlphaFoldDB; O08784; -.
DR SMR; O08784; -.
DR BioGRID; 204043; 8.
DR IntAct; O08784; 2.
DR STRING; 10090.ENSMUSP00000135476; -.
DR iPTMnet; O08784; -.
DR PhosphoSitePlus; O08784; -.
DR SwissPalm; O08784; -.
DR EPD; O08784; -.
DR jPOST; O08784; -.
DR MaxQB; O08784; -.
DR PaxDb; O08784; -.
DR PeptideAtlas; O08784; -.
DR PRIDE; O08784; -.
DR ProteomicsDB; 263149; -.
DR Antibodypedia; 27956; 199 antibodies from 30 providers.
DR DNASU; 21453; -.
DR Ensembl; ENSMUST00000176630; ENSMUSP00000135476; ENSMUSG00000024613.
DR GeneID; 21453; -.
DR KEGG; mmu:21453; -.
DR UCSC; uc008fbb.2; mouse.
DR CTD; 6949; -.
DR MGI; MGI:892003; Tcof1.
DR VEuPathDB; HostDB:ENSMUSG00000024613; -.
DR eggNOG; ENOG502S41N; Eukaryota.
DR GeneTree; ENSGT00730000111382; -.
DR HOGENOM; CLU_263315_0_0_1; -.
DR InParanoid; O08784; -.
DR PhylomeDB; O08784; -.
DR TreeFam; TF341730; -.
DR BioGRID-ORCS; 21453; 26 hits in 74 CRISPR screens.
DR ChiTaRS; Tcof1; mouse.
DR PRO; PR:O08784; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O08784; protein.
DR Bgee; ENSMUSG00000024613; Expressed in embryonic post-anal tail and 263 other tissues.
DR ExpressionAtlas; O08784; baseline and differential.
DR Genevisible; O08784; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISO:MGI.
DR GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
DR GO; GO:0014032; P:neural crest cell development; ISS:UniProtKB.
DR GO; GO:0014029; P:neural crest formation; ISS:UniProtKB.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IMP:MGI.
DR GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
DR InterPro; IPR006594; LisH.
DR InterPro; IPR017859; Treacle.
DR InterPro; IPR003993; Treacle_dom.
DR PANTHER; PTHR20787; PTHR20787; 1.
DR Pfam; PF03546; Treacle; 2.
DR SMART; SM00667; LisH; 1.
DR PROSITE; PS50896; LISH; 1.
PE 1: Evidence at protein level;
KW Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..1320
FT /note="Treacle protein"
FT /id="PRO_0000072460"
FT DOMAIN 6..38
FT /note="LisH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00126"
FT REPEAT 212..295
FT /note="1"
FT REPEAT 296..366
FT /note="2"
FT REPEAT 367..436
FT /note="3"
FT REPEAT 437..505
FT /note="4"
FT REPEAT 506..550
FT /note="5"
FT REPEAT 551..624
FT /note="6"
FT REPEAT 625..680
FT /note="7"
FT REPEAT 681..714
FT /note="8"
FT REPEAT 715..774
FT /note="9"
FT REPEAT 775..839
FT /note="10"
FT REGION 57..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..839
FT /note="10 X approximate tandem repeats"
FT REGION 1175..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..75
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 805..820
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 831..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..926
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1036..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1106..1138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1175..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1305..1320
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 104
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 153
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 301
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 324
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 521
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 630
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 655
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 765
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 853
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 869
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 922
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 976
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 1066
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1242
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 1249
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 521
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 635
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 655
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 1082
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 1092
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CROSSLNK 1249
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13428"
FT CONFLICT 35
FT /note="G -> A (in Ref. 2; AAB60933)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..142
FT /note="Missing (in Ref. 2; AAB60933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1320 AA; 135001 MW; 34D87F5F5D300758 CRC64;
MAEARKRREL LPLIYHHLLQ AGYVRAAREV KEQSGQKSFL TQPVTLLDIY THWQQTSELG
QKQKAEDDET LQAKKSRVSD PVSSSESSDQ EKEEEAATER AKATPRPTPV NSATAALPSK
VKEKGKTKTA NKTVNSVSHP GSGKTVVHLL SGKSPKKSAE PLANTVLASE TEEEGNAQAL
GPTAKSGTVS AGQGSSSSED SSISSDETDV EVKSPAKPAQ AKASAAPAKD PPARTAPGPT
KLGNVAPTPA KPARAAAAAA AAAVAAAAAA AAEESESSEE DSDSEDEAPA GLPSQVKASG
KGPHVRADSV SAKGISGKGP ILATPGKTGP AATQAKAERP EKDSETSSED DSDSEDEMPV
TVNTPQARTS GKSPRARGTS APAKESSQKG APAVTPGKAR PVAAQAGKPE AKSSEESESD
SGETPAAATL TTSPAKVKPL GKSSQVRPVS TVTPGSSGKG ANLPCPGKVG SAALRVQMVK
KEDVSESSSA ELDSDGPGSP AKAKASLALP QKVRPVATQV KTDRGKGHSG SSEESSDSEE
EAAPAASAAQ AKPALEKQMK ASSRKGTPAS ATGASTSSHC KAGAVTSSAS LSSPALAKGT
QRSDVDSSSE SESEGAAPST PRVQGKSGGK GLQGKAALGQ GVAPVHTQKT GPSVKAMAQE
DSESLEEDSS SEEEDETPAQ ATPLGRLPQA KANPPPTKTP PASASGKAVA APTKGKPPVP
NSTVSARGQR SVPAAGKAGA PATQAQKGPV AGTGEDSESS SKEESDSEEE TPAQIKPVGK
TSQVRAASAP AKESPKKGAH PGTPGKTGSS ATQAQPGKTE DSDSSSEESD SDTEMPSAQA
IKSPPVSVNR NSSPAVPAPT PEGVQAVNTT KKASGTTAQS SSSESEDGDE DLIPATQPST
YALRTSVTTP AALSRAASQP SKSEQSSRMP KGKKAKAAAS AQTSSAVETL PMMPPQSAPI
QPKATNKLGK SKLPEKQQLA PGYPKAPRSS EDSSDTSSED EEDAKRPQMP KSAHRLDPDP
SQKETVVEET PTESSEDEMV APSQSLLSGY MTPGLTVANS QASKATPRPD SNSLASSAPA
TKDNPDGKQK SKSQHAADTA LPKTGRKEAS SGSTPQKPKK LKKSTSSSPA PTQTLPNSIT
QRLLEQAWPL SEAQVQASVV KVLTELLEQE RLKATEAIKE SGKKSQKRKL SGDLEAGAPK
NKKKKEQPVP RASAVSPEKA PMTSKAKSKL DKGSAGGKGK GSPGPQGAKE KPDGELLGIK
LESGEQSDPK SKSKKKKSLK KKKDKEKKEK KKGKKSLAKD SASPIQKKKK KKKKSAEPAV
