MBB1A_MOUSE
ID MBB1A_MOUSE Reviewed; 1344 AA.
AC Q7TPV4; O35851; Q80Y66; Q8R4X2; Q99KP0;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Myb-binding protein 1A;
DE AltName: Full=Myb-binding protein of 160 kDa;
GN Name=Mybbp1a; Synonyms=P160;
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], PROTEIN SEQUENCE OF 43-53; 205-211; 286-290;
RP 458-465 AND 488-496, FUNCTION, INTERACTION WITH JUN AND MYB, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9447996; DOI=10.1128/mcb.18.2.989;
RA Tavner F.J., Simpson R., Tashiro S., Favier D., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Macmillan E.M., Lutwyche J., Keough R.A., Ishii S.,
RA Gonda T.J.;
RT "Molecular cloning reveals that the p160 Myb-binding protein is a novel,
RT predominantly nucleolar protein which may play a role in transactivation by
RT Myb.";
RL Mol. Cell. Biol. 18:989-1002(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Keough R.A., Gonda T.J.;
RT "Structural organization of the murine myb-binding protein p160 (Mybbp1a)
RT gene.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C3H/He; TISSUE=Eye, Mammary gland, and Osteoblast;
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 PARTIAL PROTEIN SEQUENCE, FUNCTION, AND INTERACTION WITH AHR.
RX PubMed=11956195; DOI=10.1074/jbc.m200740200;
RA Jones L.C., Okino S.T., Gonda T.J., Whitlock J.P. Jr.;
RT "Myb-binding protein 1a augments AhR-dependent gene expression.";
RL J. Biol. Chem. 277:22515-22519(2002).
RN [6]
RP SUBCELLULAR LOCATION, INTERACTION WITH KPNA2, MUTAGENESIS OF LEU-249;
RP VAL-251; LEU-272 AND LEU-274, AND DOMAINS NES AND NLS.
RX PubMed=12941609; DOI=10.1016/s0014-4827(03)00262-3;
RA Keough R.A., Macmillan E.M., Lutwyche J.K., Gardner J.M., Tavner F.J.,
RA Jans D.A., Henderson B.R., Gonda T.J.;
RT "Myb-binding protein 1a is a nucleocytoplasmic shuttling protein that
RT utilizes CRM1-dependent and independent nuclear export pathways.";
RL Exp. Cell Res. 289:108-123(2003).
RN [7]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH
RP PPARGC1A.
RX PubMed=14744933; DOI=10.1101/gad.1152204;
RA Fan M., Rhee J., St Pierre J., Handschin C., Puigserver P., Lin J.,
RA Jaeger S., Erdjument-Bromage H., Tempst P., Spiegelman B.M.;
RT "Suppression of mitochondrial respiration through recruitment of p160 myb
RT binding protein to PGC-1alpha: modulation by p38 MAPK.";
RL Genes Dev. 18:278-289(2004).
RN [8]
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1277 AND SER-1280, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1253 AND SER-1280, AND
RP IDENTIFICATION BY 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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-1253, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], 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 [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLOCK AND CRY1.
RX PubMed=19129230; DOI=10.1093/nar/gkn1013;
RA Hara Y., Onishi Y., Oishi K., Miyazaki K., Fukamizu A., Ishida N.;
RT "Molecular characterization of Mybbp1a as a co-repressor on the Period2
RT promoter.";
RL Nucleic Acids Res. 37:1115-1126(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1164; SER-1244; SER-1253;
RP THR-1256; THR-1277; SER-1280; SER-1323 AND SER-1325, AND IDENTIFICATION BY
RP MASS 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 [15]
RP CITRULLINATION AT ARG-1322.
RX PubMed=24463520; DOI=10.1038/nature12942;
RA Christophorou M.A., Castelo-Branco G., Halley-Stott R.P., Oliveira C.S.,
RA Loos R., Radzisheuskaya A., Mowen K.A., Bertone P., Silva J.C.,
RA Zernicka-Goetz M., Nielsen M.L., Gurdon J.B., Kouzarides T.;
RT "Citrullination regulates pluripotency and histone H1 binding to
RT chromatin.";
RL Nature 507:104-108(2014).
CC -!- FUNCTION: May activate or repress transcription via interactions with
CC sequence specific DNA-binding proteins (PubMed:9447996,
CC PubMed:11956195, PubMed:14744933). Repression may be mediated at least
CC in part by histone deacetylase activity (HDAC activity)
CC (PubMed:14744933). Acts as a corepressor and in concert with CRY1,
CC represses the transcription of the core circadian clock component PER2
CC (PubMed:19129230). Preferentially binds to dimethylated histone H3
CC 'Lys-9' (H3K9me2) on the PER2 promoter (PubMed:19129230). Has a role in
CC rRNA biogenesis together with PWP1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BQG0, ECO:0000269|PubMed:11956195,
CC ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230,
CC ECO:0000269|PubMed:9447996}.
CC -!- SUBUNIT: Component of the B-WICH complex, at least composed of
CC SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21
CC (By similarity). Binds to and represses JUN and MYB via the leucine
CC zipper regions present in these proteins. Also binds to and represses
CC PPARGC1A: this interaction is abrogated when PPARGC1A is phosphorylated
CC by MAPK1/ERK. Binds to and stimulates transcription by AHR. Binds to
CC KPNA2. Interacts with CLOCK and CRY1. {ECO:0000250|UniProtKB:Q9BQG0,
CC ECO:0000269|PubMed:11956195, ECO:0000269|PubMed:12941609,
CC ECO:0000269|PubMed:14744933, ECO:0000269|PubMed:19129230,
CC ECO:0000269|PubMed:9447996}.
CC -!- INTERACTION:
CC Q7TPV4; P12813: Nr4a1; NbExp=3; IntAct=EBI-1373622, EBI-10896863;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12941609}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:12941609, ECO:0000269|PubMed:19129230}.
CC Cytoplasm {ECO:0000269|PubMed:12941609}. Note=Predominantly nucleolar.
CC Also shuttles between the nucleus and cytoplasm. Nuclear import may be
CC mediated by KPNA2, while export appears to depend partially on
CC XPO1/CRM1. {ECO:0000269|PubMed:12941609}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:9447996}.
CC -!- PTM: Citrullinated by PADI4. {ECO:0000269|PubMed:24463520}.
CC -!- SIMILARITY: Belongs to the MYBBP1A family. {ECO:0000305}.
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DR EMBL; U63648; AAC39954.1; -; mRNA.
DR EMBL; AF345640; AAL83748.1; -; Genomic_DNA.
DR EMBL; AL662812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004078; AAH04078.1; -; mRNA.
DR EMBL; BC048858; AAH48858.1; -; mRNA.
DR EMBL; BC052889; AAH52889.1; -; mRNA.
DR CCDS; CCDS24986.1; -.
DR PIR; T34188; T34188.
DR RefSeq; NP_058056.2; NM_016776.2.
DR AlphaFoldDB; Q7TPV4; -.
DR BioGRID; 201999; 43.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR CORUM; Q7TPV4; -.
DR DIP; DIP-39831N; -.
DR IntAct; Q7TPV4; 18.
DR MINT; Q7TPV4; -.
DR STRING; 10090.ENSMUSP00000044827; -.
DR iPTMnet; Q7TPV4; -.
DR PhosphoSitePlus; Q7TPV4; -.
DR SwissPalm; Q7TPV4; -.
DR EPD; Q7TPV4; -.
DR jPOST; Q7TPV4; -.
DR MaxQB; Q7TPV4; -.
DR PaxDb; Q7TPV4; -.
DR PRIDE; Q7TPV4; -.
DR ProteomicsDB; 287318; -.
DR Antibodypedia; 23280; 271 antibodies from 31 providers.
DR DNASU; 18432; -.
DR Ensembl; ENSMUST00000045633; ENSMUSP00000044827; ENSMUSG00000040463.
DR GeneID; 18432; -.
DR KEGG; mmu:18432; -.
DR UCSC; uc007jyy.1; mouse.
DR CTD; 10514; -.
DR MGI; MGI:106181; Mybbp1a.
DR VEuPathDB; HostDB:ENSMUSG00000040463; -.
DR eggNOG; KOG1926; Eukaryota.
DR GeneTree; ENSGT00390000017457; -.
DR HOGENOM; CLU_005997_1_0_1; -.
DR InParanoid; Q7TPV4; -.
DR OMA; PWVEVMV; -.
DR OrthoDB; 86051at2759; -.
DR PhylomeDB; Q7TPV4; -.
DR TreeFam; TF317401; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR BioGRID-ORCS; 18432; 30 hits in 77 CRISPR screens.
DR ChiTaRS; Mybbp1a; mouse.
DR PRO; PR:Q7TPV4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q7TPV4; protein.
DR Bgee; ENSMUSG00000040463; Expressed in embryonic post-anal tail and 273 other tissues.
DR ExpressionAtlas; Q7TPV4; baseline and differential.
DR Genevisible; Q7TPV4; MM.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IPI:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0032922; P:circadian regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:2000210; P:positive regulation of anoikis; ISO:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:1903450; P:regulation of G1 to G0 transition; ISO:MGI.
DR GO; GO:0022904; P:respiratory electron transport chain; IDA:MGI.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007015; DNA_pol_V/MYBBP1A.
DR PANTHER; PTHR13213; PTHR13213; 1.
DR Pfam; PF04931; DNA_pol_phi; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Biological rhythms; Citrullination; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Ribosome biogenesis; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19131326"
FT CHAIN 2..1344
FT /note="Myb-binding protein 1A"
FT /id="PRO_0000096256"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..580
FT /note="Interaction with MYB"
FT /evidence="ECO:0000269|PubMed:9447996"
FT REGION 710..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1152..1344
FT /note="Required for nuclear and nucleolar localization"
FT /evidence="ECO:0000269|PubMed:12941609"
FT MOTIF 238..256
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000269|PubMed:12941609"
FT MOTIF 261..279
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000269|PubMed:12941609"
FT COMPBIAS 724..748
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1283..1299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 69
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 156
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1187
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1191
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1251
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1256
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MOD_RES 1322
FT /note="Citrulline"
FT /evidence="ECO:0000269|PubMed:24463520"
FT MOD_RES 1323
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT CROSSLNK 1149
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9BQG0"
FT MUTAGEN 249
FT /note="L->A: Reduced nuclear export; when associated with
FT A-251."
FT /evidence="ECO:0000269|PubMed:12941609"
FT MUTAGEN 251
FT /note="V->A: Reduced nuclear export; when associated with
FT A-249."
FT /evidence="ECO:0000269|PubMed:12941609"
FT MUTAGEN 272
FT /note="L->A: Reduced nuclear export; when associated with
FT A-274."
FT /evidence="ECO:0000269|PubMed:12941609"
FT MUTAGEN 274
FT /note="L->A: Reduced nuclear export; when associated with
FT A-272."
FT /evidence="ECO:0000269|PubMed:12941609"
FT CONFLICT 87
FT /note="R -> T (in Ref. 1; AAC39954 and 2; AAL83748)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="P -> A (in Ref. 1; AAC39954)"
FT /evidence="ECO:0000305"
FT CONFLICT 505..508
FT /note="DRNR -> HASG (in Ref. 4; AAH04078)"
FT /evidence="ECO:0000305"
FT CONFLICT 1282
FT /note="I -> V (in Ref. 4; AAH52889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1344 AA; 152037 MW; 64D3420981CD0767 CRC64;
MAEMKSPTKA EPATPAEAAQ SDRHSLLEHS REFLDFFWDI AKPDQETRLR ATEKLLEYLR
TRPNDSEMKY ALKRLITGLG VGREAARPCY SLALAQLLQS FEDIPLCDIL DQIQEKYSLQ
AMNKAMMRPS LFANLFGVLA LFQSGRLVKD KEALMKSVQL LKILSQHPNH LQGQPIKALV
DILSEVPESM FQEILPKVLK GNMKVILRSP KYLELFLLAK QRVPTKLESL MGSVDLFSED
NIPSLVNILK VAANSVKKEH KLPNVALDLL RLALKESRFE LFWKKVLEEG LLKNPSWTSS
YMCFRLLGAS LPLLSEEQLQ LVMRGDLIRH FGENMVISKP QNLFKIIPEI STYVGTFLEG
CQDDPKRQLT MMVAFTTITN QGLPVMPTFW RVTRFLNAEA LQSYVAWLRD MFLQPDLNSL
VDFSTANQKR AQDASLNVPE RAVFRLRKWI IHRLVSLVDH LHLEKDEAVV EQIARFCLFH
AFFKTKKATP QIPETKQHFS FPLDDRNRGV FVSAFFSLLQ TLSVKFRQTP DLAENGKPWT
YRLVQLADML LNHNRNVTSV TSLTTQQRQA WDQMMSTLKE LEARSSETRA IAFQHLLLLV
GLHIFKSPAE SCDVLGDIQT CIKKSMEQNP RRSRSRAKAS QEPVWVEVMV EILLSLLAQP
SNLMRQVVRS VFGHICPHLT PRCLQLILAV LSPVTNEDED DNVVVTDDAD EKQLQHGEDE
DSDNEDNKNS ESDMDSEDGE ESEEEDRDKD VDPGFRQQLM EVLKAGNALG GVDNEEEEEL
GDEAMMALDQ NLASLFKEQK MRIQARNEEK NKLQKEKKLR RDFQIRALDL IEVLVTKQPE
HPLILELLEP LLNVIQHSMR SKGSTKQEQD LLHKTARIFM HHLCRARRYC HEVGPCAEAL
HAQVERLVQQ AGSQADASVA LYYFNASLYL LRVLKGNTNK RHQDGHKLHG ADTEDSEDQA
ANCLDLDFVT RVYSASLESL LTKRNSSLTV PMFLSLFSRY PVICKNLLPV LAQHVAGPSR
PRHQAQACLM LQKTLSAREL RVCFEDPEWE QLITQLLGKA TQTLQTLGEA QSKGEHQKEL
SILELLNTLL RTVNHEKLSV DLTAPLGVLQ SKQQKLQQSL QQGNHSSGSN RLYDLYWQAM
RMLGVQRPKS EKKNAKDIPS DTQSPVSTKR KKKGFLPETK KRKKLKSEGT TPEKNAASQQ
DAVTEGAMPA ATGKDQPPST GKKKRKRVKA STPSQVNGIT GAKSPAPSNP TLSPSTPAKT
PKLQKKKEKL SQVNGATPVS PIEPESKKHH QEALSTKEVI RKSPHPQSAL PKKRARLSLV
SRSPSLLQSG VKKRRVASRR VQTP
