ID USP9X_MOUSE Reviewed; 2559 AA. AC P70398; E9QLY0; Q62497; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 27-MAR-2024, entry version 192. DE RecName: Full=Probable ubiquitin carboxyl-terminal hydrolase FAF-X; DE EC=3.4.19.12 {ECO:0000269|PubMed:29626158, ECO:0000269|PubMed:30951545}; DE AltName: Full=Deubiquitinating enzyme FAF-X; DE AltName: Full=Fat facets homolog; DE AltName: Full=Fat facets protein-related, X-linked; DE AltName: Full=Ubiquitin carboxyl-terminal hydrolase FAM; DE AltName: Full=Ubiquitin thioesterase FAF-X; DE AltName: Full=Ubiquitin-specific protease 9, X chromosome; DE AltName: Full=Ubiquitin-specific-processing protease FAF-X; GN Name=Usp9x {ECO:0000303|PubMed:24607389, ECO:0000312|MGI:MGI:894681}; GN Synonyms=Fafl, Fam; 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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=9178254; DOI=10.1016/s0925-4773(97)00672-2; RA Wood S.A., Pascoe W.S., Ru K., Yamada T., Hirchenhain J., Kemler R., RA Mattick J.S.; RT "Cloning and expression analysis of a novel mouse gene with sequence RT similarity to the Drosophila fat facets gene."; RL Mech. Dev. 63:29-38(1997). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 152-240. RC TISSUE=Cochlea; RX PubMed=9119401; DOI=10.1006/geno.1996.4526; RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P., RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D., RA Pujol R., Petit C.; RT "Cloning of the genes encoding two murine and human cochlear unconventional RT type I myosins."; RL Genomics 40:332-341(1997). RN [4] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-2540, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Mast cell; RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864; RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., RA Kawakami T., Salomon A.R.; RT "Quantitative time-resolved phosphoproteomic analysis of mast cell RT signaling."; RL J. Immunol. 179:5864-5876(2007). RN [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1600, AND IDENTIFICATION BY RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374; SER-375; SER-1600 AND RP SER-2443, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC 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 [7] RP SUBCELLULAR LOCATION, FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=24607389; DOI=10.1016/j.ajhg.2014.02.004; RA Homan C.C., Kumar R., Nguyen L.S., Haan E., Raymond F.L., Abidi F., RA Raynaud M., Schwartz C.E., Wood S.A., Gecz J., Jolly L.A.; RT "Mutations in USP9X are associated with X-linked intellectual disability RT and disrupt neuronal cell migration and growth."; RL Am. J. Hum. Genet. 94:470-478(2014). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=29626158; DOI=10.1042/bcj20180005; RA Zhang Y., Duan C., Yang J., Chen S., Liu Q., Zhou L., Huang Z., Xu Y., RA Xu G.; RT "Deubiquitinating enzyme USP9X regulates cellular clock function by RT modulating the ubiquitination and degradation of a core circadian protein RT BMAL1."; RL Biochem. J. 475:1507-1522(2018). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-1566. RX PubMed=30951545; DOI=10.1371/journal.pone.0214110; RA Abed M., Verschueren E., Budayeva H., Liu P., Kirkpatrick D.S., Reja R., RA Kummerfeld S.K., Webster J.D., Gierke S., Reichelt M., Anderson K.R., RA Newman R.J., Roose-Girma M., Modrusan Z., Pektas H., Maltepe E., Newton K., RA Dixit V.M.; RT "The Gag protein PEG10 binds to RNA and regulates trophoblast stem cell RT lineage specification."; RL PLoS ONE 14:e0214110-e0214110(2019). RN [10] RP TISSUE SPECIFICITY. RX PubMed=33378666; DOI=10.1016/j.celrep.2020.108564; RA Wrobel L., Siddiqi F.H., Hill S.M., Son S.M., Karabiyik C., Kim H., RA Rubinsztein D.C.; RT "mTORC2 Assembly Is Regulated by USP9X-Mediated Deubiquitination of RT RICTOR."; RL Cell Rep. 33:108564-108564(2020). CC -!- FUNCTION: Deubiquitinase involved both in the processing of ubiquitin CC precursors and of ubiquitinated proteins (PubMed:29626158, CC PubMed:30951545). May therefore play an important regulatory role at CC the level of protein turnover by preventing degradation of proteins CC through the removal of conjugated ubiquitin (PubMed:29626158, CC PubMed:30951545). Specifically hydrolyzes 'Lys-63'-, 'Lys-48'-, 'Lys- CC 29'- and 'Lys-33'-linked polyubiquitins chains (By similarity). CC Essential component of TGF-beta/BMP signaling cascade (By similarity). CC Specifically deubiquitinates monoubiquitinated SMAD4, opposing the CC activity of E3 ubiquitin-protein ligase TRIM33 (By similarity). CC Deubiquitinates alkylation repair enzyme ALKBH3 (By similarity). OTUD4 CC recruits USP7 and USP9X to stabilize ALKBH3, thereby promoting the CC repair of alkylated DNA lesions (By similarity). Deubiquitinates mTORC2 CC complex component RICTOR at 'Lys-294' by removing 'Lys-63'-linked CC polyubiquitin chains, stabilizing RICTOR and enhancing its binding to CC MTOR, thus promoting mTORC2 complex assembly (By similarity). Regulates CC chromosome alignment and segregation in mitosis by regulating the CC localization of BIRC5/survivin to mitotic centromeres (By similarity). CC Involved in axonal growth and neuronal cell migration CC (PubMed:24607389). Regulates cellular clock function by enhancing the CC protein stability and transcriptional activity of the core circadian CC protein BMAL1 via its deubiquitinating activity (PubMed:29626158). Acts CC as a regulator of peroxisome import by mediating deubiquitination of CC PEX5: specifically deubiquitinates PEX5 monoubiquitinated at 'Cys-11' CC following its retrotranslocation into the cytosol, resetting PEX5 for a CC subsequent import cycle (By similarity). Deubiquitinates PEG10 CC (PubMed:30951545). {ECO:0000250|UniProtKB:Q93008, CC ECO:0000269|PubMed:24607389, ECO:0000269|PubMed:29626158, CC ECO:0000269|PubMed:30951545}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:29626158, CC ECO:0000269|PubMed:30951545}; CC -!- SUBUNIT: Interacts with SMAD4, MARK4, NUAK1 and BIRC5/survivin. CC Interacts with DCX. Interacts with OTUD4 and USP7; the interaction is CC direct (By similarity). {ECO:0000250|UniProtKB:Q93008}. CC -!- INTERACTION: CC P70398; A5PKW4: PSD; Xeno; NbExp=3; IntAct=EBI-2214043, EBI-719999; CC P70398; Q13485: SMAD4; Xeno; NbExp=4; IntAct=EBI-2214043, EBI-347263; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q93008}. Cell projection, growth cone CC {ECO:0000269|PubMed:24607389}. Cytoplasm, cytoskeleton, cilium axoneme CC {ECO:0000250|UniProtKB:Q93008}. CC -!- TISSUE SPECIFICITY: Highest levels in liver and brain with expression CC also detected in heart, muscle, spleen and kidney (at protein leve) CC (PubMed:33378666). Ubiquitously expressed in adult tissues CC (PubMed:9178254). {ECO:0000269|PubMed:33378666, CC ECO:0000269|PubMed:9178254}. CC -!- DEVELOPMENTAL STAGE: At least expressed from 17 dpc to 21 postnatal CC days. {ECO:0000269|PubMed:9178254}. CC -!- DISRUPTION PHENOTYPE: Brain-specific USP9X deletion results in early CC postnatal death, whereas forebrain-specific deletion is compatible with CC survival to adulthood. In the absence of USP9X the cortical CC architecture is disorganized, and neurons display reduced neurite CC growth. {ECO:0000269|PubMed:24607389}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U67874; AAB07731.1; -; mRNA. DR EMBL; AL669967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z78153; CAB01555.1; -; mRNA. DR PIR; T30850; T30850. DR RefSeq; NP_033507.2; NM_009481.2. DR AlphaFoldDB; P70398; -. DR SMR; P70398; -. DR BioGRID; 204467; 40. DR IntAct; P70398; 16. DR MINT; P70398; -. DR STRING; 10090.ENSMUSP00000086716; -. DR MEROPS; C19.017; -. DR GlyGen; P70398; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P70398; -. DR PhosphoSitePlus; P70398; -. DR SwissPalm; P70398; -. DR EPD; P70398; -. DR jPOST; P70398; -. DR MaxQB; P70398; -. DR PaxDb; 10090-ENSMUSP00000086716; -. DR PeptideAtlas; P70398; -. DR ProteomicsDB; 300203; -. DR Pumba; P70398; -. DR DNASU; 22284; -. DR GeneID; 22284; -. DR KEGG; mmu:22284; -. DR AGR; MGI:894681; -. DR CTD; 8239; -. DR MGI; MGI:894681; Usp9x. DR eggNOG; KOG1866; Eukaryota. DR InParanoid; P70398; -. DR OrthoDB; 6206at2759; -. DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR Reactome; R-MMU-5689880; Ub-specific processing proteases. DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes. DR Reactome; R-MMU-9013420; RHOU GTPase cycle. DR Reactome; R-MMU-9013424; RHOV GTPase cycle. DR Reactome; R-MMU-9033241; Peroxisomal protein import. DR BioGRID-ORCS; 22284; 19 hits in 78 CRISPR screens. DR ChiTaRS; Usp9x; mouse. DR PRO; PR:P70398; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; P70398; Protein. DR GO; GO:0045177; C:apical part of cell; IDA:MGI. DR GO; GO:0005929; C:cilium; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0030426; C:growth cone; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0070410; F:co-SMAD binding; ISS:BHF-UCL. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB. DR GO; GO:0101005; F:deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0180017; F:K11-linked deubiquitinase activity; ISS:UniProtKB. DR GO; GO:1990380; F:K48-linked deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0061578; F:K63-linked deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB. DR GO; GO:0048675; P:axon extension; IMP:UniProtKB. DR GO; GO:0030509; P:BMP signaling pathway; ISS:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0016477; P:cell migration; IBA:GO_Central. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IMP:MGI. DR GO; GO:0021698; P:cerebellar cortex structural organization; IMP:MGI. DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW. DR GO; GO:0021766; P:hippocampus development; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IGI:MGI. DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; ISS:UniProtKB. DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB. DR GO; GO:1990138; P:neuron projection extension; IGI:MGI. DR GO; GO:1901537; P:positive regulation of DNA demethylation; ISS:UniProtKB. DR GO; GO:0032092; P:positive regulation of protein binding; ISS:UniProtKB. DR GO; GO:1904515; P:positive regulation of TORC2 signaling; ISS:UniProtKB. DR GO; GO:0009791; P:post-embryonic development; IMP:MGI. DR GO; GO:0016579; P:protein deubiquitination; IMP:UniProtKB. DR GO; GO:0071947; P:protein deubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; ISS:UniProtKB. DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB. DR GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB. DR GO; GO:0050856; P:regulation of T cell receptor signaling pathway; ISO:MGI. DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISS:UniProtKB. DR CDD; cd02659; peptidase_C19C; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR021905; DUF3517. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR001394; Peptidase_C19_UCH. DR InterPro; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR24006:SF897; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE FAF-X-RELATED; 1. DR Pfam; PF12030; DUF3517; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. PE 1: Evidence at protein level; KW Biological rhythms; Cell cycle; Cell division; Cell projection; KW Chromosome partition; Cytoplasm; Cytoskeleton; Hydrolase; Mitosis; KW Phosphoprotein; Protease; Reference proteome; Thiol protease; KW Ubl conjugation pathway. FT CHAIN 1..2559 FT /note="Probable ubiquitin carboxyl-terminal hydrolase FAF- FT X" FT /id="PRO_0000080691" FT DOMAIN 1557..1956 FT /note="USP" FT REGION 1..64 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 967..999 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1592..1633 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2475..2559 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..49 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 967..993 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2502..2516 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2523..2537 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 1566 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093, FT ECO:0000305|PubMed:30951545" FT ACT_SITE 1879 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT MOD_RES 374 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 375 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 588 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q93008" FT MOD_RES 1600 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 2443 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 2540 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:17947660" FT MOD_RES 2547 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q93008" FT MOD_RES 2551 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q93008" FT MUTAGEN 1566 FT /note="C->A: Abolished deubiquitinase activity." FT /evidence="ECO:0000269|PubMed:30951545" FT CONFLICT 73 FT /note="A -> P (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 182 FT /note="C -> F (in Ref. 3; CAB01555)" FT /evidence="ECO:0000305" FT CONFLICT 1243..1244 FT /note="QK -> HQ (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1626 FT /note="D -> N (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1631 FT /note="S -> I (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1635 FT /note="D -> N (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1638 FT /note="E -> K (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1645 FT /note="R -> K (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1665 FT /note="R -> K (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1671 FT /note="F -> S (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1688..1689 FT /note="EF -> KS (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1918 FT /note="N -> T (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" FT CONFLICT 1930 FT /note="F -> L (in Ref. 1; AAB07731)" FT /evidence="ECO:0000305" SQ SEQUENCE 2559 AA; 290711 MW; CC380E9F44B410DD CRC64; MTATTRGSPV GGNDNQGQAP DGQSQPPLQQ NQTSSPDSSN ENSPATPPDE QGQGDAPPQI EDEEPAFPHT DLAKLDDMIN RPRWVVPVLP KGELEVLLEA AIDLSKKGLD VKSEACQRFF RDGLTISFTK ILTDEAVSGW KFEIHRCIIN NTHRLVELCV AKLAQDWFPL LELLAMALNP HCKFHIYNGT RPCESVSSSV QLPEDELFAR SPDPRSPKGW LVDLLNKFGT LNGFQILHDR FINGSALNVQ IIAALIKPFG QCYEFLTLHT VKKYFLPIIE MVPQFLENLT DEELKKEAKN EAKNDALSMI IKSLKNLASR VPGQEETVKN LEIFRLKMIL RLLQISSFNG KMNALNEVNK VISSVSYYTH RHGSSEDEEW LTAERMAEWI QQNNILSIVL RDSLHQPQYV EKLEKILRFV IKEKALTLQD LDNIWAAQAG KHEAIVKNVH DLLAKLAWDF SPEQLDHLFD CFKASWTNAS KKQREKLLEL IRRLAEDDKD GVMAHKVLNL LWNLAHSDDV PVDIMDLALS AHIKILDYSC SQDRDTQKIQ WIDRFIEELR TNDKWVIPAL KQIREICSLF GEAPQNLSQS QRSPHVFYRH DLINQLQHNH ALVTLVAENL ATYMESMRMY GRDNEDYDPQ TVRLGSRYSH VQEVQERLNF LRFLLKDGQL WLCAPQAKQI WKCLAENAVY LCDREACFKW YSKLMGDEPD LDPDINKDFF ESNVLQLDPS LLTENGMKCF ERFFKAVNCR EGKLVAKRRA YMMDDLELIG LDYLWRVVIQ SNDDIACRAI DLLKEIYTNL GPRLQVNQVV IHEDFIQSCF DRLKASYDTL CVLDGDKDSI NCARQEAVRM VRVLTVLREY INECDSDYHE ERTILPMSRA FRGKHLSFIV RFPNQGRQVD DLEVWSHTND TIGSVRRCIL NRIKANVAHT KIELFVGGEL IDPGDDRKLI GQLNLKDKSL ITAKLTQISS NMPSSPDSSS DSSTGSPGNH GNHYSDGPNP EVESCLPGVI MSLHPRYISF LWQVADLGSS LNMPPLRDGA RVLMKLMPPD STTIEKLRAI CLDHAKLGES SLSPSLDSLF FGPSASQVLY LTEVVYALLM PAGAPLTDDS SDFQFHFLKS GGLPLVLSML TRNNFLPNAD METRRGAYLN ALKIAKLLLT AIGYGHVRAV AEACQPGVEG VNPMTSVNQV THDQAVVLQS ALQSIPNPSS ECMLRNVSVR LAQQISDEAS RYMPDICVIR AIQKIIWTSG CGGLQLVFSP NEEVTKIYEK TNAGNEPDLE DEQVCCEALE VMTLCFALIP TALDALSKEK AWQTFIIDLL LHCHSKTVRQ VAQEQFFLMC TRCCMGHRPL LFFITLLFTV LGSTARERAK HSGDYFTLLR HLLNYAYNSN INVPNAEVLL NNEIDWLKRI RDDVKRTGET GVEETILEGH LGVTKELLAF QTPEKKFHIG CEKGGANLIK ELIDDFIFPA SNVYLQYMRN GELPAEQAIP VCGSPATINA GFELLVALAV GCVRNLKQIV DSLTEMYYIG TAITTCEALT EWEYLPPVGP RPPKGFVGLK NAGATCYMNS VIQQLYMIPS IRNGILAIEG TGSDVDDDMS GDEKQDNESN VDPRDDVFGY PQQFEDKPPL SKTEDRKEYN IGVLRHLQVI FGHLAASRLQ YYVPRGFWKQ FRLWGEPVNL REQHDALEFF NSLVDSLDEA LKALGHPAML SKVLGGSFAD QKICQGCPHR YECEESFTTL NVDIRNHQNL LDSLEQYVKG DLLEGANAYH CEKCNKKVDT VKRLLIKKLP PVLAIQLKRF DYDWERECAI KFNDYFEFPR ELDMEPYTVA GVAKLEGDNV NPESQLIQQN EQSESEKAGS TKYRLVGVLV HSGQASGGHY YSYIIQRNGG DGEKNRWYKF DDGDVTECKM DDDEEMKNQC FGGEYMGEVF DHMMKRMSYR RQKRWWNAYI LFYERMDTIG HDDEVIRYIS EIAITTRPHQ IVMPSAIERS VRKQNVQFMH NRMQYSLEYF QFMKKLLTCN GVYLNPPPGQ DHLSPEAEEI TMISIQLAAR FLFTTGFHTK KIVRGSASDW YDALCILLRH SKNVRFWFAH NVLFNVSNRF SEYLLECPSA EVRGAFAKLI VFIAHFSLQD GPCPSPFASP GPSSQAYDNL SLSDHLLRAV LNLLRREVSE HGRHLQQYFN LFVMYANLGV AEKTQLLKLS VPATFMLVSL DEGPGPPIKY QYAELGKLYS VVSQLIRCCN VSSRMQSSIN GNPSLPNPFG DPNLSQPIMP IQQNVVDILF VRTSYVKKII EDCSNSDETV KLLRFCCWEN PQFSSTVLSE LLWQVAYSYT YELRPYLDLL LQILLIEDSW QTHRIHNALK GIPDDRDGLF DTIQRSKNHY QKRAYQCIKC MVALFSSCPV AYQILQGNGD LKRKWTWAVE WLGDELERRP YTGNPQYTYN NWSPPVQSNE TSNGYFLERS HSARMTLAKA CELCPEEEPD DQDAPDEHES PPPEDAPLYP HSPGSQYQQN NHVHGQPYTG PAAHHMNNPQ RTGQRAQENY EGGEEVSPPQ TKGSVKCTY //