UBPE_DROME
ID UBPE_DROME Reviewed; 1556 AA.
AC Q24574; A4V1I7; Q95TM9; Q9VRP1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 47 {ECO:0000250|UniProtKB:Q96K76};
DE EC=3.4.19.12 {ECO:0000269|PubMed:10949024, ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834};
DE AltName: Full=Ubiquitin thioesterase 47 {ECO:0000250|UniProtKB:Q96K76};
DE AltName: Full=Ubiquitin-specific-processing protease 47 {ECO:0000303|PubMed:27552662};
GN Name=Usp47 {ECO:0000303|PubMed:27552662, ECO:0000312|FlyBase:FBgn0016756};
GN Synonyms=Ubp64E {ECO:0000303|PubMed:26169834};
GN ORFNames=CG5486 {ECO:0000312|FlyBase:FBgn0016756};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 318-1556 (ISOFORMS A/D), AND FUNCTION.
RC TISSUE=Embryo;
RX PubMed=8816485; DOI=10.1128/mcb.16.10.5717;
RA Henchoz S., de Rubertis F., Pauli D., Spierer P.;
RT "The dose of a putative ubiquitin-specific protease affects position-effect
RT variegation in Drosophila melanogaster.";
RL Mol. Cell. Biol. 16:5717-5725(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-1556 (ISOFORMS A/D).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-405.
RX PubMed=10949024; DOI=10.1016/s1097-2765(05)00008-0;
RA Roerth P., Szabo K., Texido G.;
RT "The level of C/EBP protein is critical for cell migration during
RT Drosophila oogenesis and is tightly controlled by regulated degradation.";
RL Mol. Cell 6:23-30(2000).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-173; SER-238;
RP SER-1131; SER-1132; SER-1140; SER-1141; SER-1199; SER-1201 AND SER-1205,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TTK, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=18160715; DOI=10.1128/mcb.01567-07;
RA Bajpe P.K., van der Knaap J.A., Demmers J.A., Bezstarosti K., Bassett A.,
RA van Beusekom H.M., Travers A.A., Verrijzer C.P.;
RT "Deubiquitylating enzyme UBP64 controls cell fate through stabilization of
RT the transcriptional repressor tramtrack.";
RL Mol. Cell. Biol. 28:1606-1615(2008).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP MUTAGENESIS OF CYS-405.
RX PubMed=26169834; DOI=10.1128/mcb.00373-15;
RA Shi J., Liu Y., Xu X., Zhang W., Yu T., Jia J., Liu C.;
RT "Deubiquitinase USP47/UBP64E regulates beta-Catenin ubiquitination and
RT degradation and plays a positive role in wnt signaling.";
RL Mol. Cell. Biol. 35:3301-3311(2015).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27552662; DOI=10.1371/journal.pbio.1002539;
RA Ashton-Beaucage D., Lemieux C., Udell C.M., Sahmi M., Rochette S.,
RA Therrien M.;
RT "The Deubiquitinase USP47 Stabilizes MAPK by Counteracting the Function of
RT the N-end Rule ligase POE/UBR4 in Drosophila.";
RL PLoS Biol. 14:E1002539-E1002539(2016).
CC -!- FUNCTION: Ubiquitin-specific protease that deubiquitinates target
CC proteins to regulate different cellular and developmental pathways
CC (PubMed:10949024, PubMed:18160715, PubMed:26169834, PubMed:27552662).
CC Functions downstream of Dsor1/MEK to positively regulate the Ras/MAPK
CC signaling pathway (PubMed:27552662). Likely to modulate the pathway
CC during various cellular and developmental processes including rl/MAPK
CC activation by the receptors InR, Egfr and sevenless/sev
CC (PubMed:27552662). Functions in the post-translational stabilization of
CC rl/MAPK levels in a mechanism that is independent of rl activity and
CC opposes the activity of the E2 enzyme Unc6 and the putative E3 ligases
CC poe, Ufd4 and Kcmf1, which mediate the ubiquitination and proteasomal
CC degradation of rl (PubMed:27552662). During eye development it may also
CC act downstream of rl/MAPK to negatively regulate the Ras/MAPK signaling
CC pathway by stabilizing the transcriptional repressor ttk and
CC consequently inhibiting photoreceptor cell development
CC (PubMed:18160715). This suggests that at least during eye development,
CC it may act in both the positive and negative regulation of the Ras/MAPK
CC signaling pathway to mediate the development of different cell types
CC (PubMed:18160715, PubMed:27552662). Positively regulates border
CC follicle cell migration during oogenesis by mediating the
CC deubiquitination and stabilization of slbo (PubMed:10949024). In the
CC wing disks it positively regulates wg signaling by stabilizing arm
CC (PubMed:26169834). Has an effect on position-effect variegation
CC (PubMed:8816485). {ECO:0000269|PubMed:10949024,
CC ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834,
CC ECO:0000269|PubMed:27552662, ECO:0000269|PubMed:8816485}.
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:10949024,
CC ECO:0000269|PubMed:18160715, ECO:0000269|PubMed:26169834};
CC -!- SUBUNIT: Interacts with ttk. {ECO:0000269|PubMed:18160715}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000312|FlyBase:FBgn0016756}; Synonyms=B
CC {ECO:0000312|FlyBase:FBgn0016756};
CC IsoId=Q24574-1; Sequence=Displayed;
CC Name=D {ECO:0000312|FlyBase:FBgn0016756};
CC IsoId=Q24574-2; Sequence=VSP_054033;
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in the embryo (at protein
CC level). Ubiquitously expressed in the developing eye (at protein
CC level). {ECO:0000269|PubMed:18160715}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown in the adult wing results
CC in the development of wing margin bristles (PubMed:26169834). RNAi-
CC mediated knockdown in the posterior compartment of the wing reduces
CC accumulation of arm, resulting in reduced expression of sens and wg
CC (PubMed:26169834). RNAi-mediated knockdown in larval wing or eye
CC imaginal disks results in decreased rl protein levels
CC (PubMed:27552662). {ECO:0000269|PubMed:26169834,
CC ECO:0000269|PubMed:27552662}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13901.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67601.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA67601.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014296; AAF50752.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN12105.1; -; Genomic_DNA.
DR EMBL; AE014296; AAS65076.2; -; Genomic_DNA.
DR EMBL; BT003784; AAO41467.1; -; mRNA.
DR EMBL; X99211; CAA67601.1; ALT_SEQ; mRNA.
DR EMBL; AY058672; AAL13901.1; ALT_INIT; mRNA.
DR RefSeq; NP_523937.2; NM_079213.4. [Q24574-1]
DR RefSeq; NP_729087.1; NM_168129.4. [Q24574-1]
DR RefSeq; NP_996001.2; NM_206279.4. [Q24574-2]
DR AlphaFoldDB; Q24574; -.
DR SMR; Q24574; -.
DR BioGRID; 64105; 12.
DR IntAct; Q24574; 4.
DR STRING; 7227.FBpp0076802; -.
DR MEROPS; C19.105; -.
DR iPTMnet; Q24574; -.
DR PaxDb; Q24574; -.
DR PRIDE; Q24574; -.
DR EnsemblMetazoa; FBtr0077095; FBpp0076802; FBgn0016756. [Q24574-1]
DR EnsemblMetazoa; FBtr0077096; FBpp0076803; FBgn0016756. [Q24574-1]
DR EnsemblMetazoa; FBtr0306259; FBpp0297369; FBgn0016756. [Q24574-2]
DR GeneID; 38644; -.
DR KEGG; dme:Dmel_CG5486; -.
DR CTD; 55031; -.
DR FlyBase; FBgn0016756; Usp47.
DR VEuPathDB; VectorBase:FBgn0016756; -.
DR eggNOG; KOG4598; Eukaryota.
DR GeneTree; ENSGT00940000157223; -.
DR HOGENOM; CLU_002928_0_0_1; -.
DR InParanoid; Q24574; -.
DR OMA; DCDWRRY; -.
DR PhylomeDB; Q24574; -.
DR BioGRID-ORCS; 38644; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Usp47; fly.
DR GenomeRNAi; 38644; -.
DR PRO; PR:Q24574; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0016756; Expressed in thoracico-abdominal ganglion (Drosophila) and 31 other tissues.
DR Genevisible; Q24574; DM.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0042675; P:compound eye cone cell differentiation; IMP:FlyBase.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:FlyBase.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:FlyBase.
DR GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IDA:FlyBase.
DR GO; GO:0050821; P:protein stabilization; IGI:FlyBase.
DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR045578; USP47_C.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF19718; USP47_C; 1.
DR SUPFAM; SSF54001; SSF54001; 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 Alternative splicing; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..1556
FT /note="Ubiquitin carboxyl-terminal hydrolase 47"
FT /id="PRO_0000080687"
FT DOMAIN 396..779
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 117..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1087..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 405
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093,
FT ECO:0000305|PubMed:10949024, ECO:0000305|PubMed:26169834"
FT ACT_SITE 720
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1131
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1132
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1140
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1141
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1199
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1201
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1205
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 272..289
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_054033"
FT MUTAGEN 405
FT /note="C->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10949024"
FT MUTAGEN 405
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:26169834"
FT CONFLICT 437..439
FT /note="NIP -> KS (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="D -> A (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="E -> G (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
FT CONFLICT 525..526
FT /note="TR -> NDC (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="D -> DS (in Ref. 5; AAL13901)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="A -> R (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
FT CONFLICT 910
FT /note="Missing (in Ref. 4; CAA67601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1556 AA; 173794 MW; F70AE5BB2914E8BE CRC64;
MTDKESEQCT VSVFDQTPGS EQKKINVVVR SHFTVKRVID LIGTQFSYEK FELLLQPHDN
KDLVNLNALE SQLMYEVAGF EPQLKNHLIL LPSGSWDGDV TKRFELPIKR VVVKKVMKSD
GEKAKSPATG EKKKRVVGEK TKKKPASGSS SPSKAKTTSE DSLAKTSISS ESSPEKTSKI
KTTAAKISKP GSEKAPRASP EECPELSTEI NSKNTSSESP VAKKTAKVTS KPTLELLSPI
KPSSPIKELD CEPVDTLSKQ QLSEQLQLYP QGRNLISPVD DAPSDLFISD AEQLSDDDLA
LGASASPTML GPGYDYGAPT GDSDVEGVTG VTDPSTIGTD DGTYPALSNF YRRKYGGDEL
RAWQRVNTTG ADFVSSATTE TEAEARQASL GPRGYVGLVN QAMTCYLNSL LQALFMTPEF
RNALYRWEFD NDNEAKNIPY QLQKLFLNLQ TSPKAAVETT DLTRSFGWDS TEAWQQHDIQ
ELCRVMFDAL EHKFKNTKQA NLISNLYEGK MNDYVKCLEC NTEKTREDTF LDIPLPVRPF
GSSSAYGSIE EALRAFVQPE TLDGNNQYLC EKCKKKCDAH KGLHFKSFPY ILTLHLKRFD
FDYQTMHRIK LNDRVTFPQT LNLNTFINRS GNSGEQNSQL NGTVDDCSTA DSGSAMEDDN
LSSGVVTTAS SSQHENDLND EDEGIDMSSS TSKSAKQGSG PYLYELFAIM IHSGSASGGH
YYAYIKDFDN NEWFCFNDQN VTSITQEDIQ RSFGGPNGSY YSSAYTSSTN AYMLMYRQVD
AKRNELVAKV ADFPEHIKTL LPKLHSEEET RVSRLGRHIT VTDLALPDLY KPRVYFYNPS
LKKMKITRVY VSQSFNINLV LMSAYEMLNV EQFAPLSRCR LVAYNSSMDT IIQSLESCTD
PALTELRAAQ NYSLDFLLEY RAEDQEFEVY PPNGITWYVF KVDLSTMAMD GPFLVYSAAR
EREASDVLRR SIALRLHISE QQFLLATVRA TVPKAFVSYD PHPTPEALQH LQNMANTQFK
SITYFYLNVP NTDAATLEML GVPTVESVEC ASGGDVVDAA MMNGVAPGHM SSSNDYDWRR
YKRDLVEPMS QPSPSHGHES NSEDSSLSDG DRTLVETDNM AHRGGGDSQV SSTSHSPQLS
SPEDEAASHD AMMRVHAYCN GNGSYAAADV VDPLLLPTST NHFFYATKVE CVDVVGTGSS
SGHQSDEEAQ LRKPTRAYKL LVGTHMRMGA FKKHIEQLIQ VPAAHFKLQR KHDNNLSNNQ
NNSLVHLIEG ETLTVELGKT LEPDEFKAKI HFLRLADIDN ETSKLPCVCE WVYNANTTAE
QAKKELVAKL HRIDAKYATL SVQNCRIWLK GGRIPIKILS DDETLYCDMR SSIAAEFIVQ
ECEEEVDPQP KDDSLTLFVR RWCPAKLEFG KFQEITLDQD SEIRLSLSQI SDIPIDKLSY
MKLNSNFPCT SISALSVNES SSWYSVPTTL DKYPLNSTQT GNIYLYKDRT VPARELTLEE
RRLMNAREKA RLDRVGCVST TRYAQRRERA LKIYLDSPEK SSNVTASAPM DVHVNN
