UBP2_DROME
ID UBP2_DROME Reviewed; 938 AA.
AC Q8IQ27; Q8T9E4; Q9VR54;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase Usp2 {ECO:0000303|PubMed:26756164};
DE EC=3.4.19.12 {ECO:0000269|PubMed:25027767};
DE AltName: Full=Ubiquitin specific protease 2 {ECO:0000303|PubMed:25027767};
GN Name=Usp2 {ECO:0000303|PubMed:25027767, ECO:0000312|FlyBase:FBgn0031187};
GN ORFNames=CG14619 {ECO:0000312|FlyBase:FBgn0031187};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL39948.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL39948.1};
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 [4] {ECO:0000312|EMBL:AAO39652.1, ECO:0000312|EMBL:ACY46087.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAO39652.1, ECO:0000312|EMBL:ACY46087.1};
RC TISSUE=Testis {ECO:0000312|EMBL:AAO39652.1};
RA Stapleton M., Booth B., Brokstein P., Hong L., Agbayani A., Carlson J.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Sandler J., Wan K., Yu C., Lewis S.E.,
RA Rubin G.M., Celniker S.;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=24026097; DOI=10.1534/genetics.113.154211;
RA Morriss G.R., Jaramillo C.T., Mikolajczak C.M., Duong S., Jaramillo M.S.,
RA Cripps R.M.;
RT "The Drosophila wings apart gene anchors a novel, evolutionarily conserved
RT pathway of neuromuscular development.";
RL Genetics 195:927-940(2013).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH IMD AND RPT6 (ISOFORM A),
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF CYS-622.
RX PubMed=25027767; DOI=10.1186/s12964-014-0041-2;
RA Engel E., Viargues P., Mortier M., Taillebourg E., Coute Y., Thevenon D.,
RA Fauvarque M.O.;
RT "Identifying USPs regulating immune signals in Drosophila: USP2
RT deubiquitinates Imd and promotes its degradation by interacting with the
RT proteasome.";
RL Cell Commun. Signal. 12:41-41(2014).
RN [7] {ECO:0000305}
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26756164; DOI=10.1371/journal.pone.0145155;
RA Pouly D., Chenaux S., Martin V., Babis M., Koch R., Nagoshi E.,
RA Katanaev V.L., Gachon F., Staub O.;
RT "USP2-45 is a circadian clock output effector regulating calcium absorption
RT at the post-translational level.";
RL PLoS ONE 11:E0145155-E0145155(2016).
CC -!- FUNCTION: Hydrolase that deubiquitinates polyubiquitinated target
CC proteins (PubMed:25027767). Required for preventing the activation of
CC the Toll signaling cascades under unchallenged conditions
CC (PubMed:25027767). Essential for bodily calcium homeostasis
CC (PubMed:26756164). {ECO:0000269|PubMed:25027767,
CC ECO:0000269|PubMed:26756164}.
CC -!- FUNCTION: [Isoform A]: Required for preventing the activation of the
CC immune deficiency (Imd) signaling cascade under unchallenged
CC conditions. Regulates the Imd pathway by specifically removing 'Lys-
CC 48'-linked ubiquitin from imd. Also promotes imd degradation probably
CC by binding to imd and enhancing its association with the proteasome.
CC {ECO:0000269|PubMed:25027767}.
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:25027767};
CC -!- SUBUNIT: [Isoform A]: Interacts (via N-terminus) with imd (via N-
CC terminus). Interacts with Rpt6. {ECO:0000269|PubMed:25027767}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C {ECO:0000312|FlyBase:FBgn0031187}; Synonyms=F
CC {ECO:0000312|FlyBase:FBgn0031187}, G {ECO:0000312|FlyBase:FBgn0031187};
CC IsoId=Q8IQ27-1; Sequence=Displayed;
CC Name=A {ECO:0000312|FlyBase:FBgn0031187}; Synonyms=D
CC {ECO:0000312|FlyBase:FBgn0031187}, E {ECO:0000312|FlyBase:FBgn0031187};
CC IsoId=Q8IQ27-2; Sequence=VSP_059120;
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown is pupal lethal
CC (PubMed:24026097, PubMed:26756164). Pharate adults removed from their
CC pupal cases display severe defects in head eversion, with head
CC structures forming within the thoracic area (PubMed:24026097). Pupal
CC lethality can be rescued by supplementing their diet with CaCl2
CC (PubMed:26756164). RNAi-mediated knockdown in the fat body results in
CC the activation of the Imd and Toll signaling pathways under
CC unchallenged conditions, with constitutive expression of the Toll (Drs,
CC IM1) and Imd (DptA, Def, Atta) antimicrobial peptides
CC (PubMed:25027767). Flies infected with E.coli display enhanced
CC expression of Atta and DptA compared to controls (PubMed:25027767).
CC Double knockdown with imd prevents the enhanced expression of Atta and
CC DptA in uninfected and infected flies (PubMed:25027767). RNAi-mediated
CC knockdown in the clock neurons (tim) does not affect the free-running
CC period of circadian rhythms under light-dark (LD) and constant dark
CC (DD) conditions (PubMed:26756164). {ECO:0000269|PubMed:24026097,
CC ECO:0000269|PubMed:25027767, ECO:0000269|PubMed:26756164}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01035}.
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DR EMBL; AE014298; AAF50952.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09564.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09565.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09566.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07511.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07512.1; -; Genomic_DNA.
DR EMBL; AY069803; AAL39948.1; -; mRNA.
DR EMBL; BT003648; AAO39652.1; -; mRNA.
DR EMBL; BT100212; ACY46087.1; -; mRNA.
DR RefSeq; NP_001245799.1; NM_001258870.2. [Q8IQ27-1]
DR RefSeq; NP_001245800.1; NM_001258871.2. [Q8IQ27-1]
DR RefSeq; NP_608462.1; NM_134618.3. [Q8IQ27-2]
DR RefSeq; NP_728453.1; NM_167775.2. [Q8IQ27-2]
DR RefSeq; NP_728454.1; NM_167776.3. [Q8IQ27-2]
DR RefSeq; NP_728455.1; NM_167777.3. [Q8IQ27-1]
DR AlphaFoldDB; Q8IQ27; -.
DR SMR; Q8IQ27; -.
DR IntAct; Q8IQ27; 12.
DR STRING; 7227.FBpp0077041; -.
DR MEROPS; C19.A24; -.
DR PaxDb; Q8IQ27; -.
DR DNASU; 33132; -.
DR EnsemblMetazoa; FBtr0077346; FBpp0077038; FBgn0031187. [Q8IQ27-2]
DR EnsemblMetazoa; FBtr0077347; FBpp0077039; FBgn0031187. [Q8IQ27-2]
DR EnsemblMetazoa; FBtr0077348; FBpp0077040; FBgn0031187. [Q8IQ27-2]
DR EnsemblMetazoa; FBtr0077349; FBpp0077041; FBgn0031187. [Q8IQ27-1]
DR EnsemblMetazoa; FBtr0309238; FBpp0301177; FBgn0031187. [Q8IQ27-1]
DR EnsemblMetazoa; FBtr0309239; FBpp0301178; FBgn0031187. [Q8IQ27-1]
DR GeneID; 33132; -.
DR KEGG; dme:Dmel_CG14619; -.
DR UCSC; CG14619-RA; d. melanogaster.
DR CTD; 9099; -.
DR FlyBase; FBgn0031187; Usp2.
DR VEuPathDB; VectorBase:FBgn0031187; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000155545; -.
DR HOGENOM; CLU_005103_0_0_1; -.
DR InParanoid; Q8IQ27; -.
DR Reactome; R-DME-5689880; Ub-specific processing proteases.
DR BioGRID-ORCS; 33132; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33132; -.
DR PRO; PR:Q8IQ27; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0031187; Expressed in brain and 27 other tissues.
DR ExpressionAtlas; Q8IQ27; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:FlyBase.
DR GO; GO:1990380; F:Lys48-specific deubiquitinase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070628; F:proteasome binding; IPI:FlyBase.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0002785; P:negative regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0051926; P:negative regulation of calcium ion transport; IMP:UniProtKB.
DR GO; GO:0061060; P:negative regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:0045805; P:positive regulation of eclosion; IMP:UniProtKB.
DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:FlyBase.
DR GO; GO:0016579; P:protein deubiquitination; IMP:FlyBase.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; IDA:FlyBase.
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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 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; Immunity; Innate immunity; Metal-binding;
KW Protease; Reference proteome; Thiol protease; Ubl conjugation pathway;
KW Zinc.
FT CHAIN 1..938
FT /note="Ubiquitin carboxyl-terminal hydrolase Usp2"
FT /id="PRO_0000441821"
FT DOMAIN 613..938
FT /note="USP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 273..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 622
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035,
FT ECO:0000305|PubMed:25027767"
FT ACT_SITE 895
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01035"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT BINDING 817
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:O75604"
FT VAR_SEQ 1..540
FT /note="MMLDIKKTRGFHKIPQASKLQSTTKTSSVVATSASSQNEVPSPGGSAGSKVG
FT ATNPVRAANQRFFLVSSYKDPTFLKAECDLAHAHVTTSKVKTTLQPHRRSRAGEDSRNN
FT NYNTSRAPTLINMRRPSLFNGNQQPTTTNSTTINNTTSRNTTSNTSNGVLKYSVRSTTA
FT TATSTSTRNYGKLKPLNNNQTTAGVAMMNGHTNNNNNNTRNSSNINNGGNNNMQRQQQQ
FT HDDISFIDSDDPPATGGPEAGISTTKTSICYFKPITPPLQLRHEQNQVQQQEEQPQPSS
FT SKSASHRYPRPKSTIIASAHSNFAASFEKFSGGLYRQTNGETNIESKTSSNARRYGIDS
FT LSIKASIEKFNNLSGQKRQNPGSGSGIGPGSATASGLGGGRLSVASRSNHGSQAGGSSS
FT NLQQRYSSDLDNIRVAAGYSSSLTRAAYRTTATMNSVSTPVAVTSELGGPISGDGGETA
FT TAMGQPTSKVTVRGAHSNRQPIECDSVVLTNKASKDATTAATPTVATATATHTPATSSV
FT STVTVTAAAPNSASDS -> MRVIAPRRSSTSAAGSGSLYGTSAVGTSSGSTTSSNSTS
FT GSHHISITGSGAVDRTSGGAATNGYSRISSSYDRGSSLSKWLPTSSGGSNSSGYGSSYY
FT PTSYSTFSANSGSSSASYAPRSSVQRSSVGTTSSTSYMSGGSGSSSSAYRTSSYLSGSS
FT YDSPTYSRYGLPRKAASRITTNGDSLSGSAKREDYGLRRGHDTVKKPPISGGSVGHNCS
FT SSTASRDTKAVDGNKRLSSSSSSPSLARLVATSGLDIYEKYSPANYKPNCELSRSRSGH
FT SETDLENGSNKETTPTCTVTLDRPWSSTSRYSRLYRNSSDAGGDSSASAKKLGSGKYSI
FT SSSSSSGDVPTATFTLRSKRTRRNQAEEVPTSTGVEQAGPAAPPPTPPPPPPPPPPTNG
FT HKPAESNGGLEAKLNGLSLLSTSPKRNAIYERNQETADDAGVSQDTADNADVSTSATFK
FT LNDSSK (in isoform A)"
FT /evidence="ECO:0000305"
FT /id="VSP_059120"
FT MUTAGEN 622
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25027767"
SQ SEQUENCE 938 AA; 101704 MW; 6CD54A8DF5E2C4D1 CRC64;
MMLDIKKTRG FHKIPQASKL QSTTKTSSVV ATSASSQNEV PSPGGSAGSK VGATNPVRAA
NQRFFLVSSY KDPTFLKAEC DLAHAHVTTS KVKTTLQPHR RSRAGEDSRN NNYNTSRAPT
LINMRRPSLF NGNQQPTTTN STTINNTTSR NTTSNTSNGV LKYSVRSTTA TATSTSTRNY
GKLKPLNNNQ TTAGVAMMNG HTNNNNNNTR NSSNINNGGN NNMQRQQQQH DDISFIDSDD
PPATGGPEAG ISTTKTSICY FKPITPPLQL RHEQNQVQQQ EEQPQPSSSK SASHRYPRPK
STIIASAHSN FAASFEKFSG GLYRQTNGET NIESKTSSNA RRYGIDSLSI KASIEKFNNL
SGQKRQNPGS GSGIGPGSAT ASGLGGGRLS VASRSNHGSQ AGGSSSNLQQ RYSSDLDNIR
VAAGYSSSLT RAAYRTTATM NSVSTPVAVT SELGGPISGD GGETATAMGQ PTSKVTVRGA
HSNRQPIECD SVVLTNKASK DATTAATPTV ATATATHTPA TSSVSTVTVT AAAPNSASDS
TLARSGTGSS STARSVLPPM TPTSSRYWDR DSGTSRSSIG TSSALNSSSL KHNSDDGYKT
ASSSRDEKSE GLCGLRNIGN TCFMNSVIQC LSHTQELTRF LRSHHGSRSL STKDQQILHE
FAKLIQEMWT ANVHTVTPME LKRAFSTKHR MYSDYNQQDA QEFLRFFLDS LHSALNSGVK
GETLNIDDNL SDNKKADLTW EWYTRHENSL VRDLFVGQLK STLKCTTCGN TSVTFDPFWD
LSVPLPSSSR CKLEACLDLF IREEVLDGDE MPTCAKCKTR RKCTKSFTIQ RFPKYLVIHL
KRFSETRWSK LSNIVEFPTS DSELNMGSYG ANSNSNVHYS LYAISNHMGS TAGGHYVALC
KHPVSRKWHE FNDNIVSDAL SENHLVSSSA YILFYERT
