POE_DROME
ID POE_DROME Reviewed; 5322 AA.
AC Q9VLT5; O96958; Q8MS98; Q9XYD1; Q9XYD2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Protein purity of essence;
DE AltName: Full=Interaction calmodulin and colossal molecular mass protein;
DE AltName: Full=Protein Calossin;
DE AltName: Full=Protein pushover;
GN Name=poe {ECO:0000312|EMBL:AAF52598.1, ECO:0000312|FlyBase:FBgn0011230};
GN Synonyms=calo {ECO:0000312|EMBL:CAA76940.1},
GN push {ECO:0000312|EMBL:AAD20450.1}; ORFNames=CG14472;
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] {ECO:0000305, ECO:0000312|EMBL:AAD20450.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS A AND B), FUNCTION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11517334; DOI=10.1073/pnas.191107698;
RA Yager J., Richards S., Hekmat-Scafe D.S., Hurd D.D., Sundaresan V.,
RA Caprette D.R., Saxton W.M., Carlson J.R., Stern M.;
RT "Control of Drosophila perineurial glial growth by interacting
RT neurotransmitter-mediated signaling pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:10445-10450(2001).
RN [2] {ECO:0000312|EMBL:AAF52598.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAF52598.1}
RP GENOME REANNOTATION.
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 [4] {ECO:0000305, ECO:0000312|EMBL:CAA76940.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1207-5322 (ISOFORM A), PUTATIVE FUNCTION, AND
RP INTERACTION WITH CALMODULIN.
RC TISSUE=Retina {ECO:0000312|EMBL:CAA76940.1};
RX PubMed=9813038; DOI=10.1074/jbc.273.47.31297;
RA Xu X.-Z.S., Wes P.D., Chen H., Li H.-S., Yu M., Morgan S., Liu Y.,
RA Montell C.;
RT "Retinal targets for calmodulin include proteins implicated in synaptic
RT transmission.";
RL J. Biol. Chem. 273:31297-31307(1998).
RN [5] {ECO:0000305, ECO:0000312|EMBL:AAM50858.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5019-5322 (ISOFORM A).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50858.1};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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] {ECO:0000305}
RP IDENTIFICATION, AND PUTATIVE FUNCTION.
RX PubMed=8244010; DOI=10.1093/genetics/135.2.489;
RA Castrillon D.H., Gonczy P., Alexander S., Rawson R., Eberhart C.G.,
RA Viswanathan S., DiNardo S., Wasserman S.A.;
RT "Toward a molecular genetic analysis of spermatogenesis in Drosophila
RT melanogaster: characterization of male-sterile mutants generated by single
RT P element mutagenesis.";
RL Genetics 135:489-505(1993).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1894, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; THR-599; SER-600;
RP SER-1167; SER-1168; SER-1171; SER-1894; THR-3013; SER-3014; SER-3051;
RP SER-3057 AND SER-3510, 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 [9]
RP FUNCTION.
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: Has a role in growth of the perineurial glial layer of the
CC larval peripheral nerve (PubMed:27552662). May have a role in male
CC fertility and eye development or function (PubMed:27552662). Involved
CC in the negative regulation of the Ras/MAPK signaling pathway in the
CC wing by acting with the E2 enzyme Unc6 and the putative E3 ligases
CC Kcmf1 and Ufd4 to mediate the ubiquitination and proteasomal
CC degradation of rl/MAPK (PubMed:27552662). {ECO:0000269|PubMed:11517334,
CC ECO:0000269|PubMed:27552662}.
CC -!- SUBUNIT: May bind calmodulin (PubMed:9813038). Interacts with Kcmf1
CC (PubMed:27552662). {ECO:0000269|PubMed:27552662,
CC ECO:0000269|PubMed:9813038}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:11517334};
CC IsoId=Q9VLT5-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:11517334};
CC IsoId=Q9VLT5-2; Sequence=VSP_052089, VSP_052090;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic central nervous system and
CC adult testes. {ECO:0000269|PubMed:11517334}.
CC -!- DISRUPTION PHENOTYPE: Flies increase the growth of the perineurial
CC glial layer of the larval peripheral nerve and exhibit male sterility
CC due to the inhibition of sperm individualization.
CC {ECO:0000269|PubMed:11517334}.
CC -!- SIMILARITY: Belongs to the UBR4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50858.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={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; AF096896; AAD20449.1; -; Genomic_DNA.
DR EMBL; AF096897; AAD20450.1; -; mRNA.
DR EMBL; AE014134; AAF52598.1; -; Genomic_DNA.
DR EMBL; Y17920; CAA76940.1; -; mRNA.
DR EMBL; AY118998; AAM50858.1; ALT_SEQ; mRNA.
DR PIR; T13719; T13719.
DR RefSeq; NP_001260222.1; NM_001273293.1. [Q9VLT5-1]
DR RefSeq; NP_476986.1; NM_057638.4. [Q9VLT5-1]
DR BioGRID; 70146; 19.
DR IntAct; Q9VLT5; 10.
DR STRING; 7227.FBpp0079167; -.
DR iPTMnet; Q9VLT5; -.
DR PaxDb; Q9VLT5; -.
DR PRIDE; Q9VLT5; -.
DR EnsemblMetazoa; FBtr0079545; FBpp0079167; FBgn0011230. [Q9VLT5-1]
DR EnsemblMetazoa; FBtr0333088; FBpp0305301; FBgn0011230. [Q9VLT5-1]
DR GeneID; 46243; -.
DR KEGG; dme:Dmel_CG14472; -.
DR CTD; 46243; -.
DR FlyBase; FBgn0011230; poe.
DR VEuPathDB; VectorBase:FBgn0011230; -.
DR eggNOG; KOG1776; Eukaryota.
DR GeneTree; ENSGT00600000084471; -.
DR HOGENOM; CLU_000069_0_0_1; -.
DR InParanoid; Q9VLT5; -.
DR OMA; NAEACMH; -.
DR PhylomeDB; Q9VLT5; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q9VLT5; -.
DR BioGRID-ORCS; 46243; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 46243; -.
DR PRO; PR:Q9VLT5; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0011230; Expressed in eye disc (Drosophila) and 25 other tissues.
DR ExpressionAtlas; Q9VLT5; baseline and differential.
DR Genevisible; Q9VLT5; DM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0043186; C:P granule; IPI:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:FlyBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0042065; P:glial cell growth; IMP:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IGI:FlyBase.
DR GO; GO:0042066; P:perineurial glial growth; IMP:FlyBase.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:FlyBase.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR025704; E3_Ub_ligase_UBR4_C.
DR InterPro; IPR045841; E3_UBR4_N.
DR InterPro; IPR045189; UBR4-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR003126; Znf_UBR.
DR PANTHER; PTHR21725; PTHR21725; 1.
DR Pfam; PF13764; E3_UbLigase_R4; 1.
DR Pfam; PF19423; E3_UBR4_N; 3.
DR Pfam; PF02207; zf-UBR; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Developmental protein;
KW Differentiation; Metal-binding; Neurogenesis; Phosphoprotein;
KW Reference proteome; Sensory transduction; Vision; Zinc; Zinc-finger.
FT CHAIN 1..5322
FT /note="Protein purity of essence"
FT /id="PRO_0000245794"
FT ZN_FING 1794..1863
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 144..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2401..2435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2587..2610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2993..3075
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3484..3508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4196..4216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..694
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2596..2610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2996..3064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3484..3501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 599
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 600
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1167
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1171
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1894
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 3013
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3014
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3051
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3057
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 3510
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 4119..4120
FT /note="LP -> TL (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11517334"
FT /id="VSP_052089"
FT VAR_SEQ 4121..5322
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:11517334"
FT /id="VSP_052090"
FT CONFLICT 675
FT /note="S -> T (in Ref. 1; AAD20449/AAD20450)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="I -> T (in Ref. 1; AAD20449)"
FT /evidence="ECO:0000305"
FT CONFLICT 1405
FT /note="S -> A (in Ref. 1; AAD20449/AAD20450)"
FT /evidence="ECO:0000305"
FT CONFLICT 1621
FT /note="N -> D (in Ref. 1; AAD20449/AAD20450)"
FT /evidence="ECO:0000305"
FT CONFLICT 2965
FT /note="L -> P (in Ref. 4; CAA76940)"
FT /evidence="ECO:0000305"
FT CONFLICT 3105
FT /note="A -> T (in Ref. 1; AAD20450)"
FT /evidence="ECO:0000305"
FT CONFLICT 3159..3164
FT /note="DYVEIG -> GLCGNW (in Ref. 1; AAD20450)"
FT /evidence="ECO:0000305"
FT CONFLICT 3257
FT /note="G -> A (in Ref. 4; CAA76940)"
FT /evidence="ECO:0000305"
FT CONFLICT 4011
FT /note="D -> H (in Ref. 1; AAD20449)"
FT /evidence="ECO:0000305"
FT CONFLICT 4812
FT /note="V -> G (in Ref. 4; CAA76940)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 5322 AA; 590702 MW; 3890824E00F2DB50 CRC64;
MSAHSGGTDW NSVVKALILN RTGALNKNEV VNLLKAITRC EHDFFEEESN FTQFYTAFAA
LAADKLMQIK TICQTQICQL HDATAVLIRF IIYRLPRVSV YETKWLLGAL KMLCEGRECP
ASASSSMFDY NAVANVLKSC KHPESTTKSI MPSSSSSGSG ASNDKESPKS EIKRSRSDLS
SVILQQLIAP LEPGKMTWVP LSEEVTDCTE QILAANVEYF QEQNGVDTLL DVCVSLPILN
RYRSKYMETI NGGKSLYLPL TQVEATAVKS SMNHMLTDLT ILSQAQALIE MQPLTPSRIE
RLSMCGIAAL YNAVLTSIAT SVLGMSQASS SQKQTASTSQ GSGVGGSSGG QSNKDHDDFE
DQACSIVNKA LEIYSNIGHM FKTSARIHVY QNHLCYGSWL LISGIQGAMG ASGSGGSSSD
SASKSASKAT KSGSEAGTAP TTPIARVNLF KVQQGFGELN AAIANHSIKL LSELIEDLKV
EAACGQSLES TELPEPAQFD ILQNYSSLER IVRVLNTATL HQLFTFLATV AYRKACTLKR
ASAKDRTECE PISYSDSTTY FNDSLSCSDN SEEDDSESYL GHWFKETLSP ETHDDNANTS
TQERAEQKSA LVPKLDEPHE YLDLAADIFC FLDQFLANRH AYMQRYVKAG VSDQQMLLMA
NIIKDFDRDV MRNESDQGSG NAPAASAGAG TSAGASTKWQ TSMIRFSGAA GRYIHNLIST
SLLSEQLQSN LLQHLSISPW STDTNTWPLQ VYPSTLSVLV QILLLKPTQE KEAACLSVWH
RLINTLVEGV CSSNTASDSD YEDLNIEHAQ LLLFLFHSLN LMQKKSILLL TAGGVIRCAE
VCRGISEDRP VKNSQIMLLS RLLLFLEYLM KHLYNAPPEL LDQVRWNLFS VSSMPDTQKI
TDLLNCRTKL NSYCRHDIEE NFRKSAGEYG SSIRPTFYSL VMGDPEISYW AQEFKLDGLA
WNFILCTPDK LKYPLLVDAL TDILSITDMS MYSKEKDKEA SMHNLCAIQY CFTIAWKLNL
GLPPSTSHVE SLKAERSPNL HSLMWSIRLP LASSHYLVVS SLIKQGMYTQ YAETLWTHVG
DIGADIKYSL KQTILGVEAF NSQMNGNGTP RLSDLILFDS LVAHMQAVAW ANKEGLKWPR
KESEDAAGEQ SAGTSLTSSS NDPELYSSNE SIDDQKLKQD DDGKLSSDLQ KYNQLVNELM
VKLMNSYQLL SVIVRGQMLK QLSSSTPEKA LNLIVPIVSD KPAIMLELHA AFLKLLPNED
KQLIANEWPK CLMVNDFAFN GKQHPVEPYI LNVIDAHIIE LTRGSNYSTL HTLKHCLKSI
LQLFELLLPH RTANAEVETQ LKQLLISSML DMRTDYLQGH SEHCLREILS GLTQEAQKLL
LYEHMVGYCY RMLKEFAADL RQPQSAGPSG GAPLDQDRAM FNESMLFAVL KTMFKMLEKP
VAVQAMRQFF KDQRSGSLTT LLLSFTGTSL PVSYARKMLQ FVNRLFQLSL QADSQFQHED
LVECFSELAT VDVARLKQWL GHIIYGPNVS TDVSTSEALD TTCRMLTSIL QPSSSSSSNA
QTPTNMATVS AMPSISDQLD PMEIEYDCGT AAGGGESNPG TGGAAANTSQ ILSLWQAAQP
NPSEESSQAC DHSDSERNGA LLLSFVKSLV KDQSKASQIA PPLFQALLQL GQTLISPPQE
GCDFADVLQI MITLADASPA RGHVALFNTT LLWLELAKLQ LPDKHLKHAE NVSAQLRYLS
ELLQSIGFRG SRQHNPPWDD ELQTDIDELY DELAEEGEQD SLLDDSDEDT LNNKLCTFSQ
TQKEFMNQHW YHCHTCNMIN TVGVCSVCAR VCHKGHDVSY AKYGNFFCDC GAKEDGSCQA
LSRRIGSNEV RDSAGIGSYL PSHMSLLAGK KRSSLPVGQP VLTRKDSLTN ERIAVLTKLL
EPYRETLQHQ DQWLLVVRCI LEYFDLLLPS INENCMLYSI VGCHKRATAA LERLHLLEQS
FQVTDQLMFA TLGSQEGAFE NVRMNYSGDQ GQTIKHLLSS GVVRRVAFCC LSSPHGRRQQ
LAVSHEKGKV TILQLSALLK QADASKRKLT LTQLSSAPIA CTVISLAANP CNEDCLAVCG
LKECHILTFS SSGSTNEHIV VNPQLENGNY IKKAVWLPGS QTLLAVVTSD YVKIYDLAVD
TYSPKYYYLV AVGKIRDCTF VYQDGNYNML TFASSGYIYT QQLDQQSLAV HGDFYVTNTL
ELSHQHIKDI AGHIGGGGVS IYYSHTLQLL FYSYSCGRSF FSPLTNVSEG VKGIYHLDTN
SASKSASKGP LQPLVQWTEV TGHPGLVYAS MQTSNNPIIL MITPERIYLQ EIKAQSAKSR
IMDVVGIRHA VAGVEKTTLL LLCEDGSLRI FSAQPEYTSF WLSPQVQPFG NQLYSSTLMA
KGGGSGSTSK SKSNTASGKM TSRKASQQQK QPTAGGQPVF PIDFFEHCNM LADVEFGGND
LLQIYNKQKL KTRLFSTGMF VASTRSNGFT LEVINNDPNV VIVGIRVLIG TQDVQRAPQS
VTILGRTIPT PVRRARWFDI PLTREEMLQS DKLLKVVFAK APDPEHVTLL DCIEVYGKSK
ELVGWPDESE DVTVPGSSAP AVSSSQASSA NFGEGFNCIT QLDRMANHLL EVMDCALHLL
GSGVPASMRQ KAVKTASALL LLPTPNPVQT QARYVLATLY GTRALYHNYK DGVLLQFVNR
ELQSMQPKLE KLETLREIDP EAFYRLVLMV RGIANARPQS LAKICVENNY DIVPTLMGIV
LELHKVTPTL DEPVNIVKRG LCQPETIVHC LVEIMYGFAL ADPGQVGRMT KYFIDLLKHD
ASVISHSAKE ALILLLSPRM KRRKVAIVTP PACSTPTPST STMQALQAAA SSAASDIIEE
AAGVVVDGSV GGGGLPEPNA DAEGAAVGVG GVGQQQMLNL EAFMGGGFPR LLGLPEDADD
EAIMDIAIAL SLQQHGGDAN ALQSLQQGLA NLQGIRQATA MAAAVNAAAN VSLGGSDDDE
GSNVATDGST LRTSPAEPAG SGGSESGGSG VESIGGTSAR SSNFGDHANA SPPRQGSTKD
DQEQPGPSGV AGSGGVAVLS AMSSSEDNEA NEDDKLSKLH DLRIAVLESI IQHLGTFDLC
NGLQAIPLIQ VILMLTTDLN GNNERDQQVL HDLLTALVDY VEIGKRGAAA RMETKCPGNE
VRLALLSLFG VLMGKTKSKQ TGTTSPPHQF KDNSSFVAST TANVLSKSGA FVYALEALNT
LLVHWKNVLG DPYAAGGGLA SQSAQASGGA SGPGVQLLKP IKHGPKPDIS ILIPHNYLKN
YPDIFESYDG LLTEIIVRLP YQILRLSSAH PDNYDSGFCE AMTFTLCEYM MLNLNTLLRR
QVRKLLMYIC GSKEKFRMYR DGHSLDAHFR VVKRVCNIVS SKTGAPYNAN PPMLSYDALV
ELTEHLRTCQ EISQMRTGNW QKFCVVHEDA LAMLMEIACY QLDDGVSPII IQLLQAAVCN
LPPPSGSKQA QPQPSTSSAS GKLRTDREKS EDTDAYYSKF DPAQCGTFVH QIFRYACDAL
IIRFVRIFLL ENNITQLRWQ AHSFMTGLFE HANERQREKL LNIFWNLWPL VPTYGRRTAQ
FVDLLGYLTL STRSITERLP EFVSRAVDVL RQQNELLCKH PNAPIYTTLE SILQVNGYYL
ESEPCLVCNN PEVPMANIKL PSVKSDSKYT TTTMIYKLVQ CHTISKLIVR IADLKRTKMV
RTINVYYNNR SVQAVVELKN RPALWHKARS VSLQSAQTEL KIDFPLPITA CNLMIEFADF
FETVSGSSEN LQCPRCSAAV PAYPGVCGNC GENVFQCHKC RAINYDEKDP FLCHSCGFCK
YAKFDFSMYA RVCCAVDPIE SAEDRVKTVS LIHSSLERAD RNYRQLLTNK QMLELLIQKV
AEHRSSDRMV EDNMASVHST SQVNKIIQLL AQKYCVESRT SFEELSKIVQ KVKACRSELV
AYDRQQQDQP PVNPGSTTGA ENPTTNRCYG CALASTEQCL TLLRAMAYNY DCRVCLYSQG
LVSELAEHNL RRGTPLIQEE VRNLLVVLTK DNAEACMHLL QLVTTRVKNA LMGSIPLISL
EAAVHQEMTL LEVLLGQDDI CWEYKLKVIF ELFISNCRLP RGPVTAVLHP CLRIMQNLIC
PVLPGSKPNQ KVATTDLCSM KMFEGNTVDY RAWLNSDRNH EYAAWSKRMP SNNQAKLKNA
KDQNVAASGG SDAPPKSRRE VRVAFLSEKY GKRWRERVLD KQRVIKPLVF NAKWIQPLLF
NANSRFGRQL ACSLLSSLSR TNERRQQALN MLTSFLKHVG EAGEASAEYL MLYKNMATEQ
PWLQYLVLKG VLSQISQLLA IEISKVHRME EYSLSSDLSL GYALRQYVEL LWLLLECPNI
RRTYKTRMLG PVLESYLALR SLVVQRTRLI DDAQEKLLEM LEDMTSGTEE ETRAFMEILI
DTVEKTRMND IKTPVFVFER LYSIIHPEEH DESEFYMTLE KDPQQEDFLQ GRMLGNPYPS
SEMGLGPLMR DVKNKICTDC ELIALLEDDN GMELLVNNKI ISLDLPVKDV YKKVWLAEGG
DRDAMRIVYR MRGLLGDATE EFVETLNNKS QEQVDTEQLY RMANVLADCN GLRVMLERIG
SLQRISRNRE LIQVLLKLFL ICVKVRRCQE VLCQPEIGAI NTLLKVLQMC LQSENDSIQS
AVTEQLLEIM ETILSKAASD TLDSFLQFSL TFGGPEYVSA LISCTDCPNV RNNPSVLRHL
IRVLAALVYG NEVKMALLCE HFKDTLNFNR FDNERTPEEE FKLELFCVLT NQIEHNCIGG
TLKDYIVSLG IVERSLAYIT EHAPCVKPTL LRTDSDELKE FISRPSLKYI LRFLTGLSNH
HEATQVAISK DIIPIIHRLE QVSSDEHVGS LAENLLEALS TDSATAARVQ QVRDFTRAEK
KRLAMATREK QLDALGMRTN EKGQVTAKGS ILQKIEKLRD ETGLTCFICR EGYACQPDKV
LGIYTFTKRC NVEEFELKSR KTIGYTTVTH FNVVHVDCHT SAIRLTRGRD EWERASLQNA
NTRCNGLLPL WGPAVGEAAF SACMTRHSSY MQESTQRCDI SYTSSVHDLK LLLVRFAWER
SFHDDAGGGG PQSNMHFVPY LLFYSVYLLL SSRSAARDSK TLLTYLQAPP SEKWLECGYE
VDGPLFMATI SLSLHSRELW NKHKLAHLKR MIAVAQGRHV SPAVLCKALL APADRQVKDY
TVYKPFLMMW ALVDLIYDNL FKTVSTPKEE DWPISLFDYL RKNDEALLKS TDSILQTLTE
EFLPCTSFVE FCDVAGLLHL IEHPDNFIEE ILAALPSTSS SN
