HYD_DROME
ID HYD_DROME Reviewed; 2885 AA.
AC P51592; Q9VH88;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 3.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=E3 ubiquitin-protein ligase hyd;
DE EC=2.3.2.26 {ECO:0000269|PubMed:32339205};
DE AltName: Full=HECT-type E3 ubiquitin transferase hyd;
DE AltName: Full=Protein hyperplastic discs;
GN Name=hyd; Synonyms=l(3)C43; ORFNames=CG9484;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=7958417; DOI=10.1006/dbio.1994.1271;
RA Mansfield E., Hersperger E., Biggs J., Shearn A.;
RT "Genetic and molecular analysis of hyperplastic discs, a gene whose product
RT is required for regulation of cell proliferation in Drosophila melanogaster
RT imaginal discs and germ cells.";
RL Dev. Biol. 165:507-526(1994).
RN [2]
RP SEQUENCE REVISION.
RA Shearn A.;
RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP FUNCTION.
RX PubMed=12421709; DOI=10.1242/dev.00159;
RA Lee J.D., Amanai K., Shearn A., Treisman J.E.;
RT "The ubiquitin ligase Hyperplastic discs negatively regulates hedgehog and
RT decapentaplegic expression by independent mechanisms.";
RL Development 129:5697-5706(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2183, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-628; SER-631; SER-967;
RP SER-1362; SER-2037 AND SER-2574, 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, AND PATHWAY.
RX PubMed=32339205; DOI=10.1371/journal.ppat.1008458;
RA Cammarata-Mouchtouris A., Nguyen X.H., Acker A., Bonnay F., Goto A.,
RA Orian A., Fauvarque M.O., Boutros M., Reichhart J.M., Matt N.;
RT "Hyd ubiquitinates the NF-kappaB co-factor Akirin to operate an effective
RT immune response in Drosophila.";
RL PLoS Pathog. 16:e1008458-e1008458(2020).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrate
CC (PubMed:32339205). Required for regulation of cell proliferation in
CC imaginal disks and germ cells. Acts as a negative regulator of hh, ci
CC and dpp expression in the anterior of the eye disk (PubMed:12421709,
CC PubMed:7958417). Catalyzes 'Lys-63'-linked polyubiquitination of
CC akirin, thereby activating the immune deficiency pathway (Imd)
CC (PubMed:32339205). {ECO:0000269|PubMed:12421709,
CC ECO:0000269|PubMed:32339205, ECO:0000269|PubMed:7958417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000269|PubMed:32339205};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000269|PubMed:32339205}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7958417}. Cytoplasm
CC {ECO:0000269|PubMed:7958417}.
CC -!- DEVELOPMENTAL STAGE: Expressed at all stages of development, with high
CC levels at the embryonic and pupal stages (at protein level).
CC {ECO:0000269|PubMed:7958417}.
CC -!- DISRUPTION PHENOTYPE: Ectopic expression of hh and dpp, resulting in
CC non autonomous overgrowth of the disc and premature photoreceptor
CC differentiation that propagates into the surrounding tissue.
CC {ECO:0000269|PubMed:7958417}.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
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DR EMBL; L14644; AAB88625.1; -; mRNA.
DR EMBL; AE014297; AAF54431.2; -; Genomic_DNA.
DR PIR; T08437; T08437.
DR RefSeq; NP_524296.2; NM_079572.4.
DR SMR; P51592; -.
DR BioGRID; 66340; 14.
DR IntAct; P51592; 7.
DR STRING; 7227.FBpp0081568; -.
DR iPTMnet; P51592; -.
DR PaxDb; P51592; -.
DR PRIDE; P51592; -.
DR EnsemblMetazoa; FBtr0082090; FBpp0081568; FBgn0002431.
DR GeneID; 41181; -.
DR KEGG; dme:Dmel_CG9484; -.
DR CTD; 41181; -.
DR FlyBase; FBgn0002431; hyd.
DR VEuPathDB; VectorBase:FBgn0002431; -.
DR eggNOG; KOG0943; Eukaryota.
DR GeneTree; ENSGT00940000156357; -.
DR HOGENOM; CLU_000257_0_0_1; -.
DR InParanoid; P51592; -.
DR OMA; EAKFRRD; -.
DR PhylomeDB; P51592; -.
DR SignaLink; P51592; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 41181; 1 hit in 1 CRISPR screen.
DR ChiTaRS; hyd; fly.
DR GenomeRNAi; 41181; -.
DR PRO; PR:P51592; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0002431; Expressed in egg cell and 25 other tissues.
DR ExpressionAtlas; P51592; baseline and differential.
DR Genevisible; P51592; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0034450; F:ubiquitin-ubiquitin ligase activity; ISS:FlyBase.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007455; P:eye-antennal disc morphogenesis; IMP:FlyBase.
DR GO; GO:0008585; P:female gonad development; IMP:FlyBase.
DR GO; GO:0007444; P:imaginal disc development; IMP:FlyBase.
DR GO; GO:0007446; P:imaginal disc growth; IMP:FlyBase.
DR GO; GO:0007112; P:male meiosis cytokinesis; IMP:FlyBase.
DR GO; GO:1901315; P:negative regulation of histone H2A K63-linked ubiquitination; IBA:GO_Central.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:FlyBase.
DR GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IMP:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:FlyBase.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISS:FlyBase.
DR GO; GO:2000779; P:regulation of double-strand break repair; IBA:GO_Central.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
DR GO; GO:0007283; P:spermatogenesis; IMP:FlyBase.
DR GO; GO:0035220; P:wing disc development; IMP:FlyBase.
DR CDD; cd14423; CUE_UBR5; 1.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR024725; E3_UbLigase_EDD_UBA.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR003126; Znf_UBR.
DR Pfam; PF11547; E3_UbLigase_EDD; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00658; PABP; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00396; ZnF_UBR1; 1.
DR SUPFAM; SSF50985; SSF50985; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR SUPFAM; SSF63570; SSF63570; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS51157; ZF_UBR; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..2885
FT /note="E3 ubiquitin-protein ligase hyd"
FT /id="PRO_0000084107"
FT DOMAIN 154..196
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 2484..2561
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT DOMAIN 2782..2885
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ZN_FING 1217..1285
FT /note="UBR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00508"
FT REGION 83..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1642..1761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2124..2143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2473..2492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 641..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1668
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1669..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1724
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1729..1761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2126..2143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2478..2492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2854
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 967
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2037
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2183
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 2574
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 125
FT /note="T -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="T -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 294
FT /note="S -> P (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="S -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="Y -> C (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="R -> G (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="T -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="S -> C (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 657
FT /note="A -> G (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 741..759
FT /note="EDVQIFRTAMSTRGPDWLQ -> KMSDISHCYVTRLLA (in Ref. 1;
FT AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1490
FT /note="V -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1497
FT /note="E -> Q (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1503..1505
FT /note="EKR -> QKQ (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1557..1559
FT /note="MSS -> CHR (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1625
FT /note="R -> G (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1641
FT /note="R -> G (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1784
FT /note="P -> R (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 1978
FT /note="T -> S (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2037
FT /note="S -> T (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2096
FT /note="G -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2167
FT /note="G -> GELRVYAVNNLQTLNFQSTR (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2239..2272
FT /note="SASNLSTAEQAKCDTQYQKSTSDHLLLFPARGSQ -> RLQIYRPQNKPNVI
FT HNIKSQHQTTCYYFLLVVLS (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2280..2284
FT /note="ELPSW -> GIAPC (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2290..2291
FT /note="RW -> A (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2301
FT /note="V -> P (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2439..2440
FT /note="SR -> T (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2601
FT /note="T -> I (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2646
FT /note="G -> R (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2711..2728
FT /note="AVTSSNIFEYVRRYTEYR -> VSHRVIYSSTSDAIQNID (in Ref. 1;
FT AAB88625)"
FT /evidence="ECO:0000305"
FT CONFLICT 2814
FT /note="D -> H (in Ref. 1; AAB88625)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2885 AA; 318881 MW; F0735C28C962F85E CRC64;
MVSMQFVLQP LPGSDDQFIE RIREVSDKVN RFGYGSHRIF EQLKIPVKEV VIGPAHIGVL
LEDGKAFRVS FSINSEKLDL TKSDAKCSTS GGSGTASASK APSSSRPMAR SRARLLRATG
RSNSTGQGSG SRSTGVIIGG STSSRPLVTV PATYVPEELI SQAEVVLQGK SRNLIIRELQ
RTNLDVNLAV NNLLSRDDEE AEDTEEGADN YVPEDLISLL DNGFSGDNNS VIIDPSDGLF
SEEIFSNYSS IRNLLFDRIR SERSNANANA ADSNQSTTRS TSSGTALTGN SGLSAQISVN
ADREAFSRWR DRQYYGPRRW ISKDDYTWEK DADSKKKEPS PMLSPIWISE ELQPWPEKSS
VRFKTIGALY SEFIALSESG DLYQWRWSDA EPYKSETENV YHPKTVSLNI VERVELISAN
FIRCSVVTET NRVATWMDEQ LGYIGAKLEH SCCAFNEFIS DSITKIYVCS LYTVVKTESN
NIYWWGVLPF DQRRFLWDKF RTKTKKPFKV VATDINVGAQ VIMKKCPMYQ SGSIGFTCSN
GVPKVGQLLN SVWTFTDVCR MKIININTNS GVDKSQAAGN NLNAHGITPD KDLPKSTAMP
STGSSKNGQS FSNSKESTDR IDMPPPPSPA SSTCSDTGSV TSHKRTKRAT TKEDSNAPQE
GRKDEELWEV KDVVFVEDKV GPVGKVLKVD GDFVAVRFPA INAAAVAAAA AATSSTSNTA
STSKEEGKED DWQQCRLLRR EDVQIFRTAM STRGPDWLQK QPKKINVGGD AAGAQILTLA
VDSRGIHVIK KVLGKIHYSL YNLYNCKQEQ NCLFPTDCNS FIGSTPGNIL MACNDDCSGN
SSTIVLRDGN GALYPLAKDC LGSIKDPQWF DLPPVKSITM STISLPAMLS GVNLKSKVCM
TALLFDTQKL MPHILRCDVK NSFAALGRLE REDQADTALV VEERCDGARN IFHACVIMCA
PSSNKDSPPD SPSGGVEKKS LVGLSVARSI PTVSTSAYVS SIAFGASASS SNENSSFATM
SSSAAGSASS TSRDNRTNLR DMMNRLINSD QAEQSGSQPM ATNNEDHAYI PWPAETPAAS
NLSASSSQNV SDSIEDDISK IIPSSSQSSM LSNIKLGSPT YTFDLAQRRE HALTILQQMC
VSPALRPYLC HMLSTKDAQG QTPFMLSVSC RAYEAGIILL NTILMLSEQD PQLKEAMIFP
NGSPADQSPL HVICYNDTCS FTWTGADHIN QNIFECKTCG LTGSLCCCTE CARVCHKGHD
CKLKRTAPTA YCDCWEKCKC KALIAGNLTK RFALLCKLVS CTDLVTKFNS KGESILLFLI
QTVGRQIVEQ RQYRFSVRVR NVSTAATGAT GNNSVISNRK TSAAEIDNDM PDHDLEPPKF
ARKALERLLI DWNAVRSMIM SGAERGDVPN PAGSASENSN SEGFNMFIQT QHGSTLLDKF
THSLIVKCTS DHLDTLLLTL VRELQNASVS NRSKEAEEVV RRFVRSVARV FVIFNLEKQP
NPEKRKSHSS CNKYVQSCVK VFQTLHKISI EELCEVSEAL IAPVRLGVVR PTAPFTMSSS
NLDNSDDLFS VDPLAPSNVE SPSEQILVHD AGNDQSANFN IQQNYDVVAM ETIRDASESE
EVINREANSH NQDDELIENQ RNEDGMQDDE SDNDFTFNDA ETESDSDDNQ SNQEVQRSVQ
AGATVGSEND IGVLFLEDES GDSSAQEEDG SEDGESDDQS DEFNFNEQQL ERRSTNSNAR
SDLAPQTMQW AIRSRDTARS SVRVPTGSNM VFIDPMALRR STVPASTTVT TPSIEPHTMA
TTASNLARAF GITIRQISEL ISILSYNVLN DIETSLKIQN DEAIAVQAFV EKRLKATWDW
MFTVMDGTEA QLKFGAYLTN YTDPNHPLHP LNLSAQASSS QTPAPATSSS VNGVNIMGSN
SRRDFFTYCL SLMRSHTSEH RDALPVLDIT ALRHIAYVLD AFVYYMRNDS GFYDKQDTIS
GRINNLSPMT ESYDTDDELA NLEEFNADVQ MSASSMPSGS QGTRRHAFFA RSESTLSLGC
SAPEGFELPL DMAMPLADKP HLLQPNSKRQ ELFANLPLLV TTNANNSGAT NDGDGGSIFD
YTPTRLGFSN SLKRNERVYE TVPIDSSKTG DGNVTNKAEG STDSNIYVQL KKKQGSDDFK
SHKEADGNQS KYEKVVLMET DDSLPSTSKS TEALMATRPE VIIAPNKASV SPATAARSVI
VLAGGSCLKT IDSDINNYSA SNLSTAEQAK CDTQYQKSTS DHLLLFPARG SQFYQSNFSE
LPSWNFLLSR WKLTLDLFGR VFMDDVGMEH GSVLPELRGF PVKEMRFRRH MEKLRNGQQR
DLVLCKLERN RESLIVQTFK ELNTQFGNQS RRIQPPITFN RVKVTFKDEP GEGSGVARSF
YTSIAEALLA SAKIPNLESV QVGTNHSKYV VPFSSILRSR TVSGSSRDQS TLQRRGSNSK
ILWRSARERK ALNLDARPYT PPNSSDNATP ESLNDHLSVH LQQIGERLYP KIHSINQTHA
PKITGMLLEI PTPQLLSVIS SDETLRQKVN EAIEIITFKQ KSETSAQSSQ PKKSPSVVVV
DPVDDDNEPL FYSPGKRGFY TPRQGFASFE RINAFRNIGR LIGLCLLQNE LLPLFLQRHV
LKYILGRKIK FHDLAFFDPA LYESFRQIIQ NAQTKEGEET INRMELCFVI DLMKEEGCGN
RELIPGGRDV AVTSSNIFEY VRRYTEYRLI KSQEKALEAL KDGVFDVLPD NSMINLTAED
LRLLLNGVGD INVSTLISYT TFNDESSEGP DKLLKFKKWF WSIVEKMNIM ERQDLVYFWT
GSPALPASEE GFQPLPSVTI RPADDSHLPT ANTCISRLYI PLYSSKSILR SKMLMAIKSK
NFGFV
