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   02-SEP-2026, entry version 191.
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; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; 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, AND PATHWAY.
RX   PubMed=28689657; DOI=10.1016/j.molcel.2017.06.009;
RA   Flack J.E., Mieszczanek J., Novcic N., Bienz M.;
RT   "Wnt-dependent inactivation of the Groucho/TLE co-repressor by the HECT E3
RT   ubiquitin ligase Hyd/UBR5.";
RL   Mol. Cell 67:181-193(2017).
RN   [9]
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:28689657, PubMed:32339205). Required for regulation of cell
CC       proliferation in imaginal disks and germ cells (PubMed:12421709,
CC       PubMed:7958417). Acts as a negative regulator of hh, ci and dpp
CC       expression in the anterior of the eye disk (PubMed:12421709,
CC       PubMed:7958417). Acts as a positive regulator of the canonical Wnt
CC       signaling pathway by mediating ubiquitination and degradation of gro
CC       (PubMed:28689657). 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:28689657, ECO:0000269|PubMed:32339205,
CC       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:28689657, 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.
CC   -!- SIMILARITY: Belongs to the UBR5 family. {ECO:0000305}.
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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; 16.
DR   FunCoup; P51592; 2948.
DR   IntAct; P51592; 14.
DR   STRING; 7227.FBpp0308671; -.
DR   GlyGen; P51592; 2 sites.
DR   iPTMnet; P51592; -.
DR   PaxDb; 7227-FBpp0308671; -.
DR   PeptideAtlas; P51592; -.
DR   EnsemblMetazoa; FBtr0082090; FBpp0081568; FBgn0002431.
DR   GeneID; 41181; -.
DR   KEGG; dme:Dmel_CG9484; -.
DR   AGR; FB:FBgn0002431; -.
DR   CTD; 41181; -.
DR   FlyBase; FBgn0002431; hyd.
DR   VEuPathDB; VectorBase:FBgn0002431; -.
DR   eggNOG; KOG0943; Eukaryota.
DR   HOGENOM; CLU_000257_0_0_1; -.
DR   InParanoid; P51592; -.
DR   OrthoDB; 298098at2759; -.
DR   PhylomeDB; P51592; -.
DR   SignaLink; P51592; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 41181; 1 hit in 1 CRISPR screen.
DR   GenomeRNAi; 41181; -.
DR   PRO; PR:P51592; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0002431; Expressed in egg cell and 169 other cell types or tissues.
DR   ExpressionAtlas; P51592; baseline and differential.
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: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: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   CDD; cd19675; UBR-box_UBR5; 1.
DR   FunFam; 3.30.2160.10:FF:000006; E3 ubiquitin-protein ligase UBR5 isoform X2; 1.
DR   FunFam; 1.10.8.10:FF:000009; Putative E3 ubiquitin-protein ligase UBR5; 1.
DR   FunFam; 3.30.2410.10:FF:000008; Putative E3 ubiquitin-protein ligase UBR5; 1.
DR   Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR   Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 2.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 1.
DR   InterPro; IPR063155; HEAT_UBR5_1st.
DR   InterPro; IPR063527; HEAT_UBR5_2nd.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR036053; PABP-dom.
DR   InterPro; IPR002004; PABP_HYD_C.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR047503; UBR-box_UBR5.
DR   InterPro; IPR024725; UBR5_UBA.
DR   InterPro; IPR003126; Znf_UBR.
DR   PANTHER; PTHR46276; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR   PANTHER; PTHR46276:SF1; E3 UBIQUITIN-PROTEIN LIGASE UBR5; 1.
DR   Pfam; PF11547; E3_UbLigase_EDD; 1.
DR   Pfam; PF30806; HEAT_UBR5_1st; 1.
DR   Pfam; PF30807; HEAT_UBR5_2nd; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00658; MLLE; 1.
DR   Pfam; PF30802; zf-UBR_1; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00517; PolyA; 1.
DR   SMART; SM00396; ZnF_UBR1; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 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        95..108
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..138
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        266..276
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..291
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..615
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        650..664
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..722
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1008..1032
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1669..1681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1696..1721
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1735..1749
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2482..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
//