ID   RDGC_DROME              Reviewed;         661 AA.
AC   P40421; A4V255; Q5U1D3; Q9VWA4;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 210.
DE   RecName: Full=Serine/threonine-protein phosphatase rdgC;
DE            EC=3.1.3.16;
DE   AltName: Full=Retinal degeneration C protein;
GN   Name=rdgC; ORFNames=CG44746;
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 [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=Oregon-R;
RX   PubMed=1316807; DOI=10.1016/0092-8674(92)90230-a;
RA   Steele F.R., Washburn T., Rieger R., O'Tousa J.E.;
RT   "Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine
RT   protein phosphatase.";
RL   Cell 69:669-676(1992).
RN   [2]
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   [3]
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 48-661.
RC   STRAIN=Berkeley; TISSUE=Head;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA   Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Phosphatase required to prevent light-induced retinal
CC       degeneration. {ECO:0000269|PubMed:1316807}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-seryl-[protein] + H2O = L-seryl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:83421; EC=3.1.3.16;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=O-phospho-L-threonyl-[protein] + H2O = L-threonyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:61977; EC=3.1.3.16;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC   -!- TISSUE SPECIFICITY: Expressed in the visual system of the fly, as well
CC       as in the mushroom bodies of the central brain.
CC       {ECO:0000269|PubMed:1316807}.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF49044.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAO41217.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAO41218.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=AAV36844.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAV36844.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR   EMBL; M89628; AAB00734.1; -; Genomic_DNA.
DR   EMBL; AE014296; AAF49044.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014296; AAO41217.2; ALT_SEQ; Genomic_DNA.
DR   EMBL; AE014296; AAO41218.3; ALT_SEQ; Genomic_DNA.
DR   EMBL; BT015959; AAV36844.1; ALT_SEQ; mRNA.
DR   PIR; A42287; A42287.
DR   RefSeq; NP_536738.3; NM_080490.4.
DR   RefSeq; NP_788544.2; NM_176366.2.
DR   RefSeq; NP_788545.3; NM_176367.3.
DR   RefSeq; NP_788546.1; NM_176368.2.
DR   PDB; 8JFW; EM; 3.64 A; D=1-661.
DR   PDB; 8JFY; EM; 2.79 A; C/D=1-605.
DR   PDB; 8ZLW; X-ray; 2.20 A; R=1-25.
DR   AlphaFoldDB; P40421; -.
DR   EMDB; EMD-36218; -.
DR   EMDB; EMD-36219; -.
DR   SMR; P40421; -.
DR   BioGRID; 65488; 6.
DR   FunCoup; P40421; 83.
DR   IntAct; P40421; 1.
DR   MINT; P40421; -.
DR   STRING; 7227.FBpp0309721; -.
DR   PaxDb; 7227-FBpp0309721; -.
DR   PeptideAtlas; P40421; -.
DR   EnsemblMetazoa; FBtr0342946; FBpp0309720; FBgn0265959.
DR   GeneID; 40224; -.
DR   KEGG; dme:Dmel_CG44746; -.
DR   AGR; FB:FBgn0265959; -.
DR   CTD; 40224; -.
DR   FlyBase; FBgn0265959; rdgC.
DR   VEuPathDB; VectorBase:FBgn0265959; -.
DR   eggNOG; KOG0377; Eukaryota.
DR   HOGENOM; CLU_012603_1_0_1; -.
DR   InParanoid; P40421; -.
DR   OrthoDB; 442428at2759; -.
DR   PhylomeDB; P40421; -.
DR   BioGRID-ORCS; 40224; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 40224; -.
DR   PRO; PR:P40421; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0265959; Expressed in outer photoreceptor cell (Drosophila) in insect head and 121 other cell types or tissues.
DR   ExpressionAtlas; P40421; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005634; C:nucleus; ISS:FlyBase.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004723; F:calcium-dependent protein serine/threonine phosphatase activity; IMP:FlyBase.
DR   GO; GO:0005516; F:calmodulin binding; IDA:FlyBase.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:FlyBase.
DR   GO; GO:0019722; P:calcium-mediated signaling; TAS:FlyBase.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
DR   GO; GO:0016059; P:negative regulation of opsin-mediated signaling pathway; IMP:FlyBase.
DR   GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR   GO; GO:0043052; P:thermotaxis; IDA:FlyBase.
DR   CDD; cd00051; EFh; 1.
DR   CDD; cd23767; IQCD; 1.
DR   FunFam; 1.10.238.10:FF:000448; Serine/threonine-protein phosphatase with EF-hands; 1.
DR   FunFam; 3.60.21.10:FF:000056; Serine/threonine-protein phosphatase with EF-hands; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR051134; PPP_phosphatase.
DR   InterPro; IPR012008; Ser/Thr-Pase_EF-hand_contain.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR45668; SERINE/THREONINE-PROTEIN PHOSPHATASE 5-RELATED; 1.
DR   PANTHER; PTHR45668:SF3; SERINE_THREONINE-PROTEIN PHOSPHATASE RDGC; 1.
DR   Pfam; PF13499; EF-hand_7; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000912; PPEF; 1.
DR   PRINTS; PR00114; STPHPHTASE.
DR   SMART; SM00054; EFh; 3.
DR   SMART; SM00015; IQ; 1.
DR   SMART; SM00156; PP2Ac; 1.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR   PROSITE; PS00018; EF_HAND_1; 2.
DR   PROSITE; PS50222; EF_HAND_2; 3.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR   PDBsum; 8JFW; -.
DR   PDBsum; 8JFY; -.
DR   PDBsum; 8ZLW; -.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Hydrolase; Magnesium; Manganese; Metal-binding;
KW   Protein phosphatase; Reference proteome; Repeat; Sensory transduction;
KW   Vision.
FT   CHAIN           1..661
FT                   /note="Serine/threonine-protein phosphatase rdgC"
FT                   /id="PRO_0000058903"
FT   DOMAIN          7..32
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          441..476
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          526..561
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          566..601
FT                   /note="EF-hand 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          105..413
FT                   /note="Catalytic"
FT   REGION          606..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        220
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         271
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         539
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         541
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         543
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         545
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         550
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         579
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         581
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         583
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         585
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         590
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CONFLICT        522
FT                   /note="D -> G (in Ref. 4; AAV36844)"
FT                   /evidence="ECO:0000305"
FT   HELIX           4..25
FT                   /evidence="ECO:0007829|PDB:8ZLW"
FT   HELIX           31..39
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           40..44
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           45..51
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            52..58
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           102..113
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           122..138
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            148..150
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          151..156
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           163..173
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          182..184
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          189..192
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           195..208
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            210..212
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          213..215
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           223..229
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           231..238
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           243..256
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          260..263
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          267..269
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           280..283
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            288..290
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          294..296
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           307..318
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          323..329
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            331..333
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          334..339
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           341..351
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          354..358
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          366..370
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   TURN            371..374
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          375..378
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          382..386
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          392..398
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          403..408
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           428..438
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           439..442
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           443..453
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          459..462
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           463..473
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           480..487
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          493..497
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           498..506
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           508..512
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           520..525
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           531..538
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           548..558
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           565..567
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           568..578
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   STRAND          580..584
FT                   /evidence="ECO:0007829|PDB:8JFY"
FT   HELIX           588..604
FT                   /evidence="ECO:0007829|PDB:8JFY"
SQ   SEQUENCE   661 AA;  75511 MW;  A3DC42933E4CCA33 CRC64;
     MDENAIRAAI FIQKWYRRHQ ARREMQRRCN WQIFQNLEYA SEQDQAELYK FFNDLIKHMP
     QAAGRKNQYQ GSAHVSVLDD KDDLVEEFGD IVNAKIELPI RKNHIDLLID VFRKKRGNRL
     HPKYVALILR EAAKSLKQLP NISPVSTAVS QQVTVCGDLH GKLDDLLVVL HKNGLPSSSN
     PYVFNGDFVD RGKRGLEVLL LLLSLYLAFP NAVFLNRGNH EDSVMNARYG FIREVESKYP
     RNHKRILAFI DEVYRWLPLG SVLNSRVLIV HGGFSDSTSL DLIKSIDRGK YVSILRPPLT
     DGEPLDKTEW QQIFDIMWSD PQATMGCVPN TLRGAGVWFG PDVTDNFLQR HRLSYVIRSH
     ECKPNGHEFM HDNKIITIFS ASNYYAIGSN KGAYIRLNNQ LMPHFVQYIS AASQTKRLSF
     KQRMGIVESS ALKELAVRMR DHRDELEDEF RKYDPKDSGY ISISHWCKVM ENVTKLGLPW
     RLLRDKLAPG TDSQKVNYNR TLDLLDTDVI LEAEADGMSV MDALYANKAS LVAIFNIIDA
     DNSGEITLDE FETAIDLLVA HMPGAYSKAE MLEKCRMMDL NGDGKVDLNE FLEAFRLSDL
     HRKEQQDENI RRRSTGRPSV AKTATDPVTL LADKISKNTL VVEHDIDPTD CESKVIDPKK
     S
//