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   27-MAR-2024, entry version 200.
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; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; 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=H2O + O-phospho-L-seryl-[protein] = 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=H2O + O-phospho-L-threonyl-[protein] = 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   AlphaFoldDB; P40421; -.
DR   SMR; P40421; -.
DR   BioGRID; 65488; 6.
DR   IntAct; P40421; 1.
DR   MINT; P40421; -.
DR   STRING; 7227.FBpp0309721; -.
DR   PaxDb; 7227-FBpp0074602; -.
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   GeneTree; ENSGT00940000169749; -.
DR   HOGENOM; CLU_012603_1_0_1; -.
DR   InParanoid; P40421; -.
DR   OrthoDB; 3076469at2759; -.
DR   PhylomeDB; P40421; -.
DR   BioGRID-ORCS; 40224; 0 hits in 3 CRISPR screens.
DR   ChiTaRS; rdgC; fly.
DR   GenomeRNAi; 40224; -.
DR   PRO; PR:P40421; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0265959; Expressed in brain and 12 other cell types or tissues.
DR   ExpressionAtlas; P40421; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:FlyBase.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISS: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:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
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:0016059; P:deactivation of rhodopsin mediated signaling; IMP:FlyBase.
DR   GO; GO:0050906; P:detection of stimulus involved in sensory perception; IEA:InterPro.
DR   GO; GO:0007602; P:phototransduction; IMP:FlyBase.
DR   GO; GO:0006470; P:protein dephosphorylation; IMP:FlyBase.
DR   GO; GO:0043052; P:thermotaxis; IDA:FlyBase.
DR   GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR   CDD; cd00051; EFh; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; 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   Genevisible; P40421; DM.
PE   2: Evidence at transcript level;
KW   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"
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
//