RDGC_DROME
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 03-AUG-2022, entry version 194.
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.FBpp0074602; -.
DR PaxDb; P40421; -.
DR PRIDE; P40421; -.
DR EnsemblMetazoa; FBtr0342946; FBpp0309720; FBgn0265959.
DR GeneID; 40224; -.
DR KEGG; dme:Dmel_CG44746; -.
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 OMA; ATHMLTM; -.
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 tissues.
DR ExpressionAtlas; P40421; baseline and differential.
DR Genevisible; P40421; DM.
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 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 Pfam; PF13833; EF-hand_8; 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; SSF47473; 1.
DR SUPFAM; SSF56300; SSF56300; 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.
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
