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P40421 (RDGC_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase rdgC

EC=3.1.3.16
Alternative name(s):
Retinal degeneration C protein
Gene names
Name:rdgC
ORF Names:CG44746
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length661 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Phosphatase required to prevent light-induced retinal degeneration. Ref.1

Catalytic activity

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Tissue specificity

Expressed in the visual systems of the fly, as well as in the mushroom bodies of the central brain. Ref.1

Sequence similarities

Belongs to the PPP phosphatase family.

Contains 3 EF-hand domains.

Contains 1 IQ domain.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandCalcium
Iron
Magnesium
Manganese
Metal-binding
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcalcium-mediated signaling

Traceable author statement PubMed 10611962. Source: FlyBase

deactivation of rhodopsin mediated signaling

Inferred from mutant phenotype PubMed 11754840. Source: FlyBase

detection of stimulus involved in sensory perception

Inferred from electronic annotation. Source: InterPro

phototransduction

Inferred from mutant phenotype PubMed 2361011PubMed 8446607. Source: FlyBase

protein dephosphorylation

Inferred from mutant phenotype PubMed 8446607. Source: FlyBase

thermotaxis

Inferred from direct assay PubMed 18660806. Source: FlyBase

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

calmodulin binding

Inferred from direct assay PubMed 11754840. Source: FlyBase

iron ion binding

Inferred from electronic annotation. Source: InterPro

manganese ion binding

Inferred from electronic annotation. Source: InterPro

protein serine/threonine phosphatase activity

Inferred from sequence or structural similarity Ref.1. Source: FlyBase

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform B (identifier: P40421-1)

Also known as: C; D;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform A (identifier: P40421-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 661661Serine/threonine-protein phosphatase rdgC
PRO_0000058903

Regions

Domain7 – 3226IQ
Domain441 – 47636EF-hand 1
Domain526 – 56136EF-hand 2
Domain566 – 60136EF-hand 3
Calcium binding539 – 550121 Potential
Calcium binding579 – 590122 Potential
Region105 – 413309Catalytic

Sites

Active site2201Proton donor By similarity
Metal binding1581Iron By similarity
Metal binding1601Iron By similarity
Metal binding1871Iron By similarity
Metal binding1871Manganese By similarity
Metal binding2191Manganese By similarity
Metal binding2711Manganese By similarity
Metal binding3601Manganese By similarity

Natural variations

Alternative sequence1 – 5858Missing in isoform A.
VSP_009324

Experimental info

Sequence conflict5221D → G in AAV36844. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform B (C) (D) [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: A3DC42933E4CCA33

FASTA66175,511
        10         20         30         40         50         60 
MDENAIRAAI FIQKWYRRHQ ARREMQRRCN WQIFQNLEYA SEQDQAELYK FFNDLIKHMP 

        70         80         90        100        110        120 
QAAGRKNQYQ GSAHVSVLDD KDDLVEEFGD IVNAKIELPI RKNHIDLLID VFRKKRGNRL 

       130        140        150        160        170        180 
HPKYVALILR EAAKSLKQLP NISPVSTAVS QQVTVCGDLH GKLDDLLVVL HKNGLPSSSN 

       190        200        210        220        230        240 
PYVFNGDFVD RGKRGLEVLL LLLSLYLAFP NAVFLNRGNH EDSVMNARYG FIREVESKYP 

       250        260        270        280        290        300 
RNHKRILAFI DEVYRWLPLG SVLNSRVLIV HGGFSDSTSL DLIKSIDRGK YVSILRPPLT 

       310        320        330        340        350        360 
DGEPLDKTEW QQIFDIMWSD PQATMGCVPN TLRGAGVWFG PDVTDNFLQR HRLSYVIRSH 

       370        380        390        400        410        420 
ECKPNGHEFM HDNKIITIFS ASNYYAIGSN KGAYIRLNNQ LMPHFVQYIS AASQTKRLSF 

       430        440        450        460        470        480 
KQRMGIVESS ALKELAVRMR DHRDELEDEF RKYDPKDSGY ISISHWCKVM ENVTKLGLPW 

       490        500        510        520        530        540 
RLLRDKLAPG TDSQKVNYNR TLDLLDTDVI LEAEADGMSV MDALYANKAS LVAIFNIIDA 

       550        560        570        580        590        600 
DNSGEITLDE FETAIDLLVA HMPGAYSKAE MLEKCRMMDL NGDGKVDLNE FLEAFRLSDL 

       610        620        630        640        650        660 
HRKEQQDENI RRRSTGRPSV AKTATDPVTL LADKISKNTL VVEHDIDPTD CESKVIDPKK 


S 

« Hide

Isoform A [UniParc].

Checksum: A2F9A7FB905DEB03
Show »

FASTA60368,180

References

« Hide 'large scale' references
[1]"Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine protein phosphatase."
Steele F.R., Washburn T., Rieger R., O'Tousa J.E.
Cell 69:669-676(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM B), FUNCTION, TISSUE SPECIFICITY.
Strain: Oregon-R.
[2]"The genome sequence of Drosophila melanogaster."
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. expand/collapse author list , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
Strain: Berkeley.
[4]Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
Strain: Berkeley.
Tissue: Head.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M89628 Genomic DNA. Translation: AAB00734.1.
AE014296 Genomic DNA. Translation: AAF49044.2.
AE014296 Genomic DNA. Translation: AAO41217.1.
AE014296 Genomic DNA. Translation: AAO41218.1.
AE014296 Genomic DNA. Translation: AAO41219.1.
BT015959 mRNA. Translation: AAV36844.1.
PIRA42287.
RefSeqNP_536738.2. NM_080490.3.
NP_788544.1. NM_176366.1.
NP_788545.2. NM_176367.2.
UniGeneDm.5730.

3D structure databases

ProteinModelPortalP40421.
SMRP40421. Positions 12-414, 444-596.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid65488. 5 interactions.
IntActP40421. 1 interaction.
MINTMINT-6825050.

Proteomic databases

PaxDbP40421.
PRIDEP40421.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0074833; FBpp0074602; FBgn0004366. [P40421-1]
GeneID40224.
KEGGdme:Dmel_CG6571.

Organism-specific databases

CTD40224.
FlyBaseFBgn0265959. rdgC.

Phylogenomic databases

eggNOGCOG0639.
GeneTreeENSGT00530000063173.
InParanoidP40421.
KOK13807.
OMANMLEYKS.
PhylomeDBP40421.

Enzyme and pathway databases

SignaLinkP40421.

Gene expression databases

BgeeP40421.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000048. IQ_motif_EF-hand-BS.
IPR012008. Ser/Thr-Pase_EF-hand_contain.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
PF00149. Metallophos. 1 hit.
[Graphical view]
PIRSFPIRSF000912. PPEF. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00054. EFh. 3 hits.
SM00015. IQ. 1 hit.
SM00156. PP2Ac. 1 hit.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS50096. IQ. 1 hit.
PS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi40224.
NextBio817660.
PROP40421.

Entry information

Entry nameRDGC_DROME
AccessionPrimary (citable) accession number: P40421
Secondary accession number(s): A4V255, Q5U1D3, Q9VWA4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase