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Protein

Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'

Gene

PDE6C

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

Guanosine 3',5'-cyclic phosphate + H2O = guanosine 5'-phosphate.

Cofactori

a divalent metal cationBy similarityNote: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971cGMP1 Publication
Binding sitei116 – 1161cGMP1 Publication
Binding sitei176 – 1761cGMP1 Publication
Active sitei562 – 5621Proton donorBy similarity
Metal bindingi566 – 5661Divalent metal cation 1By similarity
Metal bindingi602 – 6021Divalent metal cation 1By similarity
Metal bindingi603 – 6031Divalent metal cation 1By similarity
Metal bindingi603 – 6031Divalent metal cation 2By similarity
Metal bindingi723 – 7231Divalent metal cation 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi169 – 1724cGMP1 Publication

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
  2. cGMP binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. signal transduction Source: InterPro
  2. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

cGMP, cGMP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.4.35. 1306.

Names & Taxonomyi

Protein namesi
Recommended name:
Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha' (EC:3.1.4.35)
Alternative name(s):
cGMP phosphodiesterase 6C
Gene namesi
Name:PDE6C
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539 Componenti: Unplaced

Subcellular locationi

Cell membrane Curated; Lipid-anchor Curated; Cytoplasmic side Curated

GO - Cellular componenti

  1. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 859859Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'PRO_0000198832Add
BLAST
Propeptidei860 – 8623Removed in mature formSequence AnalysisPRO_0000370790

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei859 – 8591Cysteine methyl esterSequence Analysis
Lipidationi859 – 8591S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiP52731.
PRIDEiP52731.

Interactioni

Subunit structurei

Composed of two alpha' subunits that are associated with 3 smaller proteins of 11, 13, and 15 kDa.1 Publication

Protein-protein interaction databases

STRINGi9031.ENSGALP00000010688.

Structurei

Secondary structure

1
862
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi56 – 6611Combined sources
Beta strandi71 – 744Combined sources
Helixi75 – 9117Combined sources
Beta strandi93 – 10412Combined sources
Beta strandi107 – 11711Combined sources
Helixi123 – 1264Combined sources
Helixi130 – 1323Combined sources
Helixi142 – 1498Combined sources
Beta strandi153 – 1564Combined sources
Helixi158 – 1603Combined sources
Helixi167 – 1726Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi189 – 20416Combined sources
Helixi207 – 22317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DBAX-ray2.57A/B55-225[»]
ProteinModelPortaliP52731.
SMRiP52731. Positions 55-225.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP52731.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 224150GAF 1Add
BLAST
Domaini256 – 433178GAF 2Add
BLAST

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG290744.
HOGENOMiHOG000007069.
HOVERGENiHBG053539.
InParanoidiP52731.
KOiK13757.
PhylomeDBiP52731.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P52731-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEVNKDAVE KYLENNPQFA KEYFDRKMRA EVLGSIFQVS PGDVKEGVSF
60 70 80 90 100
KDMSRLEECN ILFELLTEIQ DEAGSMEKIV HKTLQRLSQL LARDRCSMFI
110 120 130 140 150
CRSRNGIPEV ATRLLNVTPT SKFEDNLVNP DKETVFPLDI GIAGWVAHTK
160 170 180 190 200
KFFNIPDVKK NNHFSDYLDK KTGYTTVNMM AIPITQGKEV LAVVMALNKL
210 220 230 240 250
NASEFSKEDE EVFKKYLNFI SLVLRNHHTS YLYNIESRRS QMLLWSANKV
260 270 280 290 300
FEELTDIERQ FHKALYTIRM YLNCERYSVG LLDMTKEKEF YDEWPIRLGE
310 320 330 340 350
AEPYKGPKTP DGREVNFYKI IDYILHGKEE IKVIPTPPAD HWCLISGLPT
360 370 380 390 400
YVAENGFICN MMNAPADEYF TFQKGPVDET GWVIKNVLSL PIVNKKEEIV
410 420 430 440 450
GVATFYNRKD GKPFDEYDEQ IIETLTQFLG WSVLNTDTYD KMNKLENRKD
460 470 480 490 500
IAQEMLMYQT KATPTEVESI LKYKEKLNVK SIEECDEKDL IRILKEELPD
510 520 530 540 550
PKDLELYEFR FSDFPVTEHG LITCGIRLFF EINVVEKFKV PAEVLTRWMY
560 570 580 590 600
TVRKGYRDIT YHNWRHGFNV GQTMFTLLMT GRIKKYYTDL EAFAMVAAAF
610 620 630 640 650
CHDIDHRGTN NLYQMKSAAP LAKLHGSSIL ERHHLEYSKT LLQDESLNIF
660 670 680 690 700
QNLNKRQFET VLHLFEVAII ATDLALYFKK RTMFQKIVDA IEKMETEEEA
710 720 730 740 750
IKYISIDPTK KEVIMAMMMT GCDLSAITKP WEVQSKVALM VANEFWEQGD
760 770 780 790 800
LERTVLQQQP IPMMDRNKGD ELPKLQVGFI DFVCTFVYKE FSRFHKEITP
810 820 830 840 850
MFDGLQNNRV EWKTRADEYE EKMKVIEEQK KKEEEAAAKK AENAAGGGGG
860
GEDGKSKTCI VL
Length:862
Mass (Da):100,009
Last modified:October 1, 1996 - v1
Checksum:iBD3145BB5FF826A8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29233 mRNA. Translation: AAC42223.1.
PIRiI50186.
RefSeqiNP_990317.1. NM_204986.1.
UniGeneiGga.492.

Genome annotation databases

GeneIDi395834.
KEGGigga:395834.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29233 mRNA. Translation: AAC42223.1.
PIRiI50186.
RefSeqiNP_990317.1. NM_204986.1.
UniGeneiGga.492.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3DBAX-ray2.57A/B55-225[»]
ProteinModelPortaliP52731.
SMRiP52731. Positions 55-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000010688.

Proteomic databases

PaxDbiP52731.
PRIDEiP52731.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi395834.
KEGGigga:395834.

Organism-specific databases

CTDi5146.

Phylogenomic databases

eggNOGiNOG290744.
HOGENOMiHOG000007069.
HOVERGENiHBG053539.
InParanoidiP52731.
KOiK13757.
PhylomeDBiP52731.

Enzyme and pathway databases

BRENDAi3.1.4.35. 1306.

Miscellaneous databases

EvolutionaryTraceiP52731.
NextBioi20815902.
PROiP52731.

Family and domain databases

Gene3Di1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProiIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamiPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSiPR00387. PDIESTERASE1.
SMARTiSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMiSSF55781. SSF55781. 3 hits.
PROSITEiPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Molecular characterization of the alpha'-subunit of cone photoreceptor cGMP phosphodiesterase in normal and rd chicken."
    Semple-Rowland S.L., Green D.A.
    Exp. Eye Res. 59:365-372(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Rhode Island red.
    Tissue: Retina.
  2. "The structure of the GAF A domain from phosphodiesterase 6C reveals determinants of cGMP binding, a conserved binding surface, and a large cGMP-dependent conformational change."
    Martinez S.E., Heikaus C.C., Klevit R.E., Beavo J.A.
    J. Biol. Chem. 283:25913-25919(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 55-225 IN COMPLEX WITH CGMP.

Entry informationi

Entry nameiPDE6C_CHICK
AccessioniPrimary (citable) accession number: P52731
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 1, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.