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P52731 (PDE6C_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
EC=3.1.4.35
Alternative name(s):
cGMP phosphodiesterase 6C
Gene names
Name:PDE6C
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length862 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

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.

Subunit structure

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

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentCell membrane
Membrane
   DomainRepeat
   LigandMetal-binding
Nucleotide-binding
cGMP
cGMP-binding
   Molecular functionHydrolase
   PTMLipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processvisual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: EC

cGMP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 859859Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
PRO_0000198832
Propeptide860 – 8623Removed in mature form Potential
PRO_0000370790

Regions

Domain75 – 224150GAF 1
Domain256 – 433178GAF 2
Nucleotide binding169 – 1724cGMP

Sites

Active site5621Proton donor By similarity
Metal binding5661Divalent metal cation 1 By similarity
Metal binding6021Divalent metal cation 1 By similarity
Metal binding6031Divalent metal cation 1 By similarity
Metal binding6031Divalent metal cation 2 By similarity
Metal binding7231Divalent metal cation 1 By similarity
Binding site971cGMP
Binding site1161cGMP
Binding site1761cGMP

Amino acid modifications

Modified residue8591Cysteine methyl ester Potential
Lipidation8591S-geranylgeranyl cysteine By similarity

Secondary structure

1 ........................... 862
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P52731 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: BD3145BB5FF826A8

FASTA862100,009
        10         20         30         40         50         60 
MGEVNKDAVE KYLENNPQFA KEYFDRKMRA EVLGSIFQVS PGDVKEGVSF KDMSRLEECN 

        70         80         90        100        110        120 
ILFELLTEIQ DEAGSMEKIV HKTLQRLSQL LARDRCSMFI CRSRNGIPEV ATRLLNVTPT 

       130        140        150        160        170        180 
SKFEDNLVNP DKETVFPLDI GIAGWVAHTK KFFNIPDVKK NNHFSDYLDK KTGYTTVNMM 

       190        200        210        220        230        240 
AIPITQGKEV LAVVMALNKL NASEFSKEDE EVFKKYLNFI SLVLRNHHTS YLYNIESRRS 

       250        260        270        280        290        300 
QMLLWSANKV FEELTDIERQ FHKALYTIRM YLNCERYSVG LLDMTKEKEF YDEWPIRLGE 

       310        320        330        340        350        360 
AEPYKGPKTP DGREVNFYKI IDYILHGKEE IKVIPTPPAD HWCLISGLPT YVAENGFICN 

       370        380        390        400        410        420 
MMNAPADEYF TFQKGPVDET GWVIKNVLSL PIVNKKEEIV GVATFYNRKD GKPFDEYDEQ 

       430        440        450        460        470        480 
IIETLTQFLG WSVLNTDTYD KMNKLENRKD IAQEMLMYQT KATPTEVESI LKYKEKLNVK 

       490        500        510        520        530        540 
SIEECDEKDL IRILKEELPD PKDLELYEFR FSDFPVTEHG LITCGIRLFF EINVVEKFKV 

       550        560        570        580        590        600 
PAEVLTRWMY TVRKGYRDIT YHNWRHGFNV GQTMFTLLMT GRIKKYYTDL EAFAMVAAAF 

       610        620        630        640        650        660 
CHDIDHRGTN NLYQMKSAAP LAKLHGSSIL ERHHLEYSKT LLQDESLNIF QNLNKRQFET 

       670        680        690        700        710        720 
VLHLFEVAII ATDLALYFKK RTMFQKIVDA IEKMETEEEA IKYISIDPTK KEVIMAMMMT 

       730        740        750        760        770        780 
GCDLSAITKP WEVQSKVALM VANEFWEQGD LERTVLQQQP IPMMDRNKGD ELPKLQVGFI 

       790        800        810        820        830        840 
DFVCTFVYKE FSRFHKEITP MFDGLQNNRV EWKTRADEYE EKMKVIEEQK KKEEEAAAKK 

       850        860 
AENAAGGGGG GEDGKSKTCI VL

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References

[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(1994) [PubMed: 7821382] [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(2008) [PubMed: 18614542] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 55-225 IN COMPLEX WITH CGMP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L29233 mRNA. Translation: AAC42223.1.
IPIIPI00582931.
PIRI50186.
RefSeqNP_990317.1. NM_204986.1.
UniGeneGga.492.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DBAX-ray2.57A/B55-225[»]
ProteinModelPortalP52731.
SMRP52731. Positions 55-225.
ModBaseSearch...

Protein-protein interaction databases

STRINGP52731.

Proteomic databases

PRIDEP52731.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID395834.
KEGGgga:395834.

Organism-specific databases

CTD5146.

Phylogenomic databases

eggNOGveNOG09589.
GeneTreeENSGT00550000074280.
HOGENOMHBG445272.
HOVERGENHBG053539.
InParanoidP52731.
OrthoDBEOG40GCQ6.

Family and domain databases

InterProIPR003018. GAF.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
Gene3DG3DSA:1.10.1300.10. PDEase_catalytic_dom. 1 hit.
KOK13757.
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePDE6C_CHICK
AccessionPrimary (citable) accession number: P52731
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 16, 2011
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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