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Q28263 (PDE6A_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha

Short name=GMP-PDE alpha
EC=3.1.4.35
Gene names
Name:PDE6A
Synonyms:PDEA
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length861 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

This protein participates in processes of transmission and amplification of the visual signal.

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

Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain.

Subcellular location

Cell membrane; Lipid-anchor; Cytoplasmic side Potential.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 858857Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
PRO_0000198827
Propeptide859 – 8613Removed in mature form By similarity
PRO_0000396696

Regions

Domain73 – 222150GAF 1
Domain254 – 431178GAF 2

Sites

Active site5591Proton donor By similarity
Metal binding5631Divalent metal cation 1 By similarity
Metal binding5991Divalent metal cation 1 By similarity
Metal binding6001Divalent metal cation 1 By similarity
Metal binding6001Divalent metal cation 2 By similarity
Metal binding7201Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue21N-acetylglycine By similarity
Modified residue8581Cysteine methyl ester By similarity
Lipidation8581S-farnesyl cysteine By similarity

Experimental info

Sequence conflict3881M → L in AAB70037. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q28263 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 8F7DD6C2A891B4E7

FASTA86199,688
        10         20         30         40         50         60 
MGEVTAEQVE KFLDSNIIFA KQYYNLRYRA KVISDMLGAK EAAVDFSNYH SLSSVEESEI 

        70         80         90        100        110        120 
IFDLLRDFQE NLQAERCIFN VMKKLCFLLQ ADRMSLFMYR VRNGIAELAT RLFNVHKDAV 

       130        140        150        160        170        180 
LEECLVAPDS EIVFPLDMGV VGHVAHSKKI ANVVNTEEDE HFCDFVDTLT EYQTKNILAS 

       190        200        210        220        230        240 
PIMNGKDVVA VIMAVNKVDE PHFTKRDEEI LLKYLNFANL IMKVYHLSYL HNCETRRGQI 

       250        260        270        280        290        300 
LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP 

       310        320        330        340        350        360 
PYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV AQNGLICNIM 

       370        380        390        400        410        420 
NAPAEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDEMDETLM 

       430        440        450        460        470        480 
ESLAQFLGWS VLNPDTYESM NRLENRKDIF QDMVKYHVKC DNEEIQKILK TREVYGKEPW 

       490        500        510        520        530        540 
ECEEEELAEI LQGELPDAEK YEINKFHFSD LPLTELELVK CGIQMYYELK VVDKFHIPQE 

       550        560        570        580        590        600 
ALVRFMYSLS KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD 

       610        620        630        640        650        660 
IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL NRRQHEHAIH 

       670        680        690        700        710        720 
MMDIAIIATD LALYFKKRTM FQKIVDQSKT YETQQEWTQY MMLEQTRKEI VMAMMMTACD 

       730        740        750        760        770        780 
LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV 

       790        800        810        820        830        840 
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYDTKM KALEEEKQKQ QTAKQGAAGD 

       850        860 
QPGGNPSPAG GAPASKSCCI Q 

« Hide

References

[1]"Elevation of cGMP with normal expression and activity of rod cGMP-PDE in photoreceptor degenerate labrador retrievers."
Kommonen B., Kylma T., Cohen R.J., Penn J.S., Paulin L., Hurwitz M., Hurwitz R.L.
Ophthalmic Res. 28:19-28(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Cloning and characterization of the cDNA encoding the alpha-subunit of cGMP-phosphodiesterase in canine retinal rod photoreceptor cells."
Wang W., Acland G.M., Aguirre G.D., Ray K.
Mol. Vis. 2:3-3(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]Veske A., Nilsson S.E.G., Gal A.
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Beagle X Briard.
Tissue: Retina.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z68340 mRNA. Translation: CAA92763.1.
U52868 mRNA. Translation: AAB70037.1.
Y13282 mRNA. Translation: CAA73731.1.
RefSeqNP_001003073.1. NM_001003073.1.
UniGeneCfa.1198.

3D structure databases

ProteinModelPortalQ28263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000011716.

Chemistry

BindingDBQ28263.
ChEMBLCHEMBL5151.

Proteomic databases

PaxDbQ28263.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID403620.
KEGGcfa:403620.

Organism-specific databases

CTD5145.

Phylogenomic databases

eggNOGNOG242608.
HOGENOMHOG000007069.
HOVERGENHBG053539.
KOK08718.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
3.30.450.40. 3 hits.
InterProIPR003018. GAF.
IPR029016. GAF_dom_like.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
SUPFAMSSF55781. SSF55781. 3 hits.
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20817125.

Entry information

Entry namePDE6A_CANFA
AccessionPrimary (citable) accession number: Q28263
Secondary accession number(s): Q29470
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families