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P27664 (PDE6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 116. 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·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:Mpa, Pdea
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length859 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 – 856855Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
PRO_0000198829
Propeptide857 – 8593Removed in mature form By similarity
PRO_0000396698

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 residue8561Cysteine methyl ester By similarity
Lipidation8561S-farnesyl cysteine By similarity

Experimental info

Sequence conflict261F → L in CAA43072. Ref.1
Sequence conflict941M → V in CAA43072. Ref.1
Sequence conflict3481T → P in CAA43072. Ref.1
Sequence conflict4931G → R in CAA43072. Ref.1
Sequence conflict5321V → W in CAA43072. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27664 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: E51B8563A1A93526

FASTA85999,530
        10         20         30         40         50         60 
MGEVTAEEVE KFLDSNIGFA KQYYNFHYRG KVISDLLGAK EAAVDFSNYH DVNSVEESEI 

        70         80         90        100        110        120 
IFDLLRDVQE NLQAEKCTFN VMKKLCFLLR ADRMSLFMYR TRNGIAELAT RLFNVHKDAV 

       130        140        150        160        170        180 
LEDCLVMPDS EIVFPLDMGV VGHVAHSKKI ANVPNTEEDE HFCDFVDNLT EYQTKNILAS 

       190        200        210        220        230        240 
PIMNGKDVVA IIMAVNKIDE PHFTKRDEEI LLKYLNFVNL IMKVFHLSYL HNCETRRGQI 

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

       310        320        330        340        350        360 
AYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPADHW ALVSGLPTYV AQNGLICNIM 

       370        380        390        400        410        420 
NAPAEDFFEF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDDMDETLM 

       430        440        450        460        470        480 
ESLTQFLGWS VLNPDTYESM NKLENRKDIF QDIVKYHVKC DNEEIQKILK TREVYGKEPW 

       490        500        510        520        530        540 
ECEEEELAEI LQGELPDAES YEINKFHFSD LPLTELELVK CGIQMYYELR 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 YESTQEWTQY MMLEQTRKEI VMAMMMTACD 

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

       790        800        810        820        830        840 
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYEAKM KALEEEKQKQ QAAKQAASGN 

       850 
QPGGNPLQGA PASKSCCIQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete cDNA sequences of mouse rod photoreceptor cGMP phosphodiesterase alpha- and beta-subunits, and identification of beta'-, a putative beta-subunit isozyme produced by alternative splicing of the beta-subunit gene."
Baehr W., Champagne M.S., Lee A.K., Pittler S.J.
FEBS Lett. 278:107-114(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X60664 mRNA. Translation: CAA43072.1.
AC121903 Genomic DNA. No translation available.
AC148012 Genomic DNA. No translation available.
PIRS13030.
UniGeneMm.391106.

3D structure databases

ProteinModelPortalP27664.
SMRP27664. Positions 26-817.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP27664.

Proteomic databases

MaxQBP27664.
PRIDEP27664.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:97524. Pde6a.

Phylogenomic databases

eggNOGNOG242608.
HOVERGENHBG053539.
InParanoidP27664.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

CleanExMM_PDE6A.
GenevestigatorP27664.

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

PROP27664.
SOURCESearch...

Entry information

Entry namePDE6A_MOUSE
AccessionPrimary (citable) accession number: P27664
Secondary accession number(s): E9Q673
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 116 of the entry and version 3 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot