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P11541 (PDE6A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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
Alternative name(s):
PDE V-B1
Gene names
Name:PDE6A
Synonyms:PDEA
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length859 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 856855Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
PRO_0000198826
Propeptide857 – 8593Removed in mature form By similarity
PRO_0000396695

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 Ref.3
Modified residue8561Cysteine methyl ester By similarity
Lipidation8561S-farnesyl cysteine By similarity

Natural variations

Natural variant3811M → V.

Experimental info

Sequence conflict1941V → A Ref.2
Sequence conflict1941V → A Ref.3
Sequence conflict4241T → A Ref.2
Sequence conflict4241T → A Ref.3
Sequence conflict6751F → C Ref.2
Sequence conflict6751F → C Ref.3

Sequences

Sequence LengthMass (Da)Tools
P11541 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 701CB148F73A1303

FASTA85999,341
        10         20         30         40         50         60 
MGEVTAEEVE KFLDSNVSFA KQYYNLRYRA KVISDLLGPR EAAVDFSNYH ALNSVEESEI 

        70         80         90        100        110        120 
IFDLLRDFQD NLQAEKCVFN VMKKLCFLLQ ADRMSLFMYR ARNGIAELAT RLFNVHKDAV 

       130        140        150        160        170        180 
LEECLVAPDS EIVFPLDMGV VGHVALSKKI VNVPNTEEDE HFCDFVDTLT EYQTKNILAS 

       190        200        210        220        230        240 
PIMNGKDVVA IIMVVNKVDG PHFTENDEEI LLKYLNFANL IMKVFHLSYL HNCETRRGQI 

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

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

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

       430        440        450        460        470        480 
ESLTQFLGWS VLNPDTYELM NKLENRKDIF QDMVKYHVKC DNEEIQTILK TREVYGKEPW 

       490        500        510        520        530        540 
ECEEEELAEI LQGELPDADK 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 MMLDQTRKEI VMAMMMTACD 

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

       790        800        810        820        830        840 
CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYETKM KGLEEEKQKQ QAANQAAAGS 

       850 
QHGGKQPGGG PASKSCCVQ 

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References

[1]"Molecular characterization of human and bovine rod photoreceptor cGMP phosphodiesterase alpha-subunit and chromosomal localization of the human gene."
Pittler S.J., Baehr W., Wasmuth J.J., McConnell D.G., Champagne M.S., VanTuinen P., Ledbetter D., Davis R.L.
Genomics 6:272-283(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cyclic GMP phosphodiesterase from the bovine retina. Amino acid sequence of the alpha-subunit and nucleotide sequence of corresponding cDNA."
Yu A., Ovchinnikov A., Gubanov V.V., Khramtsov N.V., Akhmedov N.B., Ishchenko K.A., Zagranichnyi V.E., Vasilevskaya I.A., Rakitina T.V., Atabekova N.V., Barinov A.A., Muradov K.G., Shuvaeva T.M., Bystrov N.S., Severtsova I.V., Lipkin V.M.
Dokl. Akad. Nauk SSSR 296:487-491(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.
[3]"Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of the alpha-subunit and nucleotide sequence of the corresponding cDNA."
Ovchinnikov Y.A., Gubanov V.V., Khramtsov N.V., Ischenko K.A., Zagranichny V.E., Muradov K.G., Shuvaeva T.M., Lipkin V.M.
FEBS Lett. 223:169-173(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION AT GLY-2.
Tissue: Retina.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X12756 mRNA. Translation: CAA31243.1.
M27541 mRNA. Translation: AAA30441.1.
M36683 mRNA. Translation: AAA30442.1.
M26043 mRNA. Translation: AAA30443.1.
PIRS06418.
RefSeqNP_001001526.2. NM_001001526.2.
UniGeneBt.4147.

3D structure databases

ProteinModelPortalP11541.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP11541. 2 interactions.
MINTMINT-6824874.
STRING9913.ENSBTAP00000017199.

Chemistry

BindingDBP11541.
ChEMBLCHEMBL3741.

Proteomic databases

PRIDEP11541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281973.
KEGGbta:281973.

Organism-specific databases

CTD5145.

Phylogenomic databases

eggNOGNOG242608.
HOGENOMHOG000007069.
HOVERGENHBG053539.
InParanoidP11541.
KOK08718.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003018. GAF.
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]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805844.

Entry information

Entry namePDE6A_BOVIN
AccessionPrimary (citable) accession number: P11541
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 111 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