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Protein

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

Gene

PDE6A

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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

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
Active sitei559 – 5591Proton donorBy similarity
Metal bindingi563 – 5631Divalent metal cation 1By similarity
Metal bindingi599 – 5991Divalent metal cation 1By similarity
Metal bindingi600 – 6001Divalent metal cation 1By similarity
Metal bindingi600 – 6001Divalent metal cation 2By similarity
Metal bindingi720 – 7201Divalent metal cation 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_313434. Activation of the phototransduction cascade.
REACT_324552. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_346553. Ca2+ pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha (EC:3.1.4.35)
Short name:
GMP-PDE alpha
Gene namesi
Name:PDE6A
Synonyms:PDEA
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 858857Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alphaPRO_0000198827Add
BLAST
Propeptidei859 – 8613Removed in mature formBy similarityPRO_0000396696

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei858 – 8581Cysteine methyl esterBy similarity
Lipidationi858 – 8581S-farnesyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

PaxDbiQ28263.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000026963.

Structurei

3D structure databases

ProteinModelPortaliQ28263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini73 – 222150GAF 1Add
BLAST
Domaini254 – 431178GAF 2Add
BLAST

Sequence similaritiesi

Contains 2 GAF domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG242608.
HOGENOMiHOG000007069.
HOVERGENiHBG053539.
InParanoidiQ28263.
KOiK08718.

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.

Q28263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEVTAEQVE KFLDSNIIFA KQYYNLRYRA KVISDMLGAK EAAVDFSNYH
60 70 80 90 100
SLSSVEESEI IFDLLRDFQE NLQAERCIFN VMKKLCFLLQ ADRMSLFMYR
110 120 130 140 150
VRNGIAELAT RLFNVHKDAV LEECLVAPDS EIVFPLDMGV VGHVAHSKKI
160 170 180 190 200
ANVVNTEEDE HFCDFVDTLT EYQTKNILAS PIMNGKDVVA VIMAVNKVDE
210 220 230 240 250
PHFTKRDEEI LLKYLNFANL IMKVYHLSYL HNCETRRGQI LLWSGSKVFE
260 270 280 290 300
ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
310 320 330 340 350
PYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV
360 370 380 390 400
AQNGLICNIM NAPAEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV
410 420 430 440 450
ATFYNRKDGK PFDEMDETLM ESLAQFLGWS VLNPDTYESM NRLENRKDIF
460 470 480 490 500
QDMVKYHVKC DNEEIQKILK TREVYGKEPW ECEEEELAEI LQGELPDAEK
510 520 530 540 550
YEINKFHFSD LPLTELELVK CGIQMYYELK VVDKFHIPQE ALVRFMYSLS
560 570 580 590 600
KGYRRITYHN WRHGFNVGQT MFSLLVTGKL KRYFTDLEAL AMVTAAFCHD
610 620 630 640 650
IDHRGTNNLY QMKSQNPLAK LHGSSILERH HLEFGKTLLR DESLNIFQNL
660 670 680 690 700
NRRQHEHAIH MMDIAIIATD LALYFKKRTM FQKIVDQSKT YETQQEWTQY
710 720 730 740 750
MMLEQTRKEI VMAMMMTACD LSAITKPWEV QSKVALLVAA EFWEQGDLER
760 770 780 790 800
TVLQQNPIPM MDRNKADELP KLQVGFIDFV CTFVYKEFSR FHEEITPMLD
810 820 830 840 850
GITNNRKEWK ALADEYDTKM KALEEEKQKQ QTAKQGAAGD QPGGNPSPAG
860
GAPASKSCCI Q
Length:861
Mass (Da):99,688
Last modified:January 23, 2007 - v2
Checksum:i8F7DD6C2A891B4E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti388 – 3881M → L in AAB70037 (PubMed:9233984).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68340 mRNA. Translation: CAA92763.1.
U52868 mRNA. Translation: AAB70037.1.
Y13282 mRNA. Translation: CAA73731.1.
RefSeqiNP_001003073.1. NM_001003073.1.
UniGeneiCfa.1198.

Genome annotation databases

GeneIDi403620.
KEGGicfa:403620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68340 mRNA. Translation: CAA92763.1.
U52868 mRNA. Translation: AAB70037.1.
Y13282 mRNA. Translation: CAA73731.1.
RefSeqiNP_001003073.1. NM_001003073.1.
UniGeneiCfa.1198.

3D structure databases

ProteinModelPortaliQ28263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000026963.

Chemistry

BindingDBiQ28263.
ChEMBLiCHEMBL5151.

Proteomic databases

PaxDbiQ28263.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403620.
KEGGicfa:403620.

Organism-specific databases

CTDi5145.

Phylogenomic databases

eggNOGiNOG242608.
HOGENOMiHOG000007069.
HOVERGENiHBG053539.
InParanoidiQ28263.
KOiK08718.

Enzyme and pathway databases

ReactomeiREACT_313434. Activation of the phototransduction cascade.
REACT_324552. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_346553. Ca2+ pathway.

Miscellaneous databases

NextBioi20817125.
PROiQ28263.

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. "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.

Entry informationi

Entry nameiPDE6A_CANFA
AccessioniPrimary (citable) accession number: Q28263
Secondary accession number(s): Q29470
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.