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Protein

Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma

Gene

PDE6G

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Participates in processes of transmission and amplification of the visual signal. cGMP-PDEs are the effector molecules in G-protein-mediated phototransduction in vertebrate rods and cones.

Catalytic activityi

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

GO - Molecular functioni

  1. 3',5'-cyclic-GMP phosphodiesterase activity Source: UniProtKB-EC
  2. cGMP binding Source: InterPro

GO - Biological processi

  1. activation of MAPK activity Source: Ensembl
  2. positive regulation of epidermal growth factor receptor signaling pathway Source: Ensembl
  3. positive regulation of G-protein coupled receptor protein signaling pathway Source: Ensembl
  4. response to stimulus Source: UniProtKB-KW
  5. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

cGMP

Enzyme and pathway databases

ReactomeiREACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_209727. Ca2+ pathway.
REACT_211562. Activation of the phototransduction cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (EC:3.1.4.35)
Short name:
GMP-PDE gamma
Gene namesi
Name:PDE6G
Synonyms:PDEG
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Chromosome 19

Subcellular locationi

GO - Cellular componenti

  1. photoreceptor disc membrane Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8787Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gammaPRO_0000166113Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine

Keywords - PTMi

Acetylation

Interactioni

Subunit structurei

Oligomer composed of two catalytic chains (alpha and beta), an inhibitory chain (gamma) and the delta chain.1 Publication

Protein-protein interaction databases

IntActiP04972. 2 interactions.
STRINGi9913.ENSBTAP00000000459.

Structurei

Secondary structure

1
87
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 174Combined sources
Beta strandi24 – 274Combined sources
Beta strandi34 – 374Combined sources
Beta strandi45 – 484Combined sources
Beta strandi56 – 594Combined sources
Helixi62 – 654Combined sources
Helixi69 – 735Combined sources
Helixi78 – 836Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQJX-ray2.02C46-87[»]
2JU4NMR-A1-87[»]
DisProtiDP00347.
DP00638.
ProteinModelPortaliP04972.
SMRiP04972. Positions 1-87.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04972.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi24 – 4522Arg/Lys-rich (basic)Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG44345.
GeneTreeiENSGT00390000013260.
HOVERGENiHBG000447.
InParanoidiP04972.
KOiK13759.
OMAiDCSRRES.
OrthoDBiEOG7SN8FW.
TreeFamiTF333297.

Family and domain databases

Gene3Di4.10.1120.10. 1 hit.
InterProiIPR006952. PDE6_gamma.
[Graphical view]
PANTHERiPTHR12122. PTHR12122. 1 hit.
PfamiPF04868. PDE6_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF000969. 35-cGMP_Pdiase_g. 1 hit.

Sequencei

Sequence statusi: Complete.

P04972-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLEPPKAEI RSATRVMGGP VTPRKGPPKF KQRQTRQFKS KPPKKGVQGF
60 70 80
GDDIPGMEGL GTDITVICPW EAFNHLELHE LAQYGII
Length:87
Mass (Da):9,669
Last modified:August 13, 1987 - v1
Checksum:i3AA2D6B5D7D14D58
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04823 mRNA. Translation: CAA28507.1.
X04270 mRNA. Translation: CAA27821.1.
PIRiA25268.
RefSeqiNP_776846.1. NM_174421.2.
XP_010814750.1. XM_010816448.1.
XP_010814751.1. XM_010816449.1.
UniGeneiBt.54.

Genome annotation databases

EnsembliENSBTAT00000000459; ENSBTAP00000000459; ENSBTAG00000000354.
GeneIDi281977.
KEGGibta:281977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04823 mRNA. Translation: CAA28507.1.
X04270 mRNA. Translation: CAA27821.1.
PIRiA25268.
RefSeqiNP_776846.1. NM_174421.2.
XP_010814750.1. XM_010816448.1.
XP_010814751.1. XM_010816449.1.
UniGeneiBt.54.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FQJX-ray2.02C46-87[»]
2JU4NMR-A1-87[»]
DisProtiDP00347.
DP00638.
ProteinModelPortaliP04972.
SMRiP04972. Positions 1-87.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP04972. 2 interactions.
STRINGi9913.ENSBTAP00000000459.

Chemistry

ChEMBLiCHEMBL2096979.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000000459; ENSBTAP00000000459; ENSBTAG00000000354.
GeneIDi281977.
KEGGibta:281977.

Organism-specific databases

CTDi5148.

Phylogenomic databases

eggNOGiNOG44345.
GeneTreeiENSGT00390000013260.
HOVERGENiHBG000447.
InParanoidiP04972.
KOiK13759.
OMAiDCSRRES.
OrthoDBiEOG7SN8FW.
TreeFamiTF333297.

Enzyme and pathway databases

ReactomeiREACT_209198. Inactivation, recovery and regulation of the phototransduction cascade.
REACT_209727. Ca2+ pathway.
REACT_211562. Activation of the phototransduction cascade.

Miscellaneous databases

EvolutionaryTraceiP04972.
NextBioi20805848.

Family and domain databases

Gene3Di4.10.1120.10. 1 hit.
InterProiIPR006952. PDE6_gamma.
[Graphical view]
PANTHERiPTHR12122. PTHR12122. 1 hit.
PfamiPF04868. PDE6_gamma. 1 hit.
[Graphical view]
PIRSFiPIRSF000969. 35-cGMP_Pdiase_g. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Cyclic GMP-phosphodiesterase from the cattle retina. Amino acid sequence of the gamma subunit."
    Ovchinnikov Y.A., Muradov K.G., Feigina M.Y., Nazimov I.V., Khoroshilova N.I.
    Dokl. Akad. Nauk SSSR 287:1496-1498(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.
    Tissue: Retina.
  2. "Cyclic GMP phosphodiesterase from bovine retina. Nucleotide sequence of cDNA of the gamma-subunit."
    Ovchinnikov Y.A., Gubanov V.V., Khramtsov N.V., Akhmedov N.B., Zagranichny V.E., Ishchenko K.A., Muradov K.G., Barinov A.A., Bondarenko V.A., Kumarev V.P., Kobzev V.F., Lipkin V.M.
    Dokl. Biochem. 288:216-218(1986)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "Cyclic GMP phosphodiesterase from cattle retina. Amino acid sequence of the gamma-subunit and nucleotide sequence of the corresponding cDNA."
    Ovchinnikov Y.A., Lipkin V.M., Kumarev V.P., Gubanov V.V., Khramtsov N.V., Akhmedov N.B., Zagranichny V.E., Muradov K.G.
    FEBS Lett. 204:288-292(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  4. "Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A."
    Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., Sigler P.B.
    Nature 409:1071-1077(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 46-87 IN COMPLEX WITH RGS9 AND GNAT1.

Entry informationi

Entry nameiCNRG_BOVIN
AccessioniPrimary (citable) accession number: P04972
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: March 4, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.