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Protein

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

Gene

Pde6a

Organism
Mus musculus (Mouse)
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

  • cytosolic calcium ion homeostasis Source: MGI
  • GMP metabolic process Source: MGI
  • photoreceptor cell maintenance Source: MGI
  • retina development in camera-type eye Source: MGI
  • signal transduction Source: InterPro
  • visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Sensory transduction, Vision

Keywords - Ligandi

cGMP, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_331940. 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:Mpa, Pdea
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:97524. Pde6a.

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 – 856855Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alphaPRO_0000198829Add
BLAST
Propeptidei857 – 8593Removed in mature formBy similarityPRO_0000396698

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei856 – 8561Cysteine methyl esterBy similarity
Lipidationi856 – 8561S-farnesyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiP27664.
PRIDEiP27664.

PTM databases

PhosphoSiteiP27664.

Expressioni

Gene expression databases

CleanExiMM_PDE6A.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025468.

Structurei

3D structure databases

ProteinModelPortaliP27664.
SMRiP27664. Positions 26-815.
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.
HOVERGENiHBG053539.
InParanoidiP27664.

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.

P27664-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEVTAEEVE KFLDSNIGFA KQYYNFHYRG KVISDLLGAK EAAVDFSNYH
60 70 80 90 100
DVNSVEESEI IFDLLRDVQE NLQAEKCTFN VMKKLCFLLR ADRMSLFMYR
110 120 130 140 150
TRNGIAELAT RLFNVHKDAV LEDCLVMPDS EIVFPLDMGV VGHVAHSKKI
160 170 180 190 200
ANVPNTEEDE HFCDFVDNLT EYQTKNILAS PIMNGKDVVA IIMAVNKIDE
210 220 230 240 250
PHFTKRDEEI LLKYLNFVNL IMKVFHLSYL HNCETRRGQI LLWSGSKVFE
260 270 280 290 300
ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP
310 320 330 340 350
AYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPADHW ALVSGLPTYV
360 370 380 390 400
AQNGLICNIM NAPAEDFFEF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV
410 420 430 440 450
ATFYNRKDGK PFDDMDETLM ESLTQFLGWS VLNPDTYESM NKLENRKDIF
460 470 480 490 500
QDIVKYHVKC DNEEIQKILK TREVYGKEPW ECEEEELAEI LQGELPDAES
510 520 530 540 550
YEINKFHFSD LPLTELELVK CGIQMYYELR 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 YESTQEWTQY
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 ALADEYEAKM KALEEEKQKQ QAAKQAASGN QPGGNPLQGA

PASKSCCIQ
Length:859
Mass (Da):99,530
Last modified:July 27, 2011 - v3
Checksum:iE51B8563A1A93526
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti26 – 261F → L in CAA43072 (PubMed:1847109).Curated
Sequence conflicti94 – 941M → V in CAA43072 (PubMed:1847109).Curated
Sequence conflicti348 – 3481T → P in CAA43072 (PubMed:1847109).Curated
Sequence conflicti493 – 4931G → R in CAA43072 (PubMed:1847109).Curated
Sequence conflicti532 – 5321V → W in CAA43072 (PubMed:1847109).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60664 mRNA. Translation: CAA43072.1.
AC121903 Genomic DNA. No translation available.
AC148012 Genomic DNA. No translation available.
PIRiS13030.
UniGeneiMm.391106.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60664 mRNA. Translation: CAA43072.1.
AC121903 Genomic DNA. No translation available.
AC148012 Genomic DNA. No translation available.
PIRiS13030.
UniGeneiMm.391106.

3D structure databases

ProteinModelPortaliP27664.
SMRiP27664. Positions 26-815.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025468.

PTM databases

PhosphoSiteiP27664.

Proteomic databases

MaxQBiP27664.
PRIDEiP27664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:97524. Pde6a.

Phylogenomic databases

eggNOGiNOG242608.
HOVERGENiHBG053539.
InParanoidiP27664.

Enzyme and pathway databases

ReactomeiREACT_331940. Ca2+ pathway.

Miscellaneous databases

PROiP27664.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PDE6A.

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

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.

Entry informationi

Entry nameiPDE6A_MOUSE
AccessioniPrimary (citable) accession number: P27664
Secondary accession number(s): E9Q673
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 126 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.