Reviewed, UniProtKB/Swiss-Prot Q28263 (PDE6A_CANFA)

Names and origin

Protein names

Recommended 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:	PDEA

Organism

Canis familiaris (Dog)

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis

Protein attributes

Sequence length	861 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell membrane Membrane
Domain	Repeat
Ligand	Metal-binding cGMP
Molecular function	Hydrolase
PTM	Acetylation Lipoprotein Prenylation
Gene Ontology (GO)
Biological process	response to stimulus Inferred from electronic annotation. Source: UniProtKB-KW signal transduction Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 861	860	Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha		PRO_0000198827
Regions
	Domain	73 – 222	150	GAF 1
	Domain	254 – 431	178	GAF 2
Sites
	Active site	559	1	Proton donor By similarity
	Metal binding	563	1	Divalent metal cation 1 By similarity
	Metal binding	599	1	Divalent metal cation 1 By similarity
	Metal binding	600	1	Divalent metal cation 1 By similarity
	Metal binding	600	1	Divalent metal cation 2 By similarity
	Metal binding	720	1	Divalent metal cation 1 By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylglycine By similarity
	Lipidation	858	1	S-farnesyl cysteine By similarity
Experimental info
	Sequence conflict	388	1	M → L in AAB70037. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q28263-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 8F7DD6C2A891B4E7	FASTA	861	99,688
	10 20 30 40 50 60 MGEVTAEQVE KFLDSNIIFA KQYYNLRYRA KVISDMLGAK EAAVDFSNYH SLSSVEESEI 70 80 90 100 110 120 IFDLLRDFQE NLQAERCIFN VMKKLCFLLQ ADRMSLFMYR VRNGIAELAT RLFNVHKDAV 130 140 150 160 170 180 LEECLVAPDS EIVFPLDMGV VGHVAHSKKI ANVVNTEEDE HFCDFVDTLT EYQTKNILAS 190 200 210 220 230 240 PIMNGKDVVA VIMAVNKVDE PHFTKRDEEI LLKYLNFANL IMKVYHLSYL HNCETRRGQI 250 260 270 280 290 300 LLWSGSKVFE ELTDIERQFH KALYTVRAFL NCDRYSVGLL DMTKQKEFFD VWPVLMGEAP 310 320 330 340 350 360 PYSGPRTPDG REINFYKVID YILHGKEDIK VIPNPPPDHW ALVSGLPTYV AQNGLICNIM 370 380 390 400 410 420 NAPAEDFFAF QKEPLDESGW MIKNVLSMPI VNKKEEIVGV ATFYNRKDGK PFDEMDETLM 430 440 450 460 470 480 ESLAQFLGWS VLNPDTYESM NRLENRKDIF QDMVKYHVKC DNEEIQKILK TREVYGKEPW 490 500 510 520 530 540 ECEEEELAEI LQGELPDAEK 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 MMLEQTRKEI VMAMMMTACD 730 740 750 760 770 780 LSAITKPWEV QSKVALLVAA EFWEQGDLER TVLQQNPIPM MDRNKADELP KLQVGFIDFV 790 800 810 820 830 840 CTFVYKEFSR FHEEITPMLD GITNNRKEWK ALADEYDTKM KALEEEKQKQ QTAKQGAAGD 850 860 QPGGNPSPAG GAPASKSCCI Q

References

[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: 8726673] [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: 9233984] [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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z68340 mRNA. Translation: CAA92763.1. U52868 mRNA. Translation: AAB70037.1. Y13282 mRNA. Translation: CAA73731.1.
RefSeq	NP_001003073.1.
UniGene	Cfa.1198
3D structure databases
SMR	Q28263. Positions 64-444, 483-815.
ModBase	Search...
Protein-protein interaction databases
STRING	Q28263.
Genome annotation databases
Ensembl	ENSCAFT00000028993; ENSCAFP00000026963; ENSCAFG00000018251; Canis familiaris. [Genome view]
GeneID	403620.
KEGG	cfa:403620.
Organism-specific databases
CTD	403620.
Phylogenomic databases
HOVERGEN	Q28263.
OrthoDB	EOG97Q0R3.
PhylomeDB	Q28263.
Enzyme and pathway databases
BRENDA	3.1.4.35. 463.
Family and domain databases
InterPro	IPR003018. GAF. IPR003607. Metal-dep_PHydrolase_HD_dom. IPR002073. PDEase. [Graphical view]
Pfam	PF01590. GAF. 2 hits. PF00233. PDEase_I. 1 hit. [Graphical view]
PRINTS	PR00387. PDIESTERASE1.
SMART	SM00065. GAF. 2 hits. SM00471. HDc. 1 hit. [Graphical view]
PROSITE	PS00126. PDEASE_I. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDE6A_CANFA

Accession

Primary (citable) accession number: Q28263
Secondary accession number(s): Q29470

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)