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

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P11541 (PDE6A_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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

Alternative name(s):
PDE V-B1

Gene names

Name:	PDE6A
Synonyms:	PDEA

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	859 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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

Keywords
Biological process	Sensory transduction Vision
Cellular component	Cell membrane Membrane
Domain	Repeat
Ligand	Metal-binding cGMP
Molecular function	Hydrolase
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC signal transduction Inferred from electronic annotation. Source: InterPro visual perception Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	3',5'-cyclic-GMP phosphodiesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 856

855

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

PRO_0000198826

Propeptide

857 – 859

Removed in mature form By similarity

PRO_0000396695

Regions

Domain

73 – 222

150

GAF 1

Domain

254 – 431

178

GAF 2

Sites

Active site

559

Proton donor By similarity

Metal binding

563

Divalent metal cation 1 By similarity

Metal binding

599

Divalent metal cation 1 By similarity

Metal binding

600

Divalent metal cation 1 By similarity

Metal binding

600

Divalent metal cation 2 By similarity

Metal binding

720

Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue

N-acetylglycine Ref.3

Modified residue

856

Cysteine methyl ester By similarity

Lipidation

856

S-farnesyl cysteine By similarity

Natural variations

Natural variant

381

M → V.

Experimental info

Sequence conflict

194

V → A Ref.2

Sequence conflict

194

V → A Ref.3

Sequence conflict

424

T → A Ref.2

Sequence conflict

424

T → A Ref.3

Sequence conflict

675

F → C Ref.2

Sequence conflict

675

F → C Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P11541 [UniParc].

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

FASTA

859

99,341

        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.
IPI	IPI00690805.
PIR	S06418.
RefSeq	NP_001001526.2. NM_001001526.2.
UniGene	Bt.4147.
3D structure databases
ProteinModelPortal	P11541.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-6824874.
STRING	9913.ENSBTAP00000017199.
Proteomic databases
PRIDE	P11541.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	281973.
KEGG	bta:281973.
Organism-specific databases
CTD	5145.
Phylogenomic databases
eggNOG	NOG242608.
HOGENOM	HOG000007069.
HOVERGEN	HBG053539.
InParanoid	P11541.
KO	K08718.
OrthoDB	EOG44TP77.
Enzyme and pathway databases
BioCyc	CATTLE:281973-MONOMER.
Family and domain databases
Gene3D	1.10.1300.10. 1 hit.
InterPro	IPR003018. GAF. IPR003607. HD/PDEase_dom. IPR023088. PDEase. IPR002073. PDEase_catalytic_dom. IPR023174. PDEase_CS. [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...
Other
BindingDB	P11541.
ChEMBL	CHEMBL3741.
NextBio	20805844.

Entry information

Entry name

PDE6A_BOVIN

Accession

Primary (citable) accession number: P11541

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 105 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Other

Entry information

Relevant documents