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P23439 (PDE6B_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
Short name=GMP-PDE beta
EC=3.1.4.35
Gene names
Name:PDE6B
Synonyms:PDEB
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length853 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This protein participates in processes of transmission and amplification of the visual signal. Necessary for the formation of a functional phosphodiesterase holoenzyme.

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

Membrane; Lipid-anchor.

Sequence similarities

Belongs to the cyclic nucleotide phosphodiesterase family.

Contains 2 GAF domains.

Ontologies

Keywords
   Biological processSensory transduction
Vision
   Cellular componentMembrane
   DomainRepeat
   LigandMetal-binding
cGMP
   Molecular functionHydrolase
   PTMAcetylation
Lipoprotein
Methylation
Prenylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmetabolic 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_componentmembrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3',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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 850849Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
PRO_0000023344
Propeptide851 – 8533Removed in mature form By similarity
PRO_0000023345

Regions

Domain71 – 220150GAF 1
Domain252 – 429178GAF 2

Sites

Active site5571Proton donor By similarity
Metal binding5611Divalent metal cation 1 By similarity
Metal binding5971Divalent metal cation 1 By similarity
Metal binding5981Divalent metal cation 1 By similarity
Metal binding5981Divalent metal cation 2 By similarity
Metal binding7181Divalent metal cation 1 By similarity

Amino acid modifications

Modified residue21N-acetylserine
Modified residue8501Cysteine methyl ester By similarity
Lipidation8501S-geranylgeranyl cysteine By similarity

Experimental info

Sequence conflict483 – 4842DE → EQ Ref.2

Sequences

Sequence LengthMass (Da)Tools
P23439 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: C4B3F22CFFE7F2FB

FASTA85398,331
        10         20         30         40         50         60 
MSLSEGQVHR FLDQNPGFAD QYFGRKLSPE DVANACEDGC PEGCTSFREL CQVEESAALF 

        70         80         90        100        110        120 
ELVQDMQENV NMERVVFKIL RRLCSILHAD RCSLFMYRQR NGVAELATRL FSVQPDSVLE 

       130        140        150        160        170        180 
DCLVPPDSEI VFPLDIGVVG HVAQTKKMVN VQDVMECPHF SSFADELTDY VTRNILATPI 

       190        200        210        220        230        240 
MNGKDVVAVI MAVNKLDGPC FTSEDEDVFL KYLNFGTLNL KIYHLSYLHN CETRRGQVLL 

       250        260        270        280        290        300 
WSANKVFEEL TDIERQFHKA FYTVRAYLNC DRYSVGLLDM TKEKEFFDVW PVLMGEAQAY 

       310        320        330        340        350        360 
SGPRTPDGRE ILFYKVIDYI LHGKEDIKVI PSPPADHWAL ASGLPTYVAE SGFICNIMNA 

       370        380        390        400        410        420 
PADEMFNFQE GPLDDSGWIV KNVLSMPIVN KKEEIVGVAT FYNRKDGKPF DEQDEVLMES 

       430        440        450        460        470        480 
LTQFLGWSVL NTDTYDKMNK LENRKDIAQD MVLYHVRCDR EEIQLILPTR ERLGKEPADC 

       490        500        510        520        530        540 
EEDELGKILK EVLPGPAKFD IYEFHFSDLE CTELELVKCG IQMYYELGVV RKFQIPQEVL 

       550        560        570        580        590        600 
VRFLFSVSKG YRRITYHNWR HGFNVAQTMF TLLMTGKLKS YYTDLEAFAM VTAGLCHDID 

       610        620        630        640        650        660 
HRGTNNLYQM KSQNPLAKLH GSSILERHHL EFGKFLLSEE TLNIYQNLNR RQHEHVIHLM 

       670        680        690        700        710        720 
DIAIIATDLA LYFKKRTMFQ KIVDESKNYE DRKSWVEYLS LETTRKEIVM AMMMTACDLS 

       730        740        750        760        770        780 
AITKPWEVQS KVALLVAAEF WEQGDLERTV LDQQPIPMMD RNKAAELPKL QVGFIDFVCT 

       790        800        810        820        830        840 
FVYKEFSRFH EEILPMFDRL QNNRKEWKAL ADEYEAKVKA LEEDQKKETT AKKVGTEICN 

       850 
GGPAPRSSTC RIL

« Hide

References

[1]"Beta-subunit of bovine rod photoreceptor cGMP phosphodiesterase. Comparison with the phosphodiesterase family."
Lipkin V.M., Khramtsov N.V., Vasilevskaya I.A., Atabekova N.V., Muradov K.G., Gubanov V.V., Li T., Johnston J.P., Volpp K.J., Applebury M.L.
J. Biol. Chem. 265:12955-12959(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cyclic GMP phosphodiesterase from bovine retina. Amino acid sequence of beta-subunit and nucleotide sequence of corresponding cDNA."
Lipkin V.M., Gubanov V.V., Khramtsov N.V., Vasilevskaya I.A., Atabekova N.V., Muradov K.G., Shuvaeva T.M., Surina E.A., Zagranichny V.E., Li T.
Bioorg. Khim. 16:118-120(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J05553 mRNA. Translation: AAA30440.1.
X57146 mRNA. Translation: CAA40436.1.
IPIIPI00711026.
PIRA36617.
RefSeqNP_776843.1. NM_174418.1.
UniGeneBt.55.

3D structure databases

ProteinModelPortalP23439.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-6824892.
STRING9913.ENSBTAP00000023239.

Proteomic databases

PRIDEP23439.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281974.
KEGGbta:281974.

Organism-specific databases

CTD5158.

Phylogenomic databases

eggNOGNOG242608.
HOGENOMHOG000007069.
HOVERGENHBG053539.
InParanoidP23439.
KOK13756.
OrthoDBEOG44TP77.

Family and domain databases

Gene3D1.10.1300.10. 1 hit.
InterProIPR003018. GAF.
IPR003607. HD/PDEase_dom.
IPR023088. PDEase.
IPR002073. PDEase_catalytic_dom.
IPR023174. PDEase_CS.
[Graphical view]
PfamPF01590. GAF. 2 hits.
PF00233. PDEase_I. 1 hit.
[Graphical view]
PRINTSPR00387. PDIESTERASE1.
SMARTSM00065. GAF. 2 hits.
SM00471. HDc. 1 hit.
[Graphical view]
PROSITEPS00126. PDEASE_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP23439.
ChEMBLCHEMBL2713.
NextBio20805845.

Entry information

Entry namePDE6B_BOVIN
AccessionPrimary (citable) accession number: P23439
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 3, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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