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Reviewed, UniProtKB/Swiss-Prot P23439 (PDE6B_BOVIN)

Last modified January 19, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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
Gene Ontology (GO)
   Biological processsignal transduction

Inferred from electronic annotation. Source: InterPro

visual perception

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentanchored to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3',5'-cyclic-GMP phosphodiesterase activity

Inferred from electronic annotation. Source: EC

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
P23439-1 [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: 2165490] [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: 2161230] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

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

3D structure databases

SMRP23439. Positions 481-813.
ModBaseSearch...

Protein-protein interaction databases

STRINGP23439.

Genome annotation databases

EnsemblENSBTAT00000023239; ENSBTAP00000023239; ENSBTAG00000017480; Bos taurus. [Genome view]
GeneID281974.
KEGGbta:281974.

Organism-specific databases

CTD281974.

Phylogenomic databases

eggNOGmaNOG07458.
HOVERGENP23439.
InParanoidP23439.

Enzyme and pathway databases

BRENDA3.1.4.35. 251.

Family and domain databases

InterProIPR003018. GAF.
IPR003607. Metal-dep_PHydrolase_HD_dom.
IPR002073. PDEase.
[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...

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: January 19, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents