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P20942 (PHOS_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosducin

Short name=PHD
Alternative name(s):
33 kDa phototransducing protein
Protein MEKA
Rod photoreceptor 1
Short name=RPR-1
Gene names
Name:Pdc
Synonyms:Rpr1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May participate in the regulation of visual phototransduction or in the integration of photoreceptor metabolism.

Subunit structure

Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin.

Subcellular location

Cytoplasmcytosol. Cell projectionciliumphotoreceptor outer segment. Photoreceptor inner segment. Note: Outer and inner segments of the rod cells.

Post-translational modification

Light-induced changes in cyclic nucleotide levels modulate the phosphorylation of this protein by cAMP kinase.

Sequence similarities

Belongs to the phosducin family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Phosducin
PRO_0000163754

Amino acid modifications

Modified residue731Phosphoserine; by PKA Ref.1

Natural variations

Natural variant1911V → I.

Experimental info

Sequence conflict391G → S in AAA41841. Ref.2
Sequence conflict881G → V in AAA41841. Ref.2
Sequence conflict1191T → S in AAA41841. Ref.2
Sequence conflict2111D → E in AAA41841. Ref.2

Secondary structure

................................... 246
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20942 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 3C48ABCB4E5E3D04

FASTA24628,129
        10         20         30         40         50         60 
MEEAASQSLE EDFEGQATHT GPKGVINDWR KFKLESEDGD SIPPSKKEIL RQMSSPQSRD 

        70         80         90        100        110        120 
DKDSKERMSR KMSIQEYELI HQDKEDEGCL RKYRRQCMQD MHQKLSFGPR YGFVYELETG 

       130        140        150        160        170        180 
EQFLETIEKE QKVTTIVVNI YEDGVRGCDA LNSSLECLAA EYPMVKFCKI RASNTGAGDR 

       190        200        210        220        230        240 
FSSDVLPTLL VYKGGELISN FISVAEQFAE DFFAADVESF LNEYGLLPER EIHDLGQTNT 


EDEDIE 

« Hide

References

[1]"Analysis of the human, bovine and rat 33-kDa proteins and cDNA in retina and pineal gland."
Abe T., Nakabayashi H., Tamada H., Takagi T., Sakuragi S., Yamaki K., Shinohara T.
Gene 91:209-215(1990) [PubMed: 2210381] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Pineal gland and Retina.
[2]"Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and chromosomal assignment in the mouse."
Craft C.M., Lolley R.N., Seldin M.F., Lee R.H.
Genomics 10:400-409(1991) [PubMed: 2071146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Pineal gland.
[3]"A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G-proteins by phosducin. Structural analysis of phosducin and its phosphorylation-regulated interaction with transducin beta-gamma."
Gaudet R., Savage J.R., McLaughlin J.N., Willardson B.M., Sigler P.B.
Mol. Cell 3:649-660(1999) [PubMed: 10360181] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH G-BETA AND G-GAMMA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33528 mRNA. Translation: AAA40604.1.
M33530 mRNA. Translation: AAA40603.1.
M60738 mRNA. Translation: AAA41841.1.
IPIIPI00326074.
PIRA39903.
JH0216.
RefSeqNP_037004.1. NM_012872.1.
UniGeneRn.9739.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B9XX-ray3.00C1-246[»]
1B9YX-ray3.00C1-246[»]
2TRCX-ray2.40P14-230[»]
ProteinModelPortalP20942.
SMRP20942. Positions 14-230.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-41816N.
MINTMINT-197623.
STRINGP20942.

PTM databases

PhosphoSiteP20942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000003405; ENSRNOP00000003405; ENSRNOG00000002517.
GeneID25343.
KEGGrno:25343.
UCSCNM_012872. rat.

Organism-specific databases

CTD5132.
RGD3277. Pdc.

Phylogenomic databases

eggNOGroNOG04594.
GeneTreeENSGT00530000062970.
HOVERGENHBG003456.
InParanoidP20942.
OMANEYGLLP.
OrthoDBEOG4RBQKG.
PhylomeDBP20942.

Gene expression databases

ArrayExpressP20942.
GenevestigatorP20942.
GermOnlineENSRNOG00000002517. Rattus norvegicus.

Family and domain databases

InterProIPR001200. Phosducin.
IPR023196. Phosducin_dom2.
IPR024253. Phosducin_thioredoxin-like_dom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
Gene3DG3DSA:1.10.168.10. Phosducin_dom2. 1 hit.
G3DSA:3.40.30.10. Thioredoxin_fold. 1 hit.
KOK08327.
PfamPF02114. Phosducin. 1 hit.
[Graphical view]
PRINTSPR00677. PHOSDUCIN.
SUPFAMSSF52833. Thiordxn-like_fd. 1 hit.
ProtoNetSearch...

Other

NextBio606259.

Entry information

Entry namePHOS_RAT
AccessionPrimary (citable) accession number: P20942
Secondary accession number(s): Q63420
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: November 16, 2011
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families