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Protein

Phosducin-like protein

Gene

Pdcl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as a co-chaperone for CCT in the assembly of heterotrimeric G protein complexes, facilitates the assembly of both Gbeta-Ggamma and RGS-Gbeta5 heterodimers.1 Publication

GO - Molecular functioni

GO - Biological processi

  • heterotrimeric G-protein complex assembly Source: MGI
  • negative regulation of protein refolding Source: Ensembl
  • protein folding Source: Ensembl
  • queuosine biosynthetic process Source: GO_Central
  • response to stimulus Source: UniProtKB-KW
  • visual perception Source: MGI

Keywordsi

Molecular functionChaperone
Biological processSensory transduction, Vision

Enzyme and pathway databases

ReactomeiR-MMU-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosducin-like protein
Short name:
PHLP
Gene namesi
Name:Pdcl
Synonyms:PhLP1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914716. Pdcl.

Subcellular locationi

Pathology & Biotechi

Disruption phenotypei

Conditional deletion in photoreceptor cells leads to 50-fold decrease in Gbeta-Ggamma dimer formation and more than 10-fold decrease in light sensitivity. A 20-fold reduction in Gbeta5 and RGS9-1 expression is also observed, causing a 15-fold delay in the shutoff of light responses.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001637562 – 301Phosducin-like proteinAdd BLAST300

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineBy similarity1
Modified residuei20PhosphoserineBy similarity1
Modified residuei25PhosphoserineCombined sources1
Modified residuei226PhosphoserineBy similarity1
Modified residuei293PhosphoserineBy similarity1
Modified residuei296PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DBX2.
MaxQBiQ9DBX2.
PaxDbiQ9DBX2.
PRIDEiQ9DBX2.

PTM databases

iPTMnetiQ9DBX2.
PhosphoSitePlusiQ9DBX2.

Expressioni

Gene expression databases

BgeeiENSMUSG00000009030.
CleanExiMM_PDCL.
ExpressionAtlasiQ9DBX2. baseline and differential.
GenevisibleiQ9DBX2. MM.

Interactioni

Subunit structurei

Forms a complex with the beta and gamma subunits of the GTP-binding protein, transducin. Interacts with the CCT chaperonin complex (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000009174.

Structurei

3D structure databases

ProteinModelPortaliQ9DBX2.
SMRiQ9DBX2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni158 – 301Thioredoxin foldBy similarityAdd BLAST144

Sequence similaritiesi

Belongs to the phosducin family.Curated

Phylogenomic databases

eggNOGiKOG3171. Eukaryota.
ENOG4110DRD. LUCA.
GeneTreeiENSGT00530000062970.
HOGENOMiHOG000232010.
HOVERGENiHBG003456.
InParanoidiQ9DBX2.
OMAiPSIKFAK.
OrthoDBiEOG091G0ISM.
PhylomeDBiQ9DBX2.
TreeFamiTF315179.

Family and domain databases

CDDicd02987. Phd_like_Phd. 1 hit.
Gene3Di1.10.168.10. 1 hit.
InterProiView protein in InterPro
IPR001200. Phosducin.
IPR023196. Phosducin_N_dom.
IPR024253. Phosducin_thioredoxin-like_dom.
IPR036249. Thioredoxin-like_sf.
PfamiView protein in Pfam
PF02114. Phosducin. 1 hit.
PRINTSiPR00677. PHOSDUCIN.
SUPFAMiSSF52833. SSF52833. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9DBX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTLDDKLLG EKLQYYYSTS EDEDSDHEDK DRGRGAPAIS STPAEAELAG
60 70 80 90 100
EGISINTGPK GVINDWRRFK QLETEQREEQ CREMERLIKK LSMSCRSHLD
110 120 130 140 150
EEEEQQKQKD LQEKISGKMT LKEFGTKDKN LDDEEFLQQY RKQRMEEMRQ
160 170 180 190 200
QFHKGPQFKQ VFEIPSGEGF LDMIDKEQKS TLIMVHIYED GVPGTEAMNG
210 220 230 240 250
CMICLATEYP AVKFCRVRSS VIGASSRFTR NALPALLIYK AGELIGNFVR
260 270 280 290 300
VTDQLGEDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI

D
Length:301
Mass (Da):34,407
Last modified:June 1, 2001 - v1
Checksum:iFE0A130521AD4CFC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004704 mRNA. Translation: BAB23489.1.
AK028668 mRNA. Translation: BAC26056.1.
AK028814 mRNA. Translation: BAC26133.1.
AK166983 mRNA. Translation: BAE39165.1.
CCDSiCCDS15998.1.
RefSeqiNP_080452.2. NM_026176.3.
XP_006498315.1. XM_006498252.1.
UniGeneiMm.30709.

Genome annotation databases

EnsembliENSMUST00000009174; ENSMUSP00000009174; ENSMUSG00000009030.
ENSMUST00000112940; ENSMUSP00000108562; ENSMUSG00000009030.
GeneIDi67466.
KEGGimmu:67466.
UCSCiuc008jmp.2. mouse.

Similar proteinsi

Entry informationi

Entry nameiPHLP_MOUSE
AccessioniPrimary (citable) accession number: Q9DBX2
Secondary accession number(s): Q3TKI0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: June 1, 2001
Last modified: October 25, 2017
This is version 116 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families