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Protein

Phosducin-like protein

Gene

Pdcl

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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 (PubMed:23637185). Acts also as a positive regulator of hedgehog signaling and regulates ciliary function (PubMed:29290584).2 Publications

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone
Biological processCilium biogenesis/degradation, Sensory 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

Keywords - Cellular componenti

Cell projection

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 Expressed in 275 organ(s), highest expression level in skin of back
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

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000009174

Structurei

3D structure databases

ProteinModelPortaliQ9DBX2
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
GeneTreeiENSGT00930000150898
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_sf
IPR024253 Phosducin_thioredoxin-like_dom
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF02114 Phosducin, 1 hit
PRINTSiPR00677 PHOSDUCIN
SUPFAMiSSF52833 SSF52833, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2AVP3A2AVP3_MOUSE
Phosducin-like protein
Pdcl
193Annotation score:
A0A0N4SWE2A0A0N4SWE2_MOUSE
Phosducin-like protein
Pdcl
66Annotation score:

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

Cross-referencesi

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

3D structure databases

ProteinModelPortaliQ9DBX2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000009174

PTM databases

iPTMnetiQ9DBX2
PhosphoSitePlusiQ9DBX2

Proteomic databases

EPDiQ9DBX2
MaxQBiQ9DBX2
PaxDbiQ9DBX2
PRIDEiQ9DBX2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5082
MGIiMGI:1914716 Pdcl

Phylogenomic databases

eggNOGiKOG3171 Eukaryota
ENOG4110DRD LUCA
GeneTreeiENSGT00930000150898
HOGENOMiHOG000232010
HOVERGENiHBG003456
InParanoidiQ9DBX2
OMAiPSIKFAK
OrthoDBiEOG091G0ISM
PhylomeDBiQ9DBX2
TreeFamiTF315179

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPdcl mouse
PROiPR:Q9DBX2
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000009030 Expressed in 275 organ(s), highest expression level in skin of back
CleanExiMM_PDCL
ExpressionAtlasiQ9DBX2 baseline and differential
GenevisibleiQ9DBX2 MM

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_sf
IPR024253 Phosducin_thioredoxin-like_dom
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF02114 Phosducin, 1 hit
PRINTSiPR00677 PHOSDUCIN
SUPFAMiSSF52833 SSF52833, 1 hit
ProtoNetiSearch...

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: November 7, 2018
This is version 123 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. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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Main funding by: National Institutes of Health

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