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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 - Biological processi

  1. heterotrimeric G-protein complex assembly Source: MGI
  2. negative regulation of protein refolding Source: Ensembl
  3. protein folding Source: Ensembl
  4. response to stimulus Source: UniProtKB-KW
  5. visual perception Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Sensory transduction, Vision

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914716. Pdcl.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 301300Phosducin-like proteinPRO_0000163756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei25 – 251Phosphoserine1 Publication
Modified residuei293 – 2931PhosphoserineBy similarity
Modified residuei296 – 2961PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9DBX2.
PaxDbiQ9DBX2.
PRIDEiQ9DBX2.

PTM databases

PhosphoSiteiQ9DBX2.

Expressioni

Gene expression databases

BgeeiQ9DBX2.
CleanExiMM_PDCL.
ExpressionAtlasiQ9DBX2. baseline and differential.
GenevestigatoriQ9DBX2.

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

Structurei

3D structure databases

ProteinModelPortaliQ9DBX2.
SMRiQ9DBX2. Positions 51-277.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni158 – 301144Thioredoxin foldBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the phosducin family.Curated

Phylogenomic databases

eggNOGiNOG262340.
GeneTreeiENSGT00530000062970.
HOGENOMiHOG000232010.
HOVERGENiHBG003456.
InParanoidiQ9DBX2.
OMAiMQEYNML.
OrthoDBiEOG7H4DVC.
PhylomeDBiQ9DBX2.
TreeFamiTF315179.

Family and domain databases

Gene3Di1.10.168.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR001200. Phosducin.
IPR023196. Phosducin_N_dom.
IPR024253. Phosducin_thioredoxin-like_dom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF02114. Phosducin. 1 hit.
[Graphical view]
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.

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.
SMRiQ9DBX2. Positions 51-277.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

PhosphoSiteiQ9DBX2.

Proteomic databases

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

eggNOGiNOG262340.
GeneTreeiENSGT00530000062970.
HOGENOMiHOG000232010.
HOVERGENiHBG003456.
InParanoidiQ9DBX2.
OMAiMQEYNML.
OrthoDBiEOG7H4DVC.
PhylomeDBiQ9DBX2.
TreeFamiTF315179.

Miscellaneous databases

ChiTaRSiPdcl. mouse.
NextBioi324658.
PROiQ9DBX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBX2.
CleanExiMM_PDCL.
ExpressionAtlasiQ9DBX2. baseline and differential.
GenevestigatoriQ9DBX2.

Family and domain databases

Gene3Di1.10.168.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR001200. Phosducin.
IPR023196. Phosducin_N_dom.
IPR024253. Phosducin_thioredoxin-like_dom.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF02114. Phosducin. 1 hit.
[Graphical view]
PRINTSiPR00677. PHOSDUCIN.
SUPFAMiSSF52833. SSF52833. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung and Skin.
  2. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  3. "Phosducin-like protein 1 is essential for G-protein assembly and signaling in retinal rod photoreceptors."
    Lai C.W., Kolesnikov A.V., Frederick J.M., Blake D.R., Jiang L., Stewart J.S., Chen C.K., Barrow J.R., Baehr W., Kefalov V.J., Willardson B.M.
    J. Neurosci. 33:7941-7951(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPHLP_MOUSE
AccessioniPrimary (citable) accession number: Q9DBX2
Secondary accession number(s): Q3TKI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 17, 2003
Last sequence update: June 1, 2001
Last modified: April 1, 2015
This is version 95 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.