PHLP_MOUSE
ID PHLP_MOUSE Reviewed; 301 AA.
AC Q9DBX2; Q3TKI0;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Phosducin-like protein;
DE Short=PHLP;
GN Name=Pdcl; Synonyms=PhLP1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Lung, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=23637185; DOI=10.1523/jneurosci.5001-12.2013;
RA Lai C.W., Kolesnikov A.V., Frederick J.M., Blake D.R., Jiang L.,
RA Stewart J.S., Chen C.K., Barrow J.R., Baehr W., Kefalov V.J.,
RA Willardson B.M.;
RT "Phosducin-like protein 1 is essential for G-protein assembly and signaling
RT in retinal rod photoreceptors.";
RL J. Neurosci. 33:7941-7951(2013).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=29290584; DOI=10.1016/j.devcel.2017.12.003;
RA Pusapati G.V., Kong J.H., Patel B.B., Krishnan A., Sagner A., Kinnebrew M.,
RA Briscoe J., Aravind L., Rohatgi R.;
RT "CRISPR screens uncover genes that regulate target cell sensitivity to the
RT morphogen sonic hedgehog.";
RL Dev. Cell 44:113-129(2018).
CC -!- FUNCTION: Functions as a co-chaperone for CCT in the assembly of
CC heterotrimeric G protein complexes, facilitates the assembly of both
CC Gbeta-Ggamma and RGS-Gbeta5 heterodimers (PubMed:23637185). Acts also
CC as a positive regulator of hedgehog signaling and regulates ciliary
CC function (PubMed:29290584). {ECO:0000269|PubMed:23637185,
CC ECO:0000269|PubMed:29290584}.
CC -!- SUBUNIT: Forms a complex with the beta and gamma subunits of the GTP-
CC binding protein, transducin. Interacts with the CCT chaperonin complex
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000269|PubMed:29290584}.
CC -!- DISRUPTION PHENOTYPE: Conditional deletion in photoreceptor cells leads
CC to 50-fold decrease in Gbeta-Ggamma dimer formation and more than 10-
CC fold decrease in light sensitivity. A 20-fold reduction in Gbeta5 and
CC RGS9-1 expression is also observed, causing a 15-fold delay in the
CC shutoff of light responses. {ECO:0000269|PubMed:23637185}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; AK004704; BAB23489.1; -; mRNA.
DR EMBL; AK028668; BAC26056.1; -; mRNA.
DR EMBL; AK028814; BAC26133.1; -; mRNA.
DR EMBL; AK166983; BAE39165.1; -; mRNA.
DR CCDS; CCDS15998.1; -.
DR RefSeq; NP_080452.2; NM_026176.3.
DR RefSeq; XP_006498315.1; XM_006498252.1.
DR AlphaFoldDB; Q9DBX2; -.
DR SMR; Q9DBX2; -.
DR BioGRID; 212208; 6.
DR STRING; 10090.ENSMUSP00000108562; -.
DR iPTMnet; Q9DBX2; -.
DR PhosphoSitePlus; Q9DBX2; -.
DR EPD; Q9DBX2; -.
DR jPOST; Q9DBX2; -.
DR MaxQB; Q9DBX2; -.
DR PaxDb; Q9DBX2; -.
DR PRIDE; Q9DBX2; -.
DR ProteomicsDB; 289494; -.
DR Antibodypedia; 16148; 166 antibodies from 31 providers.
DR DNASU; 67466; -.
DR Ensembl; ENSMUST00000009174; ENSMUSP00000009174; ENSMUSG00000009030.
DR Ensembl; ENSMUST00000112940; ENSMUSP00000108562; ENSMUSG00000009030.
DR GeneID; 67466; -.
DR KEGG; mmu:67466; -.
DR UCSC; uc008jmp.2; mouse.
DR CTD; 5082; -.
DR MGI; MGI:1914716; Pdcl.
DR VEuPathDB; HostDB:ENSMUSG00000009030; -.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000159569; -.
DR HOGENOM; CLU_085598_0_0_1; -.
DR InParanoid; Q9DBX2; -.
DR OMA; RQTGHNQ; -.
DR OrthoDB; 1324495at2759; -.
DR PhylomeDB; Q9DBX2; -.
DR TreeFam; TF315179; -.
DR Reactome; R-MMU-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR BioGRID-ORCS; 67466; 19 hits in 75 CRISPR screens.
DR ChiTaRS; Pdcl; mouse.
DR PRO; PR:Q9DBX2; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DBX2; protein.
DR Bgee; ENSMUSG00000009030; Expressed in pineal body and 246 other tissues.
DR ExpressionAtlas; Q9DBX2; baseline and differential.
DR Genevisible; Q9DBX2; MM.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:1902605; P:heterotrimeric G-protein complex assembly; IMP:MGI.
DR GO; GO:0061084; P:negative regulation of protein refolding; ISO:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:InterPro.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd02987; Phd_like_Phd; 1.
DR Gene3D; 1.10.168.10; -; 1.
DR InterPro; IPR001200; Phosducin.
DR InterPro; IPR023196; Phosducin_N_dom_sf.
DR InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR PRINTS; PR00677; PHOSDUCIN.
DR SUPFAM; SSF52833; SSF52833; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell projection; Chaperone; Cilium biogenesis/degradation;
KW Phosphoprotein; Reference proteome; Sensory transduction; Vision.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
FT CHAIN 2..301
FT /note="Phosducin-like protein"
FT /id="PRO_0000163756"
FT REGION 17..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..301
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT COMPBIAS 17..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63737"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
SQ SEQUENCE 301 AA; 34407 MW; FE0A130521AD4CFC CRC64;
MTTLDDKLLG EKLQYYYSTS EDEDSDHEDK DRGRGAPAIS STPAEAELAG EGISINTGPK
GVINDWRRFK QLETEQREEQ CREMERLIKK LSMSCRSHLD EEEEQQKQKD LQEKISGKMT
LKEFGTKDKN LDDEEFLQQY RKQRMEEMRQ QFHKGPQFKQ VFEIPSGEGF LDMIDKEQKS
TLIMVHIYED GVPGTEAMNG CMICLATEYP AVKFCRVRSS VIGASSRFTR NALPALLIYK
AGELIGNFVR VTDQLGEDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI
D
