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   27-MAR-2024, entry version 152.
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; 7.
DR   STRING; 10090.ENSMUSP00000108562; -.
DR   iPTMnet; Q9DBX2; -.
DR   PhosphoSitePlus; Q9DBX2; -.
DR   EPD; Q9DBX2; -.
DR   jPOST; Q9DBX2; -.
DR   MaxQB; Q9DBX2; -.
DR   PaxDb; 10090-ENSMUSP00000108562; -.
DR   ProteomicsDB; 289494; -.
DR   Pumba; Q9DBX2; -.
DR   Antibodypedia; 16148; 178 antibodies from 31 providers.
DR   DNASU; 67466; -.
DR   Ensembl; ENSMUST00000009174.15; ENSMUSP00000009174.9; ENSMUSG00000009030.15.
DR   Ensembl; ENSMUST00000112940.8; ENSMUSP00000108562.2; ENSMUSG00000009030.15.
DR   GeneID; 67466; -.
DR   KEGG; mmu:67466; -.
DR   UCSC; uc008jmp.2; mouse.
DR   AGR; MGI:1914716; -.
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; GIIEMMP; -.
DR   OrthoDB; 2912029at2759; -.
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; 20 hits in 80 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 249 other cell types or tissues.
DR   ExpressionAtlas; Q9DBX2; baseline and differential.
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; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 1.10.168.10; Phosducin, domain 2; 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   PANTHER; PTHR46052; PHOSDUCIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR46052:SF4; PHOSDUCIN-LIKE PROTEIN; 1.
DR   Pfam; PF02114; Phosducin; 1.
DR   PRINTS; PR00677; PHOSDUCIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   Genevisible; Q9DBX2; MM.
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
//