ID PHLP_RAT Reviewed; 301 AA.
AC Q63737; Q4V8L9; Q63738;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 147.
DE RecName: Full=Phosducin-like protein;
DE Short=PHLP;
GN Name=Pdcl;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
RC TISSUE=Brain;
RX PubMed=8248177; DOI=10.1073/pnas.90.22.10831;
RA Miles M.F., Barhite S., Sganga M., Elliott M.;
RT "Phosducin-like protein: an ethanol-responsive potential modulator of
RT guanine nucleotide-binding protein function.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10831-10835(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Fischer;
RX PubMed=10095058; DOI=10.1016/s0167-4781(99)00006-8;
RA Thibault C., Wang J.-F., Charnas R., Mirel D., Barhite S., Miles M.F.;
RT "Cloning and characterization of the rat and human phosducin-like protein
RT genes: structure, expression and chromosomal localization.";
RL Biochim. Biophys. Acta 1444:346-354(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=9139665; DOI=10.1074/jbc.272.19.12253;
RA Thibault C., Sganga M.W., Miles M.F.;
RT "Interaction of phosducin-like protein with G protein betagamma subunits.";
RL J. Biol. Chem. 272:12253-12256(1997).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-25; SER-293 AND
RP SER-296, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. Acts also as a positive
CC regulator of hedgehog signaling and regulates ciliary function.
CC {ECO:0000250|UniProtKB:Q9DBX2}.
CC -!- SUBUNIT: Interacts with the CCT chaperonin complex (By similarity).
CC Forms a complex with the beta and gamma subunits of the GTP-binding
CC protein, transducin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9DBX2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=Long;
CC IsoId=Q63737-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q63737-2; Sequence=VSP_004704;
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR EMBL; L15354; AAB00333.1; -; mRNA.
DR EMBL; L15355; AAB00334.1; -; mRNA.
DR EMBL; AF080435; AAC77925.1; -; Genomic_DNA.
DR EMBL; AF080433; AAC77925.1; JOINED; Genomic_DNA.
DR EMBL; AF080434; AAC77925.1; JOINED; Genomic_DNA.
DR EMBL; BC097322; AAH97322.1; -; mRNA.
DR PIR; A58928; A58928.
DR RefSeq; NP_071583.1; NM_022247.1. [Q63737-1]
DR AlphaFoldDB; Q63737; -.
DR SMR; Q63737; -.
DR BioGRID; 248932; 1.
DR CORUM; Q63737; -.
DR STRING; 10116.ENSRNOP00000012160; -.
DR iPTMnet; Q63737; -.
DR PhosphoSitePlus; Q63737; -.
DR PaxDb; 10116-ENSRNOP00000012160; -.
DR Ensembl; ENSRNOT00000012160.6; ENSRNOP00000012160.2; ENSRNOG00000008484.6. [Q63737-1]
DR Ensembl; ENSRNOT00055014988; ENSRNOP00055011956; ENSRNOG00055008885. [Q63737-1]
DR Ensembl; ENSRNOT00060043859; ENSRNOP00060036394; ENSRNOG00060025340. [Q63737-1]
DR Ensembl; ENSRNOT00065045567; ENSRNOP00065037365; ENSRNOG00065026404. [Q63737-1]
DR GeneID; 64013; -.
DR KEGG; rno:64013; -.
DR UCSC; RGD:621135; rat. [Q63737-1]
DR AGR; RGD:621135; -.
DR CTD; 5082; -.
DR RGD; 621135; Pdcl.
DR eggNOG; KOG3171; Eukaryota.
DR GeneTree; ENSGT00940000159569; -.
DR HOGENOM; CLU_085598_0_0_1; -.
DR InParanoid; Q63737; -.
DR OMA; GIIEMMP; -.
DR OrthoDB; 2912029at2759; -.
DR PhylomeDB; Q63737; -.
DR TreeFam; TF315179; -.
DR Reactome; R-RNO-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR PRO; PR:Q63737; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000008484; Expressed in thymus and 20 other cell types or tissues.
DR Genevisible; Q63737; RN.
DR GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:1902605; P:heterotrimeric G-protein complex assembly; ISO:RGD.
DR GO; GO:0061084; P:negative regulation of protein refolding; IDA:RGD.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; IDA:RGD.
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; ISO:RGD.
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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell projection; Chaperone;
KW Cilium biogenesis/degradation; Phosphoprotein; Reference proteome;
KW 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_0000163757"
FT REGION 15..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:0007744|PubMed:22673903"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13371"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..83
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8248177"
FT /id="VSP_004704"
SQ SEQUENCE 301 AA; 34274 MW; F32C776373354AD8 CRC64;
MTTLDDKLLG EKLQYYYSTS EDEDSDHEDK DRGRGAPASS STPAEAELAG EGISVNTGPK
GVINDWRRFK QLETEQREEQ CREMERLIKK LSMSCRSHLD EEEEQQKQKD LQEKISGKMT
LKECGMMDKN LDDEEFLQQY RKQRMDEMRQ QLHKGPQFKQ VLEIPSGEGF LDMIDKEQKS
TLIMVHIYED GVPGTEAMNG CMICLAAEYP TVKFCRVRSS VIGASSRFTR NALPALLIYK
AGELIGNFVR VTDQLGEDFF AVDLEAFLQE FGLLPEKEVL VLTSVRNSAT CHSEDSDLEI
D
//
