ID   PHLP_BOVIN              Reviewed;         301 AA.
AC   Q2HJA9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Phosducin-like protein;
DE            Short=PHLP;
GN   Name=PDCL;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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: 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:0000250|UniProtKB:Q9DBX2}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR   EMBL; BC113227; AAI13228.1; -; mRNA.
DR   RefSeq; NP_777184.2; NM_174759.2.
DR   AlphaFoldDB; Q2HJA9; -.
DR   SMR; Q2HJA9; -.
DR   STRING; 9913.ENSBTAP00000040945; -.
DR   PaxDb; Q2HJA9; -.
DR   PRIDE; Q2HJA9; -.
DR   Ensembl; ENSBTAT00000043370; ENSBTAP00000040945; ENSBTAG00000030675.
DR   GeneID; 286773; -.
DR   KEGG; bta:286773; -.
DR   CTD; 5082; -.
DR   VEuPathDB; HostDB:ENSBTAG00000030675; -.
DR   VGNC; VGNC:32665; PDCL.
DR   eggNOG; KOG3171; Eukaryota.
DR   GeneTree; ENSGT00940000159569; -.
DR   HOGENOM; CLU_085598_0_0_1; -.
DR   InParanoid; Q2HJA9; -.
DR   OMA; RQTGHNQ; -.
DR   OrthoDB; 1324495at2759; -.
DR   TreeFam; TF315179; -.
DR   Reactome; R-BTA-6814122; Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
DR   Proteomes; UP000009136; Chromosome 11.
DR   Bgee; ENSBTAG00000030675; Expressed in neutrophil and 105 other tissues.
DR   GO; GO:0005929; C:cilium; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:1902605; P:heterotrimeric G-protein complex assembly; IBA:GO_Central.
DR   GO; GO:0045880; P:positive regulation of smoothened signaling pathway; ISS:UniProtKB.
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; IEA:UniProtKB-KW.
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   2: Evidence at transcript 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_0000266028"
FT   REGION          15..53
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:0000250|UniProtKB:Q9DBX2"
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;  34395 MW;  B0147BF52D850BA3 CRC64;
     MTTLDDKLLG EKLQYYYSSS EEEDSDHEDK DRGRGALAGS SMPADADLAG EGISVNTGPK
     GVINDWRRFK QLETEQREEQ CREMERLIKK LSLSCRSHLD EEEEQRKQKD LQEKISGKMT
     LKDLAVMNED QDDEEFLQQY RKQRMEEMRQ QLYQGPQFKQ VFEIPSGEGF LDMIDKEQRS
     TLIMVHIYED GIPGTEAMNG CMLCLAAEYP AVKFCRVRSS VIGASSRFTR NALPALLIYK
     GGELIGNFVR VTDQLGEDFF AVDLEAFLQE FGLLPEKEVL LRTSVRNSAT CHSEDSDLEI
     D