ID   PDCL3_RAT               Reviewed;         240 AA.
AC   Q4KLJ8;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Phosducin-like protein 3;
GN   Name=Pdcl3;
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 [LARGE SCALE MRNA].
RC   TISSUE=Thymus;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP   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).
RN   [3]
RP   FUNCTION, INTERACTION WITH HSP90AA1 AND HSP90AB1, AND INDUCTION.
RX   PubMed=27496612; DOI=10.1002/jcb.25669;
RA   Krzemien-Ojak L., Goral A., Joachimiak E., Filipek A., Fabczak H.;
RT   "Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein
RT   Hsp90.";
RL   J. Cell. Biochem. 118:420-429(2017).
CC   -!- FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor
CC       KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination
CC       and degradation (By similarity). Inhibits the folding activity of the
CC       chaperonin-containing T-complex (CCT) which leads to inhibition of
CC       cytoskeletal actin folding (By similarity). Acts as a chaperone during
CC       heat shock alongside HSP90 and HSP40/70 chaperone complexes
CC       (PubMed:27496612). Modulates the activation of caspases during
CC       apoptosis (By similarity). {ECO:0000250|UniProtKB:Q9H2J4,
CC       ECO:0000269|PubMed:27496612}.
CC   -!- SUBUNIT: Interacts (via thioredoxin fold region) with KDR/VEGFR2 (via
CC       juxtamembrane domain) (By similarity). Forms ternary complexes with the
CC       chaperonin CCT complex and actin substrate, leading to inhibition of
CC       actin folding (By similarity). Interacts with XIAP (via BIR 3 and RING
CC       domain) (By similarity). Interacts with HSP90AA1 and HSP90AB1
CC       (PubMed:27496612). {ECO:0000250|UniProtKB:Q9H2J4,
CC       ECO:0000269|PubMed:27496612}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
CC   -!- INDUCTION: By heat shock. {ECO:0000269|PubMed:27496612}.
CC   -!- PTM: N-terminal methionine acetylation destabilizes the protein.
CC       {ECO:0000250|UniProtKB:Q9H2J4}.
CC   -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000305}.
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DR   EMBL; BC099162; AAH99162.1; -; mRNA.
DR   RefSeq; NP_001020880.1; NM_001025709.1.
DR   AlphaFoldDB; Q4KLJ8; -.
DR   SMR; Q4KLJ8; -.
DR   STRING; 10116.ENSRNOP00000017882; -.
DR   iPTMnet; Q4KLJ8; -.
DR   PhosphoSitePlus; Q4KLJ8; -.
DR   jPOST; Q4KLJ8; -.
DR   PaxDb; 10116-ENSRNOP00000017882; -.
DR   GeneID; 316348; -.
DR   KEGG; rno:316348; -.
DR   AGR; RGD:1309663; -.
DR   CTD; 79031; -.
DR   RGD; 1309663; Pdcl3.
DR   VEuPathDB; HostDB:ENSRNOG00000013286; -.
DR   eggNOG; KOG3170; Eukaryota.
DR   HOGENOM; CLU_072604_0_0_1; -.
DR   InParanoid; Q4KLJ8; -.
DR   OrthoDB; 313477at2759; -.
DR   PhylomeDB; Q4KLJ8; -.
DR   TreeFam; TF315179; -.
DR   PRO; PR:Q4KLJ8; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000013286; Expressed in quadriceps femoris and 20 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0097356; C:perinucleolar compartment; ISO:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR   GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; ISO:RGD.
DR   GO; GO:0030036; P:actin cytoskeleton organization; ISO:RGD.
DR   GO; GO:0001525; P:angiogenesis; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR   GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; ISO:RGD.
DR   GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; ISO:RGD.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:RGD.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR   CDD; cd02988; Phd_like_VIAF; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   NCBIfam; TIGR01552; phd_fam; 1.
DR   PANTHER; PTHR45809:SF4; PHOSDUCIN-LIKE PROTEIN 3; 1.
DR   PANTHER; PTHR45809; VIRAL IAP-ASSOCIATED FACTOR HOMOLOG; 1.
DR   Pfam; PF02114; Phosducin; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   Genevisible; Q4KLJ8; RN.
PE   1: Evidence at protein level;
KW   Acetylation; Angiogenesis; Apoptosis; Chaperone; Cytoplasm;
KW   Endoplasmic reticulum; Host-virus interaction; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..240
FT                   /note="Phosducin-like protein 3"
FT                   /id="PRO_0000246160"
FT   REGION          21..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..240
FT                   /note="Thioredoxin fold"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT   MOD_RES         44
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT   MOD_RES         65
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         235
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT   MOD_RES         237
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
SQ   SEQUENCE   240 AA;  27699 MW;  950F1D9C0A4498E8 CRC64;
     MQDPNADTEW NDILRKKGIL PPKESLKELE EEEEGKEEQR LQQSVVKTYE DMTLEELQEN
     EDEFSEEDER AIEMYRQQRL AEWKATQLRN KFGEVLEISG KDYVQEVTKA GEGLWVVLHL
     YKQGIPLCSL INHHLSGLAR KFPDVKFIKA ISTTCIPNYP DRNLPTVFVY REGDIKAQFI
     GPLVFGGMNL TIDELEWKLS ESGAIKTELE ENPKKAIKDV LLSSVRDPVP MRRDSDSEDD
//