PDCL3_RAT
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 03-AUG-2022, entry version 106.
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; Q4KLJ8; -.
DR PRIDE; Q4KLJ8; -.
DR GeneID; 316348; -.
DR KEGG; rno:316348; -.
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 OMA; QKPDYSR; -.
DR OrthoDB; 1247977at2759; -.
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 tissues.
DR Genevisible; Q4KLJ8; RN.
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 InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR Pfam; PF02114; Phosducin; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
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
