ID   PDCL3_BOVIN             Reviewed;         240 AA.
AC   Q0VCW8;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Phosducin-like protein 3;
GN   Name=PDCL3;
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=Fetal muscle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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 (By
CC       similarity). Modulates the activation of caspases during apoptosis (By
CC       similarity). {ECO:0000250|UniProtKB:Q4KLJ8,
CC       ECO:0000250|UniProtKB:Q9H2J4}.
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 (By
CC       similarity). {ECO:0000250|UniProtKB:Q4KLJ8,
CC       ECO:0000250|UniProtKB:Q9H2J4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H2J4}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}.
CC       Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
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; BC119960; AAI19961.1; -; mRNA.
DR   RefSeq; NP_001069113.1; NM_001075645.1.
DR   AlphaFoldDB; Q0VCW8; -.
DR   SMR; Q0VCW8; -.
DR   STRING; 9913.ENSBTAP00000013139; -.
DR   PaxDb; Q0VCW8; -.
DR   PRIDE; Q0VCW8; -.
DR   GeneID; 514033; -.
DR   KEGG; bta:514033; -.
DR   CTD; 79031; -.
DR   eggNOG; KOG3170; Eukaryota.
DR   InParanoid; Q0VCW8; -.
DR   OrthoDB; 1247977at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   InterPro; IPR024253; Phosducin_thioredoxin-like_dom.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF02114; Phosducin; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Angiogenesis; Apoptosis; Chaperone; Cytoplasm;
KW   Endoplasmic reticulum; Phosphoprotein; Reference proteome.
FT   CHAIN           1..240
FT                   /note="Phosducin-like protein 3"
FT                   /id="PRO_0000266029"
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         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;  27479 MW;  22B13D945029BEA6 CRC64;
     MQDPNADTEW NDILRKKGIL PSKEDLKDLE KEAEEEEQRI LQQSIVKTYE DMTLEELEDN
     EDEFNEEDER AIEMYRQQRL AEWKATQLKN KFGEVLEISG KDYVQEVTKA GEGLWVILHL
     YKQGIPLCAL INQHLSALAR KFPDVKFIKA ISTTCIPSYP DRNLPTVFVY LEGDIKAQFI
     GPLVFGGMNL TLDELEWKLS ESGAIKTSLE ENPKKPVEDV LLSAVRCSVP AKRDSDSEDD