ID   PDCL3_PONAB             Reviewed;         239 AA.
AC   Q5RB77;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Phosducin-like protein 3;
GN   Name=PDCL3;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR858776; CAH90983.1; -; mRNA.
DR   RefSeq; NP_001125567.1; NM_001132095.1.
DR   AlphaFoldDB; Q5RB77; -.
DR   BMRB; Q5RB77; -.
DR   SMR; Q5RB77; -.
DR   GeneID; 100172481; -.
DR   KEGG; pon:100172481; -.
DR   CTD; 79031; -.
DR   InParanoid; Q5RB77; -.
DR   OrthoDB; 1247977at2759; -.
DR   Proteomes; UP000001595; 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; Host-virus interaction; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..239
FT                   /note="Phosducin-like protein 3"
FT                   /id="PRO_0000246159"
FT   REGION          91..239
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         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT   MOD_RES         234
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT   MOD_RES         236
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H2J4"
SQ   SEQUENCE   239 AA;  27572 MW;  76159ECD066FEF8A CRC64;
     MQDPNADTEW NDILRKKGIL PPKESLKELE EEAEEEQRIL QQSVVKTYED MTLEELDDHE
     DEFNEEDERA IEMYRRQRLA EWKVTKLKNK FGEVLEISGK DYVQEVTKAG EGLWVILHLY
     KQGIPLCALI NQHLSGLARK FPDVKFIKAI STTCIPNYPD RNLPTIFVYL EGDIKAQFIG
     PLVFGGMNLT RDELEWKLSE SGAIMTDLEE NPKKPIEDVL LSSVRRSALM KRDSDSEGD