PDCL3_DANRE
ID PDCL3_DANRE Reviewed; 239 AA.
AC Q6P268; Q800E3;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Phosducin-like protein 3;
DE AltName: Full=Viral IAP-associated factor 1 homolog;
GN Name=pdcl3 {ECO:0000312|EMBL:AAH64706.1};
GN Synonyms=viaf1 {ECO:0000312|EMBL:AAG09198.1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAG09198.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15371430; DOI=10.1074/jbc.m409623200;
RA Wilkinson J.C., Richter B.W.M., Wilkinson A.S., Burstein E., Rumble J.M.,
RA Balliu B., Duckett C.S.;
RT "VIAF, a conserved inhibitor of apoptosis (IAP)-interacting factor that
RT modulates caspase activation.";
RL J. Biol. Chem. 279:51091-51099(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH64706.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina {ECO:0000312|EMBL:AAH64706.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=26059764; DOI=10.1007/s10456-015-9468-3;
RA Srinivasan S., Chitalia V., Meyer R.D., Hartsough E., Mehta M., Harrold I.,
RA Anderson N., Feng H., Smith L.E., Jiang Y., Costello C.E., Rahimi N.;
RT "Hypoxia-induced expression of phosducin-like 3 regulates expression of
RT VEGFR-2 and promotes angiogenesis.";
RL Angiogenesis 18:449-462(2015).
CC -!- FUNCTION: Acts as a chaperone for the angiogenic VEGF receptor
CC KDR/VEGFR2, increasing its abundance by inhibiting its ubiquitination
CC and degradation (PubMed:26059764). 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, ECO:0000269|PubMed:26059764}.
CC -!- SUBUNIT: Interacts (via thioredoxin fold region) with kdr/vegfr2 (via
CC juxtamembrane domain). {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 -!- TISSUE SPECIFICITY: Expressed in endothelial cells.
CC {ECO:0000269|PubMed:26059764}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC significant inhibition of angiogenesis. {ECO:0000269|PubMed:26059764}.
CC -!- SIMILARITY: Belongs to the phosducin family. {ECO:0000255}.
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; AF175204; AAG09198.1; -; mRNA.
DR EMBL; BC064706; AAH64706.1; -; mRNA.
DR RefSeq; NP_991284.1; NM_205721.1.
DR AlphaFoldDB; Q6P268; -.
DR SMR; Q6P268; -.
DR GeneID; 403034; -.
DR KEGG; dre:403034; -.
DR CTD; 79031; -.
DR ZFIN; ZDB-GENE-040322-1; pdcl3.
DR InParanoid; Q6P268; -.
DR OrthoDB; 1247977at2759; -.
DR PhylomeDB; Q6P268; -.
DR PRO; PR:Q6P268; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IMP:ZFIN.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; IBA:GO_Central.
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 Angiogenesis; Apoptosis; Chaperone; Cytoplasm; Endoplasmic reticulum;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..239
FT /note="Phosducin-like protein 3"
FT /id="PRO_0000163760"
FT REGION 16..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..239
FT /note="Thioredoxin fold"
FT /evidence="ECO:0000250"
FT REGION 217..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H2J4"
FT CONFLICT 74
FT /note="L -> Q (in Ref. 1; AAG09198)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 27657 MW; 6C568D5813780D84 CRC64;
MQDPNADTEW NDILRKKGIL PPKETPVEEE EDEQLHLQSQ SVVKTYEDMT LEELEENEDE
FSEEDEHAME MYRLKRLAEW KANQMKNVFG ELKEISGQDY VQEVNKAGEG IWVVLHLYKQ
GIPLCSLINQ HLAQLARKFP QSKFLKSISS TCIPNYPDRN LPTLFVYRDG EMKAQFIGPL
VFGGMNLTCD ELEWRLSESG AVKTDLEENP RKQIQDQLMT SIRCSANTHR DGEEDSDED
