PDCL3_MOUSE
ID PDCL3_MOUSE Reviewed; 240 AA.
AC Q8BVF2; Q3TH06; Q99JX2; Q9D0W3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Phosducin-like protein 3;
DE AltName: Full=Viral IAP-associated factor 1;
DE Short=VIAF-1;
GN Name=Pdcl3; Synonyms=Viaf1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryo, and Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
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).
RN [6]
RP INTERACTION WITH HSP90AA1 AND HSP90AB1, SUBCELLULAR LOCATION, AND
RP 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 (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) (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:0000269|PubMed:27496612}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9H2J4}.
CC Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9H2J4}.
CC -!- TISSUE SPECIFICITY: Expressed in blood vessels (at protein level).
CC {ECO:0000269|PubMed:26059764}.
CC -!- INDUCTION: By hypoxia and heat shock. {ECO:0000269|PubMed:26059764,
CC 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; AF110512; AAG21888.1; -; mRNA.
DR EMBL; AK004334; BAB23267.1; -; mRNA.
DR EMBL; AK078372; BAC37242.1; -; mRNA.
DR EMBL; AK168509; BAE40392.1; -; mRNA.
DR EMBL; BC005601; AAH05601.1; -; mRNA.
DR CCDS; CCDS14903.1; -.
DR RefSeq; NP_081126.2; NM_026850.4.
DR AlphaFoldDB; Q8BVF2; -.
DR SMR; Q8BVF2; -.
DR BioGRID; 213073; 2.
DR IntAct; Q8BVF2; 2.
DR MINT; Q8BVF2; -.
DR STRING; 10090.ENSMUSP00000027247; -.
DR iPTMnet; Q8BVF2; -.
DR PhosphoSitePlus; Q8BVF2; -.
DR EPD; Q8BVF2; -.
DR jPOST; Q8BVF2; -.
DR MaxQB; Q8BVF2; -.
DR PaxDb; Q8BVF2; -.
DR PeptideAtlas; Q8BVF2; -.
DR PRIDE; Q8BVF2; -.
DR ProteomicsDB; 287802; -.
DR Antibodypedia; 17722; 188 antibodies from 26 providers.
DR DNASU; 68833; -.
DR Ensembl; ENSMUST00000027247; ENSMUSP00000027247; ENSMUSG00000026078.
DR GeneID; 68833; -.
DR KEGG; mmu:68833; -.
DR UCSC; uc007atc.1; mouse.
DR CTD; 79031; -.
DR MGI; MGI:1916083; Pdcl3.
DR VEuPathDB; HostDB:ENSMUSG00000026078; -.
DR eggNOG; KOG3170; Eukaryota.
DR GeneTree; ENSGT00940000154295; -.
DR HOGENOM; CLU_072604_0_0_1; -.
DR InParanoid; Q8BVF2; -.
DR OMA; QKPDYSR; -.
DR OrthoDB; 1247977at2759; -.
DR PhylomeDB; Q8BVF2; -.
DR TreeFam; TF315179; -.
DR BioGRID-ORCS; 68833; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Pdcl3; mouse.
DR PRO; PR:Q8BVF2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BVF2; protein.
DR Bgee; ENSMUSG00000026078; Expressed in primary oocyte and 260 other tissues.
DR ExpressionAtlas; Q8BVF2; baseline and differential.
DR Genevisible; Q8BVF2; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097356; C:perinucleolar compartment; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR GO; GO:0043184; F:vascular endothelial growth factor receptor 2 binding; IPI:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISO:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; ISO:MGI.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:1903645; P:negative regulation of chaperone-mediated protein folding; ISO:MGI.
DR GO; GO:2000059; P:negative regulation of ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..240
FT /note="Phosducin-like protein 3"
FT /id="PRO_0000163759"
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:21183079"
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"
FT CONFLICT 59
FT /note="Missing (in Ref. 2; BAB23267)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="P -> L (in Ref. 3; AAH05601)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 240 AA; 27581 MW; 446AB65099164E09 CRC64;
MQDPNADTEW NDILRKKGIL PPKESLKELE EEEAEKEEQL LQQSVVKTYE DMTLEELEEN
EDEFSEEDER AIEMYRQQRL AEWKATQLKN KFGEVLEISG KDYVQEVTKA GEGLWVILHL
YKQGIPLCSL INHHLSGLAR KFPDVKFIKA ISTTCIPNYP DRNLPTVFVY REGDIKAQFI
GPLVFGGMNL TIDELEWKLS ESGAIKTALE ENPKKPIQDL LLSSVRGPVP MRRDSDSEDD
