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PRKC apoptosis WT1 regulator protein (Prostate apoptosis response 4 protein) (Par-4) (Transcriptional repressor Par-4-like protein PAWR)

 PAWR_RAT                Reviewed;         332 AA.
Q62627;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 106.
RecName: Full=PRKC apoptosis WT1 regulator protein;
AltName: Full=Prostate apoptosis response 4 protein;
Short=Par-4;
AltName: Full=Transcriptional repressor Par-4-like protein PAWR;
Name=Pawr; Synonyms=Par4;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
TISSUE=Prostate;
PubMed=8043520;
Sells S.F., Wood D.P. Jr., Joshi-Barve S.S., Muthukumar S.,
Jacob R.J., Crist S.A., Humphreys S., Rangnekar V.M.;
"Commonality of the gene programs induced by effectors of apoptosis in
androgen-dependent and -independent prostate cells.";
Cell Growth Differ. 5:457-466(1994).
[2]
DOMAIN SAC, MUTAGENESIS, AND SUBCELLULAR LOCATION.
PubMed=12897127; DOI=10.1128/MCB.23.16.5516-5525.2003;
El-Guendy N., Zhao Y., Gurumurthy S., Burikhanov R., Rangnekar V.M.;
"Identification of a unique core domain of par-4 sufficient for
selective apoptosis induction in cancer cells.";
Mol. Cell. Biol. 23:5516-5525(2003).
[3]
PHOSPHORYLATION AT THR-155 BY PKA.
PubMed=15657440; DOI=10.1128/MCB.25.3.1146-1161.2005;
Gurumurthy S., Goswami A., Vasudevan K.M., Rangnekar V.M.;
"Phosphorylation of Par-4 by protein kinase A is critical for
apoptosis.";
Mol. Cell. Biol. 25:1146-1161(2005).
[4]
INTERACTION WITH ACTIN.
PubMed=15817164; DOI=10.1016/j.yexcr.2005.01.012;
Vetterkind S., Illenberger S., Kubicek J., Boosen M., Appel S.,
Naim H.Y., Scheidtmann K.H., Preuss U.;
"Binding of Par-4 to the actin cytoskeleton is essential for Par-
4/Dlk-mediated apoptosis.";
Exp. Cell Res. 305:392-408(2005).
-!- FUNCTION: Pro-apoptopic protein capable of selectively inducing
apoptosis in cancer cells, sensitizing the cells to diverse
apoptotic stimuli and causing regression of tumors in animal
models. Induces apoptosis in certain cancer cells by activation of
the Fas prodeath pathway and coparallel inhibition of NF-kappa-B
transcriptional activity. Inhibits the transcriptional activation
and augments the transcriptional repression mediated by WT1. Down-
regulates the anti-apoptotic protein BCL2 via its interaction with
WT1. Seems also to be a transcriptional repressor by itself. May
be directly involved in regulating the amyloid precursor protein
(APP) cleavage activity of BACE1 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homooligomer. Interacts (via the C-terminal region) with
WT1. Interacts with THAP1. Interacts with AATF. Interacts with
BACE1. Interacts with SPSB1 (via B30.2/SPRY domain); this
interaction is direct and occurs in association with the Elongin
BC complex. Interacts with SPSB2 (via B30.2/SPRY domain); this
interaction occurs in association with the Elongin BC complex.
Interacts with SPSB4 (via B30.2/SPRY domain); this interaction
occurs in association with the Elongin BC complex. Component of a
ternary complex composed of SQSTM1 and PRKCZ (By similarity).
Interacts with actin (PubMed:15817164).
{ECO:0000250|UniProtKB:Q62627, ECO:0000250|UniProtKB:Q96IZ0,
ECO:0000269|PubMed:15817164}.
-!- INTERACTION:
O88764:Dapk3; NbExp=5; IntAct=EBI-1187240, EBI-4404236;
P11021:HSPA5 (xeno); NbExp=4; IntAct=EBI-1187240, EBI-354921;
Q9JMG6:Tfpt; NbExp=8; IntAct=EBI-1187240, EBI-1767101;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Mainly cytoplasmic in absence of apoptosis
signal and in normal cells. Nuclear in most cancer cell lines.
Nuclear entry seems to be essential but not sufficient for
apoptosis. Nuclear localization includes nucleoplasm and PML
nuclear bodies (By similarity). {ECO:0000250}.
-!- INDUCTION: In ventral prostate following castration.
{ECO:0000269|PubMed:8043520}.
-!- DOMAIN: The leucine-zipper domain is not essential for apoptosis,
but is required for sensitization of cells to exogenous apoptotic
insults and for interaction with its partners. {ECO:0000250}.
-!- DOMAIN: The SAC domain is a death-inducing domain selective for
apoptosis induction in cancer cells. This domain is essential for
nuclear entry, Fas activation, inhibition of NF-kappa-B activity
and induction of apoptosis in cancer cells (By similarity).
{ECO:0000250}.
-!- DOMAIN: The B30.2/SPRY domain-binding motif mediates recognition
by proteins containing a B30.2/SPRY domain.
{ECO:0000250|UniProtKB:Q96IZ0}.
-!- PTM: Preferentially phosphorylated at the Thr-155 by PKC in cancer
cells. {ECO:0000269|PubMed:15657440}.
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EMBL; U05989; AAA16492.1; -; mRNA.
RefSeq; NP_277020.1; NM_033485.2.
UniGene; Rn.9127; -.
PDB; 5FIY; X-ray; 3.00 A; A/B/C/D/E/F/G=240-332.
PDBsum; 5FIY; -.
DisProt; DP00940; -.
ProteinModelPortal; Q62627; -.
SMR; Q62627; -.
BioGrid; 249098; 3.
IntAct; Q62627; 5.
MINT; MINT-199814; -.
STRING; 10116.ENSRNOP00000008222; -.
iPTMnet; Q62627; -.
PhosphoSitePlus; Q62627; -.
PaxDb; Q62627; -.
PRIDE; Q62627; -.
DNASU; 64513; -.
GeneID; 64513; -.
KEGG; rno:64513; -.
UCSC; RGD:69065; rat.
CTD; 5074; -.
RGD; 69065; Pawr.
eggNOG; ENOG410IFBP; Eukaryota.
eggNOG; ENOG4111M3H; LUCA.
HOGENOM; HOG000115462; -.
HOVERGEN; HBG058812; -.
InParanoid; Q62627; -.
PhylomeDB; Q62627; -.
PRO; PR:Q62627; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0008157; F:protein phosphatase 1 binding; IPI:RGD.
GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IMP:RGD.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0098703; P:calcium ion import across plasma membrane; IDA:RGD.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEP:RGD.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
GO; GO:0071347; P:cellular response to interleukin-1; IEP:RGD.
GO; GO:0071306; P:cellular response to vitamin E; IEP:RGD.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IDA:RGD.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IDA:RGD.
GO; GO:0090281; P:negative regulation of calcium ion import; IDA:RGD.
GO; GO:0045760; P:positive regulation of action potential; IDA:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
GO; GO:0060450; P:positive regulation of hindgut contraction; IDA:RGD.
GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IDA:RGD.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1904457; P:positive regulation of neuronal action potential; IMP:RGD.
GO; GO:2000391; P:positive regulation of neutrophil extravasation; IDA:RGD.
GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IMP:RGD.
GO; GO:1901082; P:positive regulation of relaxation of smooth muscle; IDA:RGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0010040; P:response to iron(II) ion; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0009611; P:response to wounding; IEP:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR026117; Par-4.
PANTHER; PTHR15093; PTHR15093; 1.
1: Evidence at protein level;
3D-structure; Apoptosis; Coiled coil; Complete proteome; Cytoplasm;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation.
CHAIN 1 332 PRKC apoptosis WT1 regulator protein.
/FTId=PRO_0000058238.
REGION 137 195 Selective for apoptosis induction in
cancer cells (SAC).
REGION 292 332 Leucine-zipper.
COILED 176 198 {ECO:0000255}.
MOTIF 61 65 B30.2/SPRY domain-binding motif.
{ECO:0000250|UniProtKB:Q96IZ0}.
MOTIF 137 153 Nuclear localization signal.
MOD_RES 155 155 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:15657440}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000250|UniProtKB:Q96IZ0}.
HELIX 257 330 {ECO:0000244|PDB:5FIY}.
SEQUENCE 332 AA; 35866 MW; 2069B32DEFFF160F CRC64;
MATGGYRSSG STTDFLEEWK AKREKMRAKQ NPVGPGSSGG DPAAKSPAGP LAQTTAAGTS
ELNHGPAGAA APAAPGPGAL NCAHGSSALP RGAPGSRRPE DECPIAAGAA GAPASRGDEE
EPDSAPEKGR SSGPSARKGK GQIEKRKLRE KRRSTGVVNI PAAECLDEYE DDEAGQKERK
REDAITQQNT IQNEAASLPD PGTSYLPQDP SRTVPGRYKS TISAPEEEIL NRYPRTDRSG
FSRHNRDTSA PANFASSSTL EKRIEDLEKE VLRERQENLR LTRLMQDKEE MIGKLKEEID
LLNRDLDDME DENEQLKQEN KTLLKVVGQL TR


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