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Protein

PRKC apoptosis WT1 regulator protein

Gene

Pawr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • enzyme binding Source: RGD
  • leucine zipper domain binding Source: RGD
  • protein kinase C binding Source: RGD
  • protein phosphatase 1 binding Source: RGD

GO - Biological processi

  • actin filament bundle assembly Source: UniProtKB
  • activation of cysteine-type endopeptidase activity Source: RGD
  • apoptotic process Source: UniProtKB
  • apoptotic signaling pathway Source: RGD
  • calcium ion import across plasma membrane Source: RGD
  • cellular response to estradiol stimulus Source: RGD
  • cellular response to follicle-stimulating hormone stimulus Source: RGD
  • cellular response to interleukin-1 Source: RGD
  • cellular response to vitamin E Source: RGD
  • detection of mechanical stimulus involved in sensory perception of pain Source: RGD
  • detection of temperature stimulus involved in sensory perception of pain Source: RGD
  • interleukin-2 biosynthetic process Source: RGD
  • negative regulation of B cell proliferation Source: RGD
  • negative regulation of calcium ion import Source: RGD
  • negative regulation of fibroblast proliferation Source: RGD
  • negative regulation of gene expression Source: RGD
  • negative regulation of T cell proliferation Source: RGD
  • negative regulation of T cell receptor signaling pathway Source: RGD
  • negative regulation of transcription from RNA polymerase II promoter Source: RGD
  • positive regulation of action potential Source: RGD
  • positive regulation of amyloid precursor protein biosynthetic process Source: RGD
  • positive regulation of apoptotic process Source: RGD
  • positive regulation of cellular senescence Source: RGD
  • positive regulation of gene expression Source: RGD
  • positive regulation of hindgut contraction Source: RGD
  • positive regulation of hydrogen peroxide-mediated programmed cell death Source: RGD
  • positive regulation of leukocyte tethering or rolling Source: RGD
  • positive regulation of neuronal action potential Source: RGD
  • positive regulation of neuron apoptotic process Source: RGD
  • positive regulation of neutrophil extravasation Source: RGD
  • positive regulation of phosphoprotein phosphatase activity Source: RGD
  • positive regulation of relaxation of smooth muscle Source: RGD
  • response to estradiol Source: RGD
  • response to iron(II) ion Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to wounding Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW

Keywordsi

Biological processApoptosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
PRKC apoptosis WT1 regulator protein
Alternative name(s):
Prostate apoptosis response 4 protein
Short name:
Par-4
Transcriptional repressor Par-4-like protein PAWR
Gene namesi
Name:Pawr
Synonyms:Par4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi69065. Pawr.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000582381 – 332PRKC apoptosis WT1 regulator proteinAdd BLAST332

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei155Phosphothreonine; by PKA1 Publication1
Modified residuei223PhosphoserineBy similarity1

Post-translational modificationi

Preferentially phosphorylated at the Thr-155 by PKC in cancer cells.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ62627.
PRIDEiQ62627.

PTM databases

iPTMnetiQ62627.
PhosphoSitePlusiQ62627.

Expressioni

Inductioni

In ventral prostate following castration.1 Publication

Interactioni

Subunit structurei

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).By similarity1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • enzyme binding Source: RGD
  • leucine zipper domain binding Source: RGD
  • protein kinase C binding Source: RGD
  • protein phosphatase 1 binding Source: RGD

Protein-protein interaction databases

BioGridi249098. 3 interactors.
IntActiQ62627. 5 interactors.
MINTiMINT-199814.
STRINGi10116.ENSRNOP00000008222.

Structurei

Secondary structure

1332
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi257 – 330Combined sources74

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5FIYX-ray3.00A/B/C/D/E/F/G240-332[»]
DisProtiDP00940.
ProteinModelPortaliQ62627.
SMRiQ62627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni137 – 195Selective for apoptosis induction in cancer cells (SAC)Add BLAST59
Regioni292 – 332Leucine-zipperAdd BLAST41

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili176 – 198Sequence analysisAdd BLAST23

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi61 – 65B30.2/SPRY domain-binding motifBy similarity5
Motifi137 – 153Nuclear localization signalAdd BLAST17

Domaini

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.By similarity
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).By similarity
The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain.By similarity

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IFBP. Eukaryota.
ENOG4111M3H. LUCA.
HOGENOMiHOG000115462.
HOVERGENiHBG058812.
InParanoidiQ62627.
PhylomeDBiQ62627.

Family and domain databases

InterProiView protein in InterPro
IPR026117. Par-4.
PANTHERiPTHR15093. PTHR15093. 1 hit.

Sequencei

Sequence statusi: Complete.

Q62627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGGYRSSG STTDFLEEWK AKREKMRAKQ NPVGPGSSGG DPAAKSPAGP
60 70 80 90 100
LAQTTAAGTS ELNHGPAGAA APAAPGPGAL NCAHGSSALP RGAPGSRRPE
110 120 130 140 150
DECPIAAGAA GAPASRGDEE EPDSAPEKGR SSGPSARKGK GQIEKRKLRE
160 170 180 190 200
KRRSTGVVNI PAAECLDEYE DDEAGQKERK REDAITQQNT IQNEAASLPD
210 220 230 240 250
PGTSYLPQDP SRTVPGRYKS TISAPEEEIL NRYPRTDRSG FSRHNRDTSA
260 270 280 290 300
PANFASSSTL EKRIEDLEKE VLRERQENLR LTRLMQDKEE MIGKLKEEID
310 320 330
LLNRDLDDME DENEQLKQEN KTLLKVVGQL TR
Length:332
Mass (Da):35,866
Last modified:November 1, 1996 - v1
Checksum:i2069B32DEFFF160F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U05989 mRNA. Translation: AAA16492.1.
RefSeqiNP_277020.1. NM_033485.2.
UniGeneiRn.9127.

Genome annotation databases

GeneIDi64513.
KEGGirno:64513.
UCSCiRGD:69065. rat.

Similar proteinsi

Entry informationi

Entry nameiPAWR_RAT
AccessioniPrimary (citable) accession number: Q62627
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: November 1, 1996
Last modified: November 22, 2017
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references