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Interferon-inducible double-stranded RNA-dependent protein kinase activator A (PKR-associated protein X) (PKR-associating protein X) (RAX) (Protein activator of the interferon-induced protein kinase) (Protein kinase, interferon-inducible double-stranded RNA-dependent activator)

 PRKRA_MOUSE             Reviewed;         313 AA.
Q9WTX2; Q9CZB7;
21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 140.
RecName: Full=Interferon-inducible double-stranded RNA-dependent protein kinase activator A;
AltName: Full=PKR-associated protein X;
AltName: Full=PKR-associating protein X;
Short=RAX;
AltName: Full=Protein activator of the interferon-induced protein kinase;
AltName: Full=Protein kinase, interferon-inducible double-stranded RNA-dependent activator;
Name=Prkra; Synonyms=Rax;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH EIF2AK2, TISSUE
SPECIFICITY, AND PHOSPHORYLATION.
PubMed=10336432; DOI=10.1074/jbc.274.22.15427;
Ito T., Yang M., May W.S.;
"RAX, a cellular activator for double-stranded RNA-dependent protein
kinase during stress signaling.";
J. Biol. Chem. 274:15427-15432(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
FUNCTION, AND INTERACTION WITH UBC9.
PubMed=22214662; DOI=10.4161/cc.11.2.18999;
Bennett R.L., Pan Y., Christian J., Hui T., May W.S. Jr.;
"The RAX/PACT-PKR stress response pathway promotes p53 sumoylation and
activation, leading to G(1) arrest.";
Cell Cycle 11:407-417(2012).
-!- FUNCTION: Required for siRNA production by DICER1 and for
subsequent siRNA-mediated post-transcriptional gene silencing.
Does not seem to be required for processing of pre-miRNA to miRNA
by DICER1 (By similarity). Activates EIF2AK2/PKR in the absence of
double-stranded RNA (dsRNA), leading to phosphorylation of
EIF2S1/EFI2-alpha and inhibition of translation and induction of
apoptosis. Promotes UBC9-p53/TP53 association and sumoylation and
phosphorylation of p53/TP53 at 'Lys-386' at 'Ser-392' respectively
and enhances its activity in a EIF2AK2/PKR-dependent manner.
{ECO:0000250, ECO:0000269|PubMed:10336432,
ECO:0000269|PubMed:22214662}.
-!- SUBUNIT: Homodimer. Interacts with DICER1, AGO2 and TARBP2. Also
able to interact with dsRNA (By similarity). Interacts with
EIF2AK2/PKR through its DRBM domains. Interacts with DUS2L (via
DRBM domain) (By similarity). Interacts with UBC9. Forms a complex
with UBC9 and p53/TP53. {ECO:0000250, ECO:0000269|PubMed:10336432,
ECO:0000269|PubMed:22214662}.
-!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver,
lung, muscle, spleen and testis. {ECO:0000269|PubMed:10336432}.
-!- DOMAIN: Self-association may occur via interactions between DRBM
domains as follows: DRBM 1/DRBM 1, DRBM 1/DRBM 2, DRBM 2/DRBM 2 or
DRBM 3/DRBM3. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-246 in unstressed cells and at Ser-287
in stressed cells. Phosphorylation at Ser-246 appears to be a
prerequisite for subsequent phosphorylation at Ser-287.
Phosphorylation at Ser-246 and Ser-287 are necessary for
activation of EIF2AK2/PKR under conditions of stress (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the PRKRA family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF083032; AAD33098.1; -; mRNA.
EMBL; AK012798; BAB28477.1; -; mRNA.
EMBL; AK155112; BAE33056.1; -; mRNA.
EMBL; BC011311; AAH11311.1; -; mRNA.
CCDS; CCDS16159.1; -.
RefSeq; NP_036001.1; NM_011871.2.
UniGene; Mm.277250; -.
ProteinModelPortal; Q9WTX2; -.
SMR; Q9WTX2; -.
ComplexPortal; CPX-1073; RISC-loading complex, PRKRA variant.
IntAct; Q9WTX2; 4.
MINT; Q9WTX2; -.
STRING; 10090.ENSMUSP00000002808; -.
iPTMnet; Q9WTX2; -.
PhosphoSitePlus; Q9WTX2; -.
EPD; Q9WTX2; -.
MaxQB; Q9WTX2; -.
PaxDb; Q9WTX2; -.
PeptideAtlas; Q9WTX2; -.
PRIDE; Q9WTX2; -.
Ensembl; ENSMUST00000002808; ENSMUSP00000002808; ENSMUSG00000002731.
GeneID; 23992; -.
KEGG; mmu:23992; -.
UCSC; uc008kff.1; mouse.
CTD; 8575; -.
MGI; MGI:1344375; Prkra.
eggNOG; KOG3732; Eukaryota.
eggNOG; ENOG410XSCK; LUCA.
GeneTree; ENSGT00900000141030; -.
HOGENOM; HOG000231919; -.
HOVERGEN; HBG001700; -.
InParanoid; Q9WTX2; -.
OMA; VTVCHGT; -.
OrthoDB; EOG091G0I2L; -.
PhylomeDB; Q9WTX2; -.
TreeFam; TF315953; -.
Reactome; R-MMU-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-MMU-426486; Small interfering RNA (siRNA) biogenesis.
PRO; PR:Q9WTX2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000002731; Expressed in 265 organ(s), highest expression level in dorsal pancreas.
CleanEx; MM_RAX; -.
Genevisible; Q9WTX2; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005622; C:intracellular; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0070578; C:RISC-loading complex; ISO:MGI.
GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0070883; F:pre-miRNA binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:MGI.
GO; GO:0043583; P:ear development; IMP:MGI.
GO; GO:0042474; P:middle ear morphogenesis; IMP:MGI.
GO; GO:0042473; P:outer ear morphogenesis; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0031054; P:pre-miRNA processing; ISO:MGI.
GO; GO:0035196; P:production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0030422; P:production of siRNA involved in RNA interference; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0050821; P:protein stabilization; ISO:MGI.
GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
CDD; cd00048; DSRM; 3.
InterPro; IPR014720; dsRBD_dom.
InterPro; IPR033363; PRKRA.
InterPro; IPR032478; Staufen_C.
PANTHER; PTHR10910:SF8; PTHR10910:SF8; 1.
Pfam; PF00035; dsrm; 2.
Pfam; PF16482; Staufen_C; 1.
SMART; SM00358; DSRM; 3.
PROSITE; PS50137; DS_RBD; 3.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Phosphoprotein; Reference proteome;
Repeat; RNA-binding; RNA-mediated gene silencing.
CHAIN 1 313 Interferon-inducible double-stranded RNA-
dependent protein kinase activator A.
/FTId=PRO_0000223610.
DOMAIN 34 101 DRBM 1. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 126 194 DRBM 2. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
DOMAIN 240 308 DRBM 3. {ECO:0000255|PROSITE-
ProRule:PRU00266}.
REGION 1 103 Sufficient for self-association and
interaction with TARBP2. {ECO:0000250}.
REGION 102 195 Sufficient for self-association and
interaction with TARBP2. {ECO:0000250}.
REGION 195 313 Sufficient for self-association and
interaction with TARBP2. {ECO:0000250}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000250|UniProtKB:O75569}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000250|UniProtKB:O75569}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000250|UniProtKB:O75569}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000250|UniProtKB:O75569}.
CONFLICT 177 177 K -> N (in Ref. 2; BAB28477).
{ECO:0000305}.
SEQUENCE 313 AA; 34371 MW; 6EDF248A55A391D2 CRC64;
MSHSRHRAEA PPLQREDSGT FSLGKMITAK PGKTPIQVLH EYGMKTKNIP VYECERSDVQ
VHVPTFTFRV TVGDITCTGE GTSKKLAKHR AAEAAINILK ANASICFAVP DPLMPDPSKQ
PKNQLNPIGS LQELAIHHGW RLPEYTLSQE GGPAHKREYT TICRLESFME TGKGASKKQA
KRNAAEKFLA KFSNISPENH ISLTNVVGHS LGCTWHSLRN SPGEKINLLK RSLLSLPNTD
YIQLLSEIAS EQGFNITYLD IEELSANGQY QCLAELSTSP ITVCHGSGIS CGNAQSDAAH
NALQYLKIIA ERK


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