PRKAB_XENLA
ID PRKAB_XENLA Reviewed; 298 AA.
AC Q91836;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Interferon-inducible double-stranded RNA-dependent protein kinase activator A homolog B;
DE AltName: Full=Double-stranded RNA-binding protein A;
DE AltName: Full=XlRBPA;
GN Name=prkra-b; Synonyms=rbpa;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], RNA-BINDING, ASSOCIATION WITH RIBOSOMES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9230068; DOI=10.1083/jcb.138.2.239;
RA Eckmann C.R., Jantsch M.F.;
RT "Xlrbpa, a double-stranded RNA-binding protein associated with ribosomes
RT and heterogeneous nuclear RNPs.";
RL J. Cell Biol. 138:239-253(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 112-180.
RX PubMed=9857205; DOI=10.1093/emboj/17.24.7505;
RA Ryter J.M., Schultz S.C.;
RT "Molecular basis of double-stranded RNA-protein interactions: structure of
RT a dsRNA-binding domain complexed with dsRNA.";
RL EMBO J. 17:7505-7513(1998).
CC -!- FUNCTION: Activates eif2ak2/pkr in the absence of double-stranded RNA
CC (dsRNA), leading to phosphorylation of eif2s1/efi2-alpha and inhibition
CC of translation and induction of apoptosis. Required for siRNA
CC production by dicer1 and for subsequent siRNA-mediated post-
CC transcriptional gene silencing. Does not seem to be required for
CC processing of pre-miRNA to miRNA by dicer1 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with dicer1 and eif2ak2/pkr. Also able to
CC interact with dsRNA (By similarity). Associates with ribosomes.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}.
CC Nucleus {ECO:0000269|PubMed:9230068}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:9230068}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, nerve and
CC spleen. {ECO:0000269|PubMed:9230068}.
CC -!- SIMILARITY: Belongs to the PRKRA family. {ECO:0000305}.
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DR EMBL; M96370; AAA49947.1; -; mRNA.
DR PIR; S27945; S27945.
DR PDB; 1DI2; X-ray; 1.90 A; A/B=112-180.
DR PDBsum; 1DI2; -.
DR AlphaFoldDB; Q91836; -.
DR SMR; Q91836; -.
DR EvolutionaryTrace; Q91836; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro.
DR GO; GO:0030422; P:siRNA processing; ISS:UniProtKB.
DR CDD; cd19889; DSRM_PRKRA_rpt1; 1.
DR CDD; cd19891; DSRM_PRKRA_rpt2; 1.
DR CDD; cd19892; DSRM_PRKRA_rpt3; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR033363; PRKRA.
DR InterPro; IPR044465; PRKRA_DSRM_1.
DR InterPro; IPR044466; PRKRA_DSRM_2.
DR InterPro; IPR044467; PRKRA_DSRM_3.
DR InterPro; IPR032478; Staufen_C.
DR PANTHER; PTHR46205:SF2; PTHR46205:SF2; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Repeat; RNA-binding;
KW RNA-mediated gene silencing.
FT CHAIN 1..298
FT /note="Interferon-inducible double-stranded RNA-dependent
FT protein kinase activator A homolog B"
FT /id="PRO_0000065624"
FT DOMAIN 20..87
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 112..180
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 225..293
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:1DI2"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:1DI2"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:1DI2"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1DI2"
FT STRAND 154..162
FT /evidence="ECO:0007829|PDB:1DI2"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:1DI2"
SQ SEQUENCE 298 AA; 32852 MW; 8624D02F3AA1AFB1 CRC64;
MSSEKPTSLN AMRATNPCET PIQLLHEFGT KTGNHPVYTL EKAEGQAHNP SFTFRLVIGD
ITSLGEGPSK KTPKQKAAEF ALNILRGDTS KCLPVTDTLR DPKKPPNQMQ ENPVGSLQEL
AVQKGWRLPE YTVAQESGPP HKREFTITCR VETFVETGSG TSKQVAKRVA AEKLLTKFKT
ISTDNIPLNK LIGNKMGCTW DSMRNSSGEK ISMLKRSPLS IPNTDYVKML KDVAEELDFN
LTYLDIDELS VNGQYQCLAE LSTNPITVCH GTGISCGNAH NDAAHNALQY LKIMCIKK