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2-5A-dependent ribonuclease (2-5A-dependent RNase) (EC 3.1.26.-) (Ribonuclease 4) (Ribonuclease L) (RNase L)

 RN5A_MOUSE              Reviewed;         735 AA.
Q05921; Q9ERU7;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
11-FEB-2002, sequence version 2.
12-SEP-2018, entry version 161.
RecName: Full=2-5A-dependent ribonuclease;
Short=2-5A-dependent RNase;
EC=3.1.26.-;
AltName: Full=Ribonuclease 4;
AltName: Full=Ribonuclease L;
Short=RNase L;
Name=Rnasel; Synonyms=Rns4;
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].
STRAIN=C3H/An; TISSUE=Adipose tissue;
PubMed=11063255; DOI=10.1007/s003350010194;
Zhou A., Nie H., Silverman R.H.;
"Analysis and origins of the human and mouse RNase L genes: mediators
of interferon action.";
Mamm. Genome 11:989-992(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-679.
PubMed=7680958; DOI=10.1016/0092-8674(93)90403-D;
Zhou A., Hassel B.A., Silverman R.H.;
"Expression cloning of 2-5A-dependent RNAase: a uniquely regulated
mediator of interferon action.";
Cell 72:753-765(1993).
[3]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11585831; DOI=10.1074/jbc.M107482200;
Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B.,
Salehzada T.;
"The 2-5A/RNase L/RNase L inhibitor (RNI) pathway regulates
mitochondrial mRNAs stability in interferon alpha-treated H9 cells.";
J. Biol. Chem. 276:48473-48482(2001).
[4]
ERRATUM.
Le Roy F., Bisbal C., Silhol M., Martinand C., Lebleu B.,
Salehzada T.;
J. Biol. Chem. 277:13354-13354(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
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).
-!- FUNCTION: Endoribonuclease that functions in the interferon (IFN)
antiviral response. In INF treated and virus infected cells,
RNASEL probably mediates its antiviral effects through a
combination of direct cleavage of single-stranded viral RNAs,
inhibition of protein synthesis through the degradation of rRNA,
induction of apoptosis, and induction of other antiviral genes.
RNASEL mediated apoptosis is the result of a JNK-dependent stress-
response pathway leading to cytochrome c release from mitochondria
and caspase-dependent apoptosis. Therefore, activation of RNASEL
could lead to elimination of virus infected cells under some
circumstances. In the crosstalk between autophagy and apoptosis
proposed to induce autophagy as an early stress response to small
double-stranded RNA and at later stages of prolonged stress to
activate caspase-dependent proteolytic cleavage of BECN1 to
terminate autophagy and promote apoptosis. Might play a central
role in the regulation of mRNA turnover (By similarity). Cleaves
3' of UpNp dimers, with preference for UU and UA sequences, to
sets of discrete products ranging from between 4 and 22
nucleotides in length (By similarity).
{ECO:0000250|UniProtKB:Q05823, ECO:0000269|PubMed:11585831}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Manganese or magnesium. Required for optimal RNA cleavage
rates.;
-!- ACTIVITY REGULATION: After binding to 2-5A (5'-phosphorylated
2',5'-linked oligoadenylates) the homodimerization and subsequent
activation occurs. Inhibited by RNASEL inhibitor ABCE1/RLI, a
cytoplasmic member of the ATP-binding cassette (ABC) transporter
family (By similarity). {ECO:0000250}.
-!- SUBUNIT: Monomer (inactive form) or homodimer. Interacts with
ABCE1; this interaction inhibits the RNASEL (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11585831}.
Mitochondrion {ECO:0000269|PubMed:11585831}.
-!- TISSUE SPECIFICITY: Expressed in spleen, thymus, lung, testis,
kidney, liver and heart.
-!- INDUCTION: By interferons. Virus replication in higher vertebrates
is restrained by IFNs that cause cells to transcribe genes
encoding antiviral proteins, such as 2'-5' oligoadenylate
synthetases (OASs). oligoadenylate synthetase is stimulated by
dsRNA to produce 5'-phosphorylated, 2'-5'-linked oligoadenylates
(2-5A), whose function is to activate RNASEL.
-!- DOMAIN: The nine ankyrin repeats also called 2-5A sensor
constitute the N-terminus 2-5A binding domain.
-!- DOMAIN: The protein kinase domain is predicted to be catalytically
inactive. It allows the homodimerization.
-!- DOMAIN: The ribonuclease domain is located in the C-terminus. A
single active nuclease domain in a dimer is sufficient for
ribonuclease activity.
-!- SIMILARITY: Belongs to the protein kinase superfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF281045; AAG33708.1; -; mRNA.
EMBL; L10382; AAA37117.1; -; Genomic_DNA.
CCDS; CCDS15377.1; -.
PIR; B45771; B45771.
RefSeq; NP_036012.1; NM_011882.2.
RefSeq; XP_006529590.1; XM_006529527.3.
RefSeq; XP_006529591.1; XM_006529528.3.
RefSeq; XP_006529593.1; XM_006529530.2.
RefSeq; XP_011246295.1; XM_011247993.2.
UniGene; Mm.259254; -.
ProteinModelPortal; Q05921; -.
SMR; Q05921; -.
STRING; 10090.ENSMUSP00000083385; -.
BindingDB; Q05921; -.
ChEMBL; CHEMBL2687; -.
iPTMnet; Q05921; -.
PhosphoSitePlus; Q05921; -.
EPD; Q05921; -.
MaxQB; Q05921; -.
PaxDb; Q05921; -.
PRIDE; Q05921; -.
Ensembl; ENSMUST00000086209; ENSMUSP00000083385; ENSMUSG00000066800.
GeneID; 24014; -.
KEGG; mmu:24014; -.
UCSC; uc007daf.1; mouse.
CTD; 6041; -.
MGI; MGI:1098272; Rnasel.
eggNOG; KOG1027; Eukaryota.
eggNOG; KOG4177; Eukaryota.
eggNOG; COG0666; LUCA.
GeneTree; ENSGT00920000148967; -.
HOGENOM; HOG000276879; -.
HOVERGEN; HBG012673; -.
InParanoid; Q05921; -.
KO; K01165; -.
OMA; DCGDLVM; -.
OrthoDB; EOG091G03H3; -.
PhylomeDB; Q05921; -.
TreeFam; TF344032; -.
Reactome; R-MMU-909733; Interferon alpha/beta signaling.
PRO; PR:Q05921; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000066800; Expressed in 218 organ(s), highest expression level in blood.
ExpressionAtlas; Q05921; baseline and differential.
Genevisible; Q05921; MM.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016363; C:nuclear matrix; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
GO; GO:0004540; F:ribonuclease activity; ISO:MGI.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0019843; F:rRNA binding; ISO:MGI.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
GO; GO:0006397; P:mRNA processing; IEA:InterPro.
GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IMP:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0043488; P:regulation of mRNA stability; IMP:MGI.
GO; GO:0006364; P:rRNA processing; ISO:MGI.
CDD; cd00204; ANK; 2.
Gene3D; 1.20.1440.180; -; 1.
Gene3D; 1.25.40.20; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
InterPro; IPR010513; KEN_dom.
InterPro; IPR038357; KEN_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR018997; PUB_domain.
Pfam; PF12796; Ank_2; 2.
Pfam; PF13606; Ank_3; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF06479; Ribonuc_2-5A; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 8.
SMART; SM00580; PUG; 1.
SUPFAM; SSF48403; SSF48403; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 7.
PROSITE; PS51392; KEN; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
1: Evidence at protein level;
ANK repeat; Antiviral defense; ATP-binding; Complete proteome;
Cytoplasm; Endonuclease; Hydrolase; Metal-binding; Mitochondrion;
Nuclease; Nucleotide-binding; Reference proteome; Repeat; RNA-binding;
Zinc; Zinc-finger.
CHAIN 1 735 2-5A-dependent ribonuclease.
/FTId=PRO_0000067052.
REPEAT 24 53 ANK 1.
REPEAT 58 87 ANK 2.
REPEAT 91 120 ANK 3.
REPEAT 124 153 ANK 4.
REPEAT 167 197 ANK 5.
REPEAT 201 234 ANK 6.
REPEAT 238 268 ANK 7.
REPEAT 272 301 ANK 8.
REPEAT 303 328 ANK 9.
DOMAIN 364 584 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 587 722 KEN. {ECO:0000255|PROSITE-
ProRule:PRU00725}.
ZN_FING 401 436 C6-type. {ECO:0000255}.
REGION 229 242 2-5A binding (P-loop) 1.
REGION 253 275 2-5A binding (P-loop) 2.
SEQUENCE 735 AA; 83275 MW; B6632F4A5B50F711 CRC64;
METPDYNTPQ GGTPSAGSQR TVVEDDSSLI KAVQKGDVVR VQQLLEKGAD ANACEDTWGW
TPLHNAVQAG RVDIVNLLLS HGADPHRRKK NGATPFIIAG IQGDVKLLEI LLSCGADVNE
CDENGFTAFM EAAERGNAEA LRFLFAKGAN VNLRRQTTKD KRRLKQGGAT ALMSAAEKGH
LEVLRILLND MKAEVDARDN MGRNALIRTL LNWDCENVEE ITSILIQHGA DVNVRGERGK
TPLIAAVERK HTGLVQMLLS REGINIDARD NEGKTALLIA VDKQLKEIVQ LLLEKGADKC
DDLVWIARRN HDYHLVKLLL PYVANPDTDP PAGDWSPHSS RWGTALKSLH SMTRPMIGKL
KIFIHDDYKI AGTSEGAVYL GIYDNREVAV KVFRENSPRG CKEVSCLRDC GDHSNLVAFY
GREDDKGCLY VCVSLCEWTL EEFLRLPREE PVENGEDKFA HSILLSIFEG VQKLHLHGYS
HQDLQPQNIL IDSKKAVRLA DFDQSIRWMG ESQMVRRDLE DLGRLVLYVV MKGEIPFETL
KTQNDEVLLT MSPDEETKDL IHCLFSPGEN VKNCLVDLLG HPFFWTWENR YRTLRNVGNE
SDIKVRKCKS DLLRLLQHQT LEPPRSFDQW TSKIDKNVMD EMNHFYEKRK KNPYQDTVGD
LLKFIRNIGE HINEEKKRGM KEILGDPSRY FQETFPDLVI YIYKKLKETE YRKHFPQPPP
RLSVPEAVGP GGIQS


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