RNS2B_MOUSE
ID RNS2B_MOUSE Reviewed; 155 AA.
AC O35292; Q8K416;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ribonuclease 2B {ECO:0000312|MGI:MGI:1858598};
DE EC=4.6.1.18 {ECO:0000250|UniProtKB:P10153};
DE AltName: Full=Eosinophil cationic-type ribonuclease 5 {ECO:0000305};
DE AltName: Full=MR-5 {ECO:0000305};
DE Flags: Precursor;
GN Name=Rnase2b {ECO:0000312|MGI:MGI:1858598};
GN Synonyms=Ear5 {ECO:0000312|MGI:MGI:1858598};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Fibroblast;
RX PubMed=9336452; DOI=10.1093/nar/25.21.4235;
RA Batten D., Dyer K.D., Domachowske J.B., Rosenberg H.F.;
RT "Molecular cloning of four novel murine ribonuclease genes: unusual
RT expansion within the ribonuclease A gene family.";
RL Nucleic Acids Res. 25:4235-4239(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Moreau J.M., McDevitt A.L., Rosenberg H.F., Dyer K.D.;
RT "Transcriptional activation of the mouse eosinophil-associated ribonuclease
RT 2 (Ear2) gene by an intronic enhancer element that binds NFATc1.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NITRATION.
RX PubMed=18694936; DOI=10.1074/jbc.m801196200;
RA Ulrich M., Petre A., Youhnovski N., Proemm F., Schirle M., Schumm M.,
RA Pero R.S., Doyle A., Checkel J., Kita H., Thiyagarajan N., Acharya K.R.,
RA Schmid-Grendelmeier P., Simon H.-U., Schwarz H., Tsutsui M., Shimokawa H.,
RA Bellon G., Lee J.J., Przybylski M., Doering G.;
RT "Post-translational tyrosine nitration of eosinophil granule toxins
RT mediated by eosinophil peroxidase.";
RL J. Biol. Chem. 283:28629-28640(2008).
CC -!- FUNCTION: This is a non-secretory ribonuclease. It is a pyrimidine
CC specific nuclease with a slight preference for U. Cytotoxin and
CC helminthotoxin. Possesses a wide variety of biological activities.
CC {ECO:0000250|UniProtKB:P10153}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing cytidine + H2O = an [RNA]-3'-cytidine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P10153};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an [RNA] containing uridine + H2O = an [RNA]-3'-uridine-3'-
CC phosphate + a 5'-hydroxy-ribonucleotide-3'-[RNA].; EC=4.6.1.18;
CC Evidence={ECO:0000250|UniProtKB:P10153};
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AF017260; AAC53491.1; -; Genomic_DNA.
DR EMBL; AF512013; AAM44856.1; -; Genomic_DNA.
DR EMBL; AC163664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466605; EDL20848.1; -; Genomic_DNA.
DR EMBL; BC117776; AAI17777.1; -; mRNA.
DR EMBL; BC119506; AAI19507.1; -; mRNA.
DR CCDS; CCDS27039.1; -.
DR RefSeq; NP_062271.2; NM_019398.2.
DR AlphaFoldDB; O35292; -.
DR SMR; O35292; -.
DR STRING; 10090.ENSMUSP00000075074; -.
DR GlyGen; O35292; 1 site.
DR iPTMnet; O35292; -.
DR PhosphoSitePlus; O35292; -.
DR PaxDb; O35292; -.
DR PRIDE; O35292; -.
DR ProteomicsDB; 260827; -.
DR DNASU; 54159; -.
DR Ensembl; ENSMUST00000075648; ENSMUSP00000075074; ENSMUSG00000059606.
DR GeneID; 54159; -.
DR KEGG; mmu:54159; -.
DR UCSC; uc007tmt.2; mouse.
DR CTD; 54159; -.
DR MGI; MGI:1858598; Rnase2b.
DR VEuPathDB; HostDB:ENSMUSG00000059606; -.
DR eggNOG; ENOG502TF52; Eukaryota.
DR GeneTree; ENSGT00940000162253; -.
DR HOGENOM; CLU_117006_0_1_1; -.
DR InParanoid; O35292; -.
DR OMA; RISTNCH; -.
DR OrthoDB; 1482425at2759; -.
DR PhylomeDB; O35292; -.
DR TreeFam; TF333393; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 54159; 3 hits in 72 CRISPR screens.
DR PRO; PR:O35292; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; O35292; protein.
DR Bgee; ENSMUSG00000059606; Expressed in lip and 23 other tissues.
DR ExpressionAtlas; O35292; baseline and differential.
DR Genevisible; O35292; MM.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR GO; GO:0004540; F:ribonuclease activity; ISO:MGI.
DR GO; GO:0006935; P:chemotaxis; IBA:GO_Central.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0002227; P:innate immune response in mucosa; IBA:GO_Central.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR001427; RNaseA.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR InterPro; IPR023411; RNaseA_AS.
DR InterPro; IPR023412; RNaseA_domain.
DR PANTHER; PTHR11437; PTHR11437; 1.
DR Pfam; PF00074; RnaseA; 1.
DR PRINTS; PR00794; RIBONUCLEASE.
DR SMART; SM00092; RNAse_Pc; 1.
DR SUPFAM; SSF54076; SSF54076; 1.
DR PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nitration;
KW Nuclease; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..155
FT /note="Ribonuclease 2B"
FT /evidence="ECO:0000305"
FT /id="PRO_0000030870"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..106
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT DISULFID 61..118
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT DISULFID 79..133
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT DISULFID 86..94
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT CONFLICT 35
FT /note="D -> A (in Ref. 1; AAC53491)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="A -> G (in Ref. 1; AAC53491)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 155 AA; 17514 MW; E22D48C15634065A CRC64;
MGLKLLESRL CLLLLLGLVL TLVSCQRPTP SQKFDIQHIY KKSSPKCDDA MRVVNKYTGK
CKDLNTFLHT TFADVVRVCH NPPKTCKDGT SPNCHDSSSK VSVTICKLTK RARNYTHCRY
KTTGAKKSYT VACNPRTPKD RPTYPVVPVH LDRLF
