RNAS2_MOUSE
ID RNAS2_MOUSE Reviewed; 155 AA.
AC O35291;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Non-secretory ribonuclease;
DE EC=4.6.1.18 {ECO:0000250|UniProtKB:P47784};
DE AltName: Full=Eosinophil cationic-type ribonuclease 4;
DE AltName: Full=MR-4;
DE AltName: Full=Ribonuclease 2;
DE Short=RNase 2;
DE Flags: Precursor;
GN Name=Rnase2; Synonyms=Ear4;
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 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 -!- 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:P47784};
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:P47784};
CC -!- SUBUNIT: Interacts with and forms a tight 1:1 complex with RNH1.
CC Dimerization of two such complexes may occur (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Lysosome {ECO:0000305}. Cytoplasmic granule.
CC Note=Matrix of eosinophil's large specific granule.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
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DR EMBL; AF017259; AAC53490.1; -; Genomic_DNA.
DR RefSeq; NP_001017422.1; NM_001017422.1.
DR AlphaFoldDB; O35291; -.
DR SMR; O35291; -.
DR STRING; 10090.ENSMUSP00000056293; -.
DR GlyGen; O35291; 4 sites.
DR PhosphoSitePlus; O35291; -.
DR PRIDE; O35291; -.
DR DNASU; 53877; -.
DR GeneID; 53877; -.
DR KEGG; mmu:53877; -.
DR CTD; 53877; -.
DR MGI; MGI:1858238; Ear4.
DR eggNOG; ENOG502TF52; Eukaryota.
DR InParanoid; O35291; -.
DR PhylomeDB; O35291; -.
DR BioGRID-ORCS; 53877; 0 hits in 15 CRISPR screens.
DR ChiTaRS; Ear2; mouse.
DR PRO; PR:O35291; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O35291; protein.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
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; Lysosome;
KW Nitration; Nuclease; Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..155
FT /note="Non-secretory ribonuclease"
FT /id="PRO_0000030882"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 150
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 33
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..66
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 57
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P10153"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 107
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..106
FT /evidence="ECO:0000250"
FT DISULFID 61..118
FT /evidence="ECO:0000250"
FT DISULFID 79..133
FT /evidence="ECO:0000250"
FT DISULFID 86..94
FT /evidence="ECO:0000250"
SQ SEQUENCE 155 AA; 17723 MW; 36879AAF1CCFB961 CRC64;
MGPKLLESRL CLLLLLGLVL MLASCQAQIL SQKFYTQHIY NSTYPRCDAV MRVVNRYRPR
CKDINTFLHT SFADVVAVCG HPNITCNNLT RKNCHASSFQ VFITFCNLTM PTRICTQCRY
QTTGSVKYYR VACENRTPQD TPMYPVVPVH LDGTF
