ID   RNAS2_MACFA             Reviewed;         160 AA.
AC   P47783;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Non-secretory ribonuclease;
DE            EC=4.6.1.18 {ECO:0000269|PubMed:7663519};
DE   AltName: Full=Eosinophil-derived neurotoxin;
DE   AltName: Full=RNase UpI-2;
DE   AltName: Full=Ribonuclease 2;
DE            Short=RNase 2;
DE   AltName: Full=Ribonuclease US;
DE   Flags: Precursor;
GN   Name=RNASE2; Synonyms=EDN, RNS2;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=7663519; DOI=10.1038/ng0695-219;
RA   Rosenberg H.F., Dyer K.D., Tiffany H.L., Gonzalez M.;
RT   "Rapid evolution of a unique family of primate ribonuclease genes.";
RL   Nat. Genet. 10:219-223(1995).
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:0000269|PubMed:7663519}.
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:0000269|PubMed:7663519};
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:0000269|PubMed:7663519};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 uM for yeast tRNA (in the presence of 40 mM sodium phosphate
CC         at pH 7.0) {ECO:0000269|PubMed:7663519};
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; U24096; AAC50145.1; -; Genomic_DNA.
DR   PIR; I84444; I84444.
DR   AlphaFoldDB; P47783; -.
DR   SMR; P47783; -.
DR   STRING; 9541.XP_005560776.1; -.
DR   eggNOG; ENOG502TF52; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
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; IDA:UniProtKB.
DR   GO; GO:0051607; P:defense response to virus; IDA:UniProtKB.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IDA:UniProtKB.
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..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..160
FT                   /note="Non-secretory ribonuclease"
FT                   /id="PRO_0000030876"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        155
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         60
FT                   /note="3'-nitrotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P10153"
FT   CARBOHYD        34
FT                   /note="C-linked (Man) tryptophan"
FT                   /evidence="ECO:0000250|UniProtKB:P10153"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..122
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..137
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..98
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   160 AA;  18000 MW;  918F7840BC40C6F3 CRC64;
     MVPKLFTSQI CLLLLLGLMG VEGSLHAKPG QFTWAQWFEI QHINMTSGQC TNAMQVINNY
     QRRCKNQNTF LLTTFADVVH VCGNPSMPCP SNTSLNNCHH SGVQVPLIHC NLTTPSRRIS
     NCRYTQTTAN KYYIVACNNS DPVRDPPQYP VVPVHLDRII