ID   RNAS2_CALJA             Reviewed;         158 AA.
AC   Q8SPY2;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 87.
DE   RecName: Full=Non-secretory ribonuclease;
DE            EC=4.6.1.18 {ECO:0000250|UniProtKB:O18937};
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   Callithrix jacchus (White-tufted-ear marmoset) (Simia Jacchus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11917138; DOI=10.1073/pnas.072626199;
RA   Zhang J., Rosenberg H.F.;
RT   "Complementary advantageous substitutions in the evolution of an antiviral
RT   RNase of higher primates.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:5486-5491(2002).
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 (By
CC       similarity). {ECO:0000250}.
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:O18937};
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:O18937};
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       {ECO:0000250}. Note=Matrix of eosinophil's large specific granule.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Arg-34 is present instead of the conserved Trp which is
CC       expected to be C-glycosylated by mannose. {ECO:0000305}.
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DR   EMBL; AF479634; AAM14441.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8SPY2; -.
DR   SMR; Q8SPY2; -.
DR   FunCoup; Q8SPY2; 36.
DR   STRING; 9483.ENSCJAP00000017651; -.
DR   GlyCosmos; Q8SPY2; 3 sites, No reported glycans.
DR   eggNOG; ENOG502TF52; Eukaryota.
DR   InParanoid; Q8SPY2; -.
DR   Proteomes; UP000008225; Unplaced.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR   GO; GO:0006935; P:chemotaxis; IEA:TreeGrafter.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-ARBA.
DR   GO; GO:0002227; P:innate immune response in mucosa; IEA:TreeGrafter.
DR   CDD; cd06265; RNase_A_canonical; 1.
DR   FunFam; 3.10.130.10:FF:000001; Ribonuclease pancreatic; 1.
DR   Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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:SF62; NON-SECRETORY RIBONUCLEASE; 1.
DR   PANTHER; PTHR11437; RIBONUCLEASE; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; RNase A-like; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Glycoprotein; Hydrolase; Lyase; Lysosome; Nitration;
KW   Nuclease; Reference proteome; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..158
FT                   /note="Non-secretory ribonuclease"
FT                   /id="PRO_0000251795"
FT   ACT_SITE        42
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        153
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        86
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"
SQ   SEQUENCE   158 AA;  17598 MW;  07275DE03F0B3A78 CRC64;
     MVPKLFTSQI CLLPLLGLLS AEGSPHARPQ QYSRAQWFSI QHIQTAPLHC TSAMRAINKY
     QSRCKNKNTF LHTTFADVVN VCGNTNMTCP HNASLNNCHH SGVQVPLTYC NLTGPQTISN
     CVYSSTQANK FYVVACENRD PRDPPQYPVV PVHLDTII
//