ID   RNAS1_SAISC             Reviewed;         156 AA.
AC   Q8SQ08;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Ribonuclease pancreatic;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1;
DE   AltName: Full=RNase A;
DE   Flags: Precursor;
GN   Name=RNASE1;
OS   Saimiri sciureus (Common squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=9521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11925567; DOI=10.1038/ng852;
RA   Zhang J., Zhang Y.-P., Rosenberg H.F.;
RT   "Adaptive evolution of a duplicated pancreatic ribonuclease gene in a leaf-
RT   eating monkey.";
RL   Nat. Genet. 30:411-415(2002).
CC   -!- FUNCTION: Endonuclease that catalyzes the cleavage of RNA on the 3'
CC       side of pyrimidine nucleotides. Acts on single-stranded and double-
CC       stranded RNA (By 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   -!- 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   -!- SUBUNIT: Monomer. Interacts with and forms tight 1:1 complexes with
CC       RNH1. Dimerization of two such complexes may occur. Interaction with
CC       RNH1 inhibits this protein (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AF449637; AAL87058.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8SQ08; -.
DR   SMR; Q8SQ08; -.
DR   GO; GO:0005576; C:extracellular region; 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   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   3: Inferred from homology;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000250"
FT   CHAIN           29..156
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000030943"
FT   REGION          33..52
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        40
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        54..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..123
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   156 AA;  17611 MW;  990BDEB3DA366700 CRC64;
     MALEKSLALL PLLVLVLLVL GWVQPSLGRE SRAKKFQRQH MDSDGSPSSN PTYCNDMMRR
     RNMTQGRCKP VNTFVHEPLV DVQDVCFQEK VTCKNGQANC YKSSSSMHIT DCRLTNGSRY
     PNCAYRTSQK ERHIIVACEG NPYVPVHFDA SVEDST