ID   RNAS1_CRIGR             Reviewed;         130 AA.
AC   P24717;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   04-NOV-2026, entry version 112.
DE   RecName: Full=Ribonuclease pancreatic;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1;
DE   AltName: Full=RNase A;
DE   Flags: Precursor; Fragment;
GN   Name=RNASE1; Synonyms=RNS1;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Ovary;
RX   PubMed=1741299; DOI=10.1093/nar/20.3.612;
RA   Haugg M., Schein C.H.;
RT   "The DNA sequences of the human and hamster secretory ribonucleases
RT   determined with the polymerase chain reaction (PCR).";
RL   Nucleic Acids Res. 20:612-612(1992).
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.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; X62945; CAA44717.1; -; Genomic_DNA.
DR   PIR; S22808; S22808.
DR   SMR; P24717; -.
DR   GlyCosmos; P24717; 1 site, No reported glycans.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   OMA; ACDVVHY; -.
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; RIBONUCLEASE; 1.
DR   PANTHER; PTHR11437:SF24; RIBONUCLEASE PANCREATIC; 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.
DR   GO; GO:0005576; C:extracellular region; 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:0050830; P:defense response to Gram-positive bacterium; IEA:TreeGrafter.
DR   Proteomes; UP001108280; Unplaced.
DR   AlphaFoldDB; P24717; -.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          <1..6
FT   CHAIN           7..130
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000030918"
FT   ACT_SITE        18
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        125
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         13
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         16
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         47..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   DISULFID        32..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        46..101
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..116
FT                   /evidence="ECO:0000250"
FT   DISULFID        71..78
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   130 AA;  14517 MW;  8D227FD6491B413D CRC64;
     VQPSLGKESA AMKFERQHMD STVATSSSPT YCNQMMKRRN MTQGQCKPVN TFVHESLADV
     HAVCSQENVK CKNGKSNCYK SHSALHITDC RLKGNAKYPN CDYQTSQHQK HIIVACEGNP
     FVPVHFDATV
//