ID   RNAS1_CHESE             Reviewed;         119 AA.
AC   P04061;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Ribonuclease;
DE            EC=4.6.1.18;
OS   Chelydra serpentina (Snapping turtle) (Testudo serpentina).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC   Americhelydia; Chelydroidea; Chelydridae; Chelydra.
OX   NCBI_TaxID=8475;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=4076178; DOI=10.1111/j.1432-1033.1985.tb09301.x;
RA   Beintema J.J., Broos J., Meulenberg J., Schueller C.;
RT   "The amino acid sequence of snapping turtle (Chelydra serpentina)
RT   ribonuclease.";
RL   Eur. J. Biochem. 153:305-312(1985).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-30.
RX   PubMed=4564316; DOI=10.1038/240395a0;
RA   Barnard E.A., Cohen M.S., Gold M.H., Kim J.K.;
RT   "Evolution of ribonuclease in relation to polypeptide folding mechanisms.";
RL   Nature 240:395-398(1972).
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   PIR; A91155; NRST.
DR   AlphaFoldDB; P04061; -.
DR   SMR; P04061; -.
DR   Proteomes; UP000694403; Unplaced.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease; Reference proteome; Secreted.
FT   CHAIN           1..119
FT                   /note="Ribonuclease"
FT                   /id="PRO_0000057175"
FT   ACT_SITE        11
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        114
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        26..81
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..92
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..107
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   119 AA;  12915 MW;  77078988B4423123 CRC64;
     ETRYEKFLRQ HVDYPKSSAP DSRTYCNQMM QRRGMTSPVC KFTNTFVHAS AASITTVCGS
     GGTPASGDLR DSNASFALTT CRLQGGSQTP NCPYNADAST QRIRIACVGG LPVHYDKSI