ID   RNAS1_GLIGL             Reviewed;         156 AA.
AC   Q9WUS1;
DT   21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 85.
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   Glis glis (Fat dormouse) (Myoxus glis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Gliridae;
OC   Glirinae; Glis.
OX   NCBI_TaxID=41261;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10508551; DOI=10.1006/mpev.1999.0674;
RA   Dubois J.-Y.F., Catzeflis F.M., Beintema J.J.;
RT   "The phylogenetic position of 'Acomyinae' (Rodentia, Mammalia) as sister
RT   group of a Murinae + Gerbillinae clade: evidence from the nuclear
RT   ribonuclease gene.";
RL   Mol. Phylogenet. Evol. 13:181-192(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ005767; CAB41478.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9WUS1; -.
DR   SMR; Q9WUS1; -.
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   2: Evidence at transcript level;
KW   Disulfide bond; Endonuclease; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..156
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000030932"
FT   ACT_SITE        38
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         33
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36
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        90
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;  17353 MW;  58B0D7793EAC082E CRC64;
     MGLEKSLVFF PLLVLLALGW VQPCLGRESS AHKFRRQHMD SEGLSSSSSS PTYCNQMMQR
     RKLTRGHCKP VNTFVHEPLA DVQAVCFQEN VTCKNGQTNC YRSGSSMHVT DCRTTGSSKY
     PNCAYRTTQK VKRIVVACEG DPSVPVHYDG SVEDST