RNAS1_ODOVI
ID RNAS1_ODOVI Reviewed; 30 AA.
AC P19640;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Ribonuclease pancreatic;
DE EC=4.6.1.18;
DE AltName: Full=RNase 1;
DE AltName: Full=RNase A;
DE Flags: Fragment;
GN Name=RNASE1; Synonyms=RNS1;
OS Odocoileus virginianus virginianus (Virginia white-tailed deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Odocoileinae; Odocoileus.
OX NCBI_TaxID=9875;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Pancreas;
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; A05004; A05004.
DR BMRB; P19640; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0004522; F:ribonuclease A activity; IEA:UniProtKB-EC.
DR Gene3D; 3.10.130.10; -; 1.
DR InterPro; IPR036816; RNaseA-like_dom_sf.
DR SUPFAM; SSF54076; SSF54076; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endonuclease; Hydrolase; Lyase; Nuclease;
KW Secreted.
FT CHAIN 1..>30
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000057207"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 10
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VARIANT 3
FT /note="T -> S"
FT NON_TER 30
SQ SEQUENCE 30 AA; 3376 MW; 9184E7C816394D20 CRC64;
KETAAAKFER QHMDPAPAAA XXQNYCNQMM