ID   RNAS1_BISBI             Reviewed;         124 AA.
AC   P61824; P00656; Q9TSF2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   02-SEP-2026, entry version 91.
DE   RecName: Full=Ribonuclease pancreatic;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1;
DE   AltName: Full=RNase A;
GN   Name=RNASE1; Synonyms=RNS1;
OS   Bison bison (American bison) (Bos bison).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bison.
OX   NCBI_TaxID=9901;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=955781; DOI=10.1111/j.1399-3011.1976.tb02513.x;
RA   Muskiet F.A.J., Welling G.W., Beintema J.J.;
RT   "Studies on the primary structure of bison pancreatic ribonuclease.";
RL   Int. J. Pept. Protein Res. 8:345-348(1976).
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   PDB; 6QMN; X-ray; 2.31 A; A/B/C=1-124.
DR   PDB; 9EO5; X-ray; 1.99 A; AAA/BBB=1-124.
DR   PDB; 9EO8; X-ray; 1.76 A; AAA/BBB=1-124.
DR   AlphaFoldDB; P61824; -.
DR   BMRB; P61824; -.
DR   SMR; P61824; -.
DR   GlyCosmos; P61824; 1 site, No reported glycans.
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   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   PDBsum; 6QMN; -.
DR   PDBsum; 9EO5; -.
DR   PDBsum; 9EO8; -.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW   Glycoprotein; Hydrolase; Lyase; Nuclease; Secreted.
FT   CHAIN           1..124
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000057181"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..13
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         7
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         10
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..45
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        40..95
FT                   /evidence="ECO:0000250"
FT   DISULFID        58..110
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..72
FT                   /evidence="ECO:0000250"
FT   HELIX           4..12
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   HELIX           25..32
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          35..39
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          42..47
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   HELIX           51..55
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          60..63
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          79..86
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          97..104
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          106..111
FT                   /evidence="ECO:0007829|PDB:6QMN"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:6QMN"
SQ   SEQUENCE   124 AA;  13690 MW;  C09FFCC4FFE3065C CRC64;
     KETAAAKFER QHMDSSTSAA SSSNYCNQMM KSRNLTKDRC KPVNTFVHES LADVQAVCSQ
     KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QANKHIIVAC EGNPYVPVHF
     DASV
//