ID   RNAS1_SHEEP             Reviewed;         124 AA.
AC   P67927; P00661; P04420;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 68.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=4356260; DOI=10.1016/s0021-9258(19)43264-x;
RA   Kobayashi R., Hirs C.H.W.;
RT   "The amino acid sequence of ovine pancreatic ribonuclease A.";
RL   J. Biol. Chem. 248:7833-7837(1973).
RN   [2]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas;
RX   PubMed=4855010; DOI=10.1016/0014-5793(74)80953-1;
RA   Welling G.W., Scheffer A.J., Beintema J.J.;
RT   "The primary structure of goat and sheep pancreatic ribonucleases.";
RL   FEBS Lett. 41:58-61(1974).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8587129; DOI=10.1007/bf00173164;
RA   Confalone E., Beintema J.J., Sasso M.P., Carsana A., Palmieri M.,
RA   Vento M.T., Furia A.;
RT   "Molecular evolution of genes encoding ribonucleases in ruminant species.";
RL   J. Mol. Evol. 41:850-858(1995).
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; S81741; AAB36135.1; -; Genomic_DNA.
DR   PIR; A91406; NRSH.
DR   AlphaFoldDB; P67927; -.
DR   SMR; P67927; -.
DR   STRING; 9940.ENSOARP00000013570; -.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   BRENDA; 4.6.1.18; 2668.
DR   Proteomes; UP000002356; 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; Glycoprotein;
KW   Hydrolase; Lyase; Nuclease; Reference proteome; Secreted.
FT   CHAIN           1..124
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000057214"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT   ACT_SITE        119
FT                   /note="Proton donor"
FT   BINDING         7
FT                   /ligand="substrate"
FT   BINDING         10
FT                   /ligand="substrate"
FT   BINDING         41..45
FT                   /ligand="substrate"
FT   BINDING         66
FT                   /ligand="substrate"
FT   BINDING         85
FT                   /ligand="substrate"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine; partial"
FT   DISULFID        26..84
FT   DISULFID        40..95
FT   DISULFID        58..110
FT   DISULFID        65..72
FT   CONFLICT        49
FT                   /note="E -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        103
FT                   /note="E -> Q (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   124 AA;  13707 MW;  3570EC14528EDDFA CRC64;
     KESAAAKFER QHMDSSTSSA SSSNYCNQMM KSRNLTQDRC KPVNTFVHES LADVQAVCSQ
     KNVACKNGQT NCYQSYSTMS ITDCRETGSS KYPNCAYKTT QAEKHIIVAC EGNPYVPVHF
     DASV