ID   RNAS1_PIG               Reviewed;         124 AA.
AC   P00671;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 106.
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   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=5460946; DOI=10.1016/s0021-9258(18)63378-2;
RA   Jackson R.L., Hirs C.H.W.;
RT   "The primary structure of porcine pancreatic ribonuclease. II. The amino
RT   acid sequence of the reduced S-aminoethylated protein.";
RL   J. Biol. Chem. 245:637-653(1970).
RN   [2]
RP   SEQUENCE REVISION TO 2.
RX   PubMed=11947109; DOI=10.1016/0014-5793(73)80098-5;
RA   Wierenga R.K., Huizinga J.D., Gaastra W., Welling G.W., Beintema J.J.;
RT   "Affinity chromatography of porcine pancreatic ribonuclease and
RT   reinvestigation of the N-terminal amino acid sequence.";
RL   FEBS Lett. 31:181-185(1973).
RN   [3]
RP   DISULFIDE BONDS.
RX   PubMed=4904878; DOI=10.1016/s0021-9258(18)63379-4;
RA   Phelan J.J., Hirs C.H.W.;
RT   "The primary structure of porcine pancreatic ribonuclease. 3. The disulfide
RT   bonds.";
RL   J. Biol. Chem. 245:654-661(1970).
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; A92071; NRPG.
DR   AlphaFoldDB; P00671; -.
DR   SMR; P00671; -.
DR   IntAct; P00671; 1.
DR   STRING; 9823.ENSSSCP00000023197; -.
DR   PRIDE; P00671; -.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   InParanoid; P00671; -.
DR   BRENDA; 4.6.1.18; 6170.
DR   SABIO-RK; P00671; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; 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   GO; GO:0004540; F:ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
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_0000057210"
FT   REGION          1..24
FT                   /note="Disordered"
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        21
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   CARBOHYD        76
FT                   /note="N-linked (GlcNAc...) asparagine"
FT   DISULFID        26..84
FT                   /evidence="ECO:0000269|PubMed:4904878"
FT   DISULFID        40..95
FT                   /evidence="ECO:0000269|PubMed:4904878"
FT   DISULFID        58..110
FT                   /evidence="ECO:0000269|PubMed:4904878"
FT   DISULFID        65..72
FT                   /evidence="ECO:0000269|PubMed:4904878"
SQ   SEQUENCE   124 AA;  13804 MW;  0AC28CDE14111845 CRC64;
     KESPAKKFQR QHMDPDSSSS NSSNYCNLMM SRRNMTQGRC KPVNTFVHES LADVQAVCSQ
     INVNCKNGQT NCYQSNSTMH ITDCRQTGSS KYPNCAYKAS QEQKHIIVAC EGNPPVPVHF
     DASV