ID   RNAS1_IGUIG             Reviewed;         119 AA.
AC   P80287;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   02-SEP-2026, entry version 92.
DE   RecName: Full=Ribonuclease pancreatic;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1;
DE   AltName: Full=RNase A;
OS   Iguana iguana (Common iguana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Iguanidae; Iguaninae; Iguana.
OX   NCBI_TaxID=8517;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Pancreas;
RX   PubMed=8307028; DOI=10.1111/j.1432-1033.1994.tb19979.x;
RA   Zhao W., Beintema J.J., Hofsteenge J.;
RT   "The amino acid sequence of iguana (Iguana iguana) pancreatic
RT   ribonuclease.";
RL   Eur. J. Biochem. 219:641-646(1994).
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; S41111; S41111.
DR   AlphaFoldDB; P80287; -.
DR   SMR; P80287; -.
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   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:SF10; ANGIOGENIN-RELATED; 1.
DR   PANTHER; PTHR11437; RIBONUCLEASE; 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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease; Pyrrolidone carboxylic acid; Secreted.
FT   CHAIN           1..119
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000057203"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        113
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         40..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:8307028"
FT   DISULFID        25..80
FT                   /evidence="ECO:0000250"
FT   DISULFID        39..91
FT                   /evidence="ECO:0000250"
FT   DISULFID        57..106
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   119 AA;  13324 MW;  6072FB5B7B15BD5A CRC64;
     QDWSSFQNKH IDYPETSASN PNAYCDLMMQ RRNLNPTKCK TRNTFVHASP SEIQQVCGSG
     GTHYEDNLYD SNESFDLTDC KNVGGTAPSS CKYNGTPGTK RIRIACENNQ PVHFELVLS
//