ID   RNS1B_CAVPO             Reviewed;         128 AA.
AC   P00679;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Ribonuclease pancreatic B;
DE            Short=RNase IB;
DE            EC=4.6.1.18;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-21 AND ASN-34.
RC   TISSUE=Pancreas;
RX   PubMed=862624; DOI=10.1111/j.1432-1033.1977.tb11507.x;
RA   van den Berg A., van den Hende-Timmer L., Hofsteenge J., Gaastra W.,
RA   Beintema J.J.;
RT   "Guinea-pig pancreatic ribonucleases. Isolation, properties, primary
RT   structure and glycosidation.";
RL   Eur. J. Biochem. 75:91-100(1977).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Pancreas.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   PIR; A00826; NRGPB.
DR   AlphaFoldDB; P00679; -.
DR   SMR; P00679; -.
DR   STRING; 10141.ENSCPOP00000019991; -.
DR   iPTMnet; P00679; -.
DR   PRIDE; P00679; -.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   HOGENOM; CLU_117006_0_0_1; -.
DR   InParanoid; P00679; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
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..128
FT                   /note="Ribonuclease pancreatic B"
FT                   /id="PRO_0000057189"
FT   REGION          1..21
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                   /evidence="ECO:0000269|PubMed:862624"
FT   CARBOHYD        34
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:862624"
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   VARIANT         64
FT                   /note="L -> P"
SQ   SEQUENCE   128 AA;  14406 MW;  A2F4101A1A33E93B CRC64;
     AESSAMKFQR QHMDPEGSPS NSSNYCNVMM IRRNMTQGRC KPVNTFVHES LADVQAVCFQ
     KNVLCKNGQT NCYQSYSRMR ITDCRVTSSS KFPNCSYRMS QAQKSIIVAC EGDPYVPVHF
     DASVEPST