ID   RNAS1_NOTRU             Reviewed;         122 AA.
AC   B3EWJ0;
DT   13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2012, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Ribonuclease pancreatic {ECO:0000303|PubMed:658039};
DE            EC=4.6.1.18 {ECO:0000250|UniProtKB:P61823};
DE   AltName: Full=RNase 1 {ECO:0000250|UniProtKB:P61823};
DE   AltName: Full=RNase A {ECO:0000250|UniProtKB:P61823};
OS   Notamacropus rufogriseus (Red-necked wallaby) (Macropus rufogriseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Diprotodontia; Macropodidae; Notamacropus.
OX   NCBI_TaxID=1960652;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RC   TISSUE=Pancreas {ECO:0000269|PubMed:658039};
RX   PubMed=658039; DOI=10.1111/j.1432-1033.1978.tb12301.x;
RA   Gaastra W., Welling G.W., Beintema J.J.;
RT   "The amino-acid sequence of kangaroo pancreatic ribonuclease.";
RL   Eur. J. Biochem. 86:209-217(1978).
RN   [2] {ECO:0000305}
RP   UPDATE TO PROTEIN SEQUENCE.
RA   Beintema J.;
RL   Submitted (APR-2012) to UniProtKB.
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         Evidence={ECO:0000250|UniProtKB:P61823};
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         Evidence={ECO:0000250|UniProtKB:P61823};
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).
CC       {ECO:0000250|UniProtKB:P07998}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P61823}.
CC   -!- TISSUE SPECIFICITY: Pancreas. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000255}.
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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; Hydrolase; Lyase;
KW   Nuclease; Secreted.
FT   CHAIN           1..122
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000417916"
FT   ACT_SITE        11
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   ACT_SITE        117
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   BINDING         6
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   BINDING         9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   BINDING         40..44
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   BINDING         84
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   DISULFID        25..83
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   DISULFID        39..94
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   DISULFID        57..109
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
FT   DISULFID        64..71
FT                   /evidence="ECO:0000250|UniProtKB:P61823"
SQ   SEQUENCE   122 AA;  13807 MW;  2B52D03CC92E8F31 CRC64;
     ETAAEKFQRQ HMDTEHSTAS SSNYCNLMMK AREMTSDRCK PVNTFIHEPK SVVDAVCXQE
     NVTCKNGQTN CYKSNSRLSI TNCRQTGASX YPNCQYETSN LQKQIIVACE GQYVPVHFDA
     YV