RNAS1_MESAU
ID RNAS1_MESAU Reviewed; 124 AA.
AC P00682;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-34.
RC TISSUE=Pancreas;
RX PubMed=518928; DOI=10.1016/s0300-9084(79)80277-1;
RA Jekel P.A., Sips H.J., Lenstra J.A., Beintema J.J.;
RT "The amino acid sequence of hamster pancreatic ribonuclease.";
RL Biochimie 61:827-839(1979).
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; A00829; NRHY.
DR AlphaFoldDB; P00682; -.
DR SMR; P00682; -.
DR STRING; 10036.XP_005087526.1; -.
DR iPTMnet; P00682; -.
DR PRIDE; P00682; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR Proteomes; UP000189706; 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_0000057205"
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 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:518928"
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"
SQ SEQUENCE 124 AA; 13867 MW; 4E3C57F94E73C478 CRC64;
KESAAMKFER QHMDSTVATS SSPTYCNQMM KRRNMTQGYC KPVNTFVHES LADVHAVCSQ
ENVACKNGKS NCYKSHSALH ITDCRLKGNA KYPNCDYQTS QLQKQIIVAC EGNPFVPVHF
DASV
