RNAS1_SPAEH
ID RNAS1_SPAEH Reviewed; 125 AA.
AC P16414;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Spalax ehrenbergi (Middle East blind mole rat) (Nannospalax ehrenbergi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Spalacidae; Spalacinae; Nannospalax.
OX NCBI_TaxID=30637;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-35.
RC TISSUE=Pancreas;
RX PubMed=2673297; DOI=10.1515/bchm3.1989.370.1.583;
RA Schueller C., Neuteboom B., Wuebbels G., Beintema J.J., Nevo E.;
RT "The amino-acid sequence of pancreatic ribonuclease from the mole rat
RT Spalax ehrenbergi, chromosomal species 2n = 60.";
RL Biol. Chem. Hoppe-Seyler 370:583-589(1989).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; S04503; S04503.
DR AlphaFoldDB; P16414; -.
DR SMR; P16414; -.
DR iPTMnet; P16414; -.
DR PRIDE; P16414; -.
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; Secreted.
FT CHAIN 1..125
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000057215"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 120
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 42..46
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:2673297"
FT DISULFID 27..85
FT /evidence="ECO:0000250"
FT DISULFID 41..96
FT /evidence="ECO:0000250"
FT DISULFID 59..111
FT /evidence="ECO:0000250"
FT DISULFID 66..73
FT /evidence="ECO:0000250"
SQ SEQUENCE 125 AA; 14031 MW; 9D07C4F74261E7E4 CRC64;
KESSAEKFLR QHVDSIDSPG NLSPTYCNQM MLRRNMTKGS CKPVNTFVHE PLKDIKAVCF
QENVTCKNGN SNCYKSHASL HITDCRTISS SKYPDCAYKT SQEQKHIIVA CEGDPFVPVH
YDASV
