RNS1B_RAT
ID RNS1B_RAT Reviewed; 152 AA.
AC P00684;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Ribonuclease pancreatic beta-type;
DE EC=4.6.1.18;
DE AltName: Full=RL1;
DE AltName: Full=RNase 1 gamma;
DE AltName: Full=RNase A;
DE Flags: Precursor;
GN Name=Rnase1; Synonyms=Rib-1, Rib1, Rns1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7174650; DOI=10.1016/s0021-9258(18)33312-x;
RA McDonald R.J., Stary S.J., Swift G.H.;
RT "Rat pancreatic ribonuclease messenger RNA. The nucleotide sequence of the
RT entire mRNA and the derived amino acid sequence of the pre-enzyme.";
RL J. Biol. Chem. 257:14582-14585(1982).
RN [2]
RP PROTEIN SEQUENCE OF 26-152.
RC TISSUE=Pancreas;
RX PubMed=4710592; DOI=10.1016/0005-2795(73)90020-2;
RA Beintema J.J., Gruber M.;
RT "Rat pancreatic ribonuclease. II. Amino acid sequence.";
RL Biochim. Biophys. Acta 310:161-173(1973).
RN [3]
RP SEQUENCE REVISION TO 98; 124; 126; 129 AND 131.
RC TISSUE=Pancreas;
RX PubMed=6873294; DOI=10.1016/0014-5793(83)80444-x;
RA Beintema J.J.;
RT "Rat pancreatic ribonuclease: agreement between the corrected amino acid
RT sequence and the sequence derived from its messenger RNA.";
RL FEBS Lett. 159:191-195(1983).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 30-152.
RC TISSUE=Pancreas;
RX PubMed=10090281;
RX DOI=10.1002/(sici)1097-0134(19990401)35:1<1::aid-prot1>3.0.co;2-2;
RA Gupta V., Muyldermans S., Wyns L., Salunke D.M.;
RT "The crystal structure of recombinant rat pancreatic RNase A.";
RL Proteins 35:1-12(1999).
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. {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 EMBL; J00771; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; A92356; NRRT.
DR RefSeq; XP_008768852.1; XM_008770630.1.
DR PDB; 1RRA; X-ray; 2.50 A; A=30-152.
DR PDBsum; 1RRA; -.
DR AlphaFoldDB; P00684; -.
DR SMR; P00684; -.
DR STRING; 10116.ENSRNOP00000043700; -.
DR PaxDb; P00684; -.
DR Ensembl; ENSRNOT00000082938; ENSRNOP00000072263; ENSRNOG00000063584.
DR GeneID; 364304; -.
DR UCSC; RGD:3574; rat.
DR CTD; 6035; -.
DR RGD; 3574; Rnase1.
DR VEuPathDB; HostDB:ENSRNOG00000069584; -.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR GeneTree; ENSGT00940000160869; -.
DR HOGENOM; CLU_117006_0_0_1; -.
DR InParanoid; P00684; -.
DR OMA; SNSTYCN; -.
DR OrthoDB; 1549558at2759; -.
DR PhylomeDB; P00684; -.
DR BRENDA; 4.6.1.18; 5301.
DR EvolutionaryTrace; P00684; -.
DR PRO; PR:P00684; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000053633; Expressed in pancreas and 12 other tissues.
DR Genevisible; P00684; RN.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
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 GO; GO:0004540; F:ribonuclease activity; ISO:RGD.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; ISO:RGD.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Lyase; Nuclease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:4710592"
FT CHAIN 26..152
FT /note="Ribonuclease pancreatic beta-type"
FT /id="PRO_0000030940"
FT REGION 25..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 40
FT /note="Proton acceptor"
FT ACT_SITE 147
FT /note="Proton donor"
FT BINDING 35
FT /ligand="substrate"
FT BINDING 38
FT /ligand="substrate"
FT BINDING 69..73
FT /ligand="substrate"
FT BINDING 94
FT /ligand="substrate"
FT BINDING 113
FT /ligand="substrate"
FT DISULFID 54..112
FT DISULFID 68..123
FT DISULFID 86..138
FT DISULFID 93..100
FT HELIX 34..40
FT /evidence="ECO:0007829|PDB:1RRA"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1RRA"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:1RRA"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1RRA"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:1RRA"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1RRA"
FT STRAND 144..151
FT /evidence="ECO:0007829|PDB:1RRA"
SQ SEQUENCE 152 AA; 16823 MW; 86A53CCD7F8FCBEF CRC64;
MGLEKSLFLF SLLVLVLGWV QPSLGGESRE SSADKFKRQH MDTEGPSKSS PTYCNQMMKR
QGMTKGSCKP VNTFVHEPLE DVQAICSQGQ VTCKNGRNNC HKSSSTLRIT DCRLKGSSKY
PNCDYTTTDS QKHIIIACDG NPYVPVHFDA SV
