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   24-JAN-2024, entry version 167.
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}.
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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.ENSRNOP00000068653; -.
DR   PhosphoSitePlus; P00684; -.
DR   PaxDb; 10116-ENSRNOP00000043700; -.
DR   Ensembl; ENSRNOT00000082938.2; ENSRNOP00000072263.2; ENSRNOG00000063584.1.
DR   Ensembl; ENSRNOT00055042658; ENSRNOP00055034831; ENSRNOG00055024757.
DR   Ensembl; ENSRNOT00060046940; ENSRNOP00060039035; ENSRNOG00060027078.
DR   Ensembl; ENSRNOT00065001308; ENSRNOP00065000928; ENSRNOG00065000987.
DR   Ensembl; ENSRNOT00065055752; ENSRNOP00065045918; ENSRNOG00065032392.
DR   UCSC; RGD:3574; rat.
DR   AGR; RGD:3574; -.
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; CEGDPYV; -.
DR   OrthoDB; 4596772at2759; -.
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 cell types or tissues.
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:RNA nuclease activity; ISO:RGD.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR   CDD; cd06265; RNase_A_canonical; 1.
DR   Gene3D; 3.10.130.10; Ribonuclease A-like domain; 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; RIBONUCLEASE; 1.
DR   PANTHER; PTHR11437:SF24; RIBONUCLEASE PANCREATIC; 1.
DR   Pfam; PF00074; RnaseA; 1.
DR   PRINTS; PR00794; RIBONUCLEASE.
DR   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; RNase A-like; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
DR   Genevisible; P00684; RN.
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
//