ID   RNAS1_MOUSE             Reviewed;         149 AA.
AC   P00683;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 2.
DT   08-NOV-2023, entry version 159.
DE   RecName: Full=Ribonuclease pancreatic;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1;
DE   AltName: Full=RNase A;
DE   Flags: Precursor;
GN   Name=Rnase1; Synonyms=Rib-1, Rib1, Rns1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2299980; DOI=10.1093/oxfordjournals.molbev.a040585;
RA   Schueller C., Nijssen H.M.J., Kok R., Beintema J.J.;
RT   "Evolution of nucleic acids coding for ribonucleases: the mRNA sequence of
RT   mouse pancreatic ribonuclease.";
RL   Mol. Biol. Evol. 7:29-44(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C3H/HeJ; TISSUE=Spleen;
RX   PubMed=1840677; DOI=10.1093/nar/19.24.6935;
RA   Samuelson L.C., Wiebauer K., Howard G., Schmid R.M., Koeplin D.,
RA   Meisler M.H.;
RT   "Isolation of the murine ribonuclease gene Rib-1: structure and tissue
RT   specific expression in pancreas and parotid gland.";
RL   Nucleic Acids Res. 19:6935-6941(1991).
RN   [3]
RP   PROTEIN SEQUENCE OF 26-149.
RC   TISSUE=Pancreas;
RX   PubMed=556267; DOI=10.1111/j.1432-1033.1979.tb13199.x;
RA   Lenstra J.A., Beintema J.J.;
RT   "The amino acid sequence of mouse pancreatic ribonuclease. Extremely rapid
RT   evolutionary rates of the myomorph rodent ribonucleases.";
RL   Eur. J. Biochem. 98:399-408(1979).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   EMBL; M27814; AAA40060.1; -; mRNA.
DR   EMBL; X60103; CAA42697.1; -; Genomic_DNA.
DR   CCDS; CCDS27038.1; -.
DR   PIR; A34090; NRMS.
DR   PDB; 3TSR; X-ray; 2.20 A; A/B/C/D=26-149.
DR   PDBsum; 3TSR; -.
DR   AlphaFoldDB; P00683; -.
DR   SMR; P00683; -.
DR   STRING; 10090.ENSMUSP00000079025; -.
DR   PhosphoSitePlus; P00683; -.
DR   MaxQB; P00683; -.
DR   PaxDb; 10090-ENSMUSP00000079025; -.
DR   PeptideAtlas; P00683; -.
DR   ProteomicsDB; 300453; -.
DR   AGR; MGI:97919; -.
DR   MGI; MGI:97919; Rnase1.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   InParanoid; P00683; -.
DR   PhylomeDB; P00683; -.
DR   ChiTaRS; Rnase1; mouse.
DR   PRO; PR:P00683; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; P00683; Protein.
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   GO; GO:0004540; F:RNA nuclease activity; ISO:MGI.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0009617; P:response to bacterium; IEP:MGI.
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.
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:556267"
FT   CHAIN           26..149
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000030929"
FT   ACT_SITE        37
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        144
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         66..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        51..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        65..120
FT                   /evidence="ECO:0000250"
FT   DISULFID        83..135
FT                   /evidence="ECO:0000250"
FT   DISULFID        90..97
FT                   /evidence="ECO:0000250"
FT   HELIX           29..37
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           50..57
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          67..72
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           76..80
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   HELIX           81..84
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          122..136
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   TURN            137..140
FT                   /evidence="ECO:0007829|PDB:3TSR"
FT   STRAND          141..149
FT                   /evidence="ECO:0007829|PDB:3TSR"
SQ   SEQUENCE   149 AA;  16820 MW;  2FC1E0A50D245162 CRC64;
     MGLEKSLILF PLFFLLLGWV QPSLGRESAA QKFQRQHMDP DGSSINSPTY CNQMMKRRDM
     TNGSCKPVNT FVHEPLADVQ AVCSQENVTC KNRKSNCYKS SSALHITDCH LKGNSKYPNC
     DYKTTQYQKH IIVACEGNPY VPVHFDATV
//