ID   RNS1G_RAT               Reviewed;         152 AA.
AC   Q8VD89;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Ribonuclease pancreatic gamma-type;
DE            EC=4.6.1.18;
DE   AltName: Full=RNase 1 gamma;
DE   Flags: Precursor;
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 [GENOMIC DNA].
RX   PubMed=12399926; DOI=10.1007/s00239-002-2347-8;
RA   Dubois J.-Y.F., Jekel P.A., Mulder P.P.M.F.A., Bussink A.P.,
RA   Catzeflis F.M., Carsana A., Beintema J.J.;
RT   "Pancreatic-type ribonuclease 1 gene duplications in rat species.";
RL   J. Mol. Evol. 55:522-533(2002).
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AJ315460; CAC86441.1; -; Genomic_DNA.
DR   RefSeq; NP_001020287.1; NM_001025116.1.
DR   RefSeq; XP_006251937.1; XM_006251875.1.
DR   RefSeq; XP_008772017.1; XM_008773795.1.
DR   RefSeq; XP_017457997.1; XM_017602508.1.
DR   RefSeq; XP_017460460.1; XM_017604971.1.
DR   AlphaFoldDB; Q8VD89; -.
DR   SMR; Q8VD89; -.
DR   STRING; 10116.ENSRNOP00000049752; -.
DR   iPTMnet; Q8VD89; -.
DR   PhosphoSitePlus; Q8VD89; -.
DR   PaxDb; Q8VD89; -.
DR   Ensembl; ENSRNOT00000086427; ENSRNOP00000068653; ENSRNOG00000069584.
DR   GeneID; 305844; -.
DR   KEGG; rno:305844; -.
DR   UCSC; RGD:1565230; rat.
DR   CTD; 305844; -.
DR   RGD; 1565230; RGD1565230.
DR   VEuPathDB; HostDB:ENSRNOG00000063584; -.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   GeneTree; ENSGT00940000160869; -.
DR   HOGENOM; CLU_117006_0_0_1; -.
DR   InParanoid; Q8VD89; -.
DR   OMA; MRFQRQH; -.
DR   OrthoDB; 1549558at2759; -.
DR   PhylomeDB; Q8VD89; -.
DR   TreeFam; TF333393; -.
DR   PRO; PR:Q8VD89; -.
DR   Proteomes; UP000002494; Chromosome 15.
DR   Bgee; ENSRNOG00000054433; Expressed in pancreas and 6 other tissues.
DR   Genevisible; Q8VD89; RN.
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: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   3: Inferred from homology;
KW   Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000250"
FT   CHAIN           26..152
FT                   /note="Ribonuclease pancreatic gamma-type"
FT                   /id="PRO_0000234935"
FT   ACT_SITE        40
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         35
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        54..112
FT                   /evidence="ECO:0000250"
FT   DISULFID        68..123
FT                   /evidence="ECO:0000250"
FT   DISULFID        86..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        93..100
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  16935 MW;  7B8D6458E0E68DD3 CRC64;
     MGLEKSLFLF SLLVLVLGWV QPSLGVESRE TPAQKFERQH MDEEGPFPSS PTYCNEMMKS
     RGMTSGWCKS MNTFVHEPLA TVQAICSQGQ VTCKNGRNNC HKSSSTLRIT DCRLKGSSKY
     PNCDYTTTNS QKHIIIACEG NPLVPVHFDD SV