ID   RNAS1_MACMU             Reviewed;         152 AA.
AC   Q8SPN5;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 117.
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=RNS1;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11925567; DOI=10.1038/ng852;
RA   Zhang J., Zhang Y.-P., Rosenberg H.F.;
RT   "Adaptive evolution of a duplicated pancreatic ribonuclease gene in a leaf-
RT   eating monkey.";
RL   Nat. Genet. 30:411-415(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. 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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   EMBL; AF449632; AAL87053.1; -; Genomic_DNA.
DR   RefSeq; NP_001038203.1; NM_001044738.1.
DR   RefSeq; XP_014998586.1; XM_015143100.1.
DR   RefSeq; XP_014998587.1; XM_015143101.1.
DR   RefSeq; XP_014998588.1; XM_015143102.1.
DR   AlphaFoldDB; Q8SPN5; -.
DR   SMR; Q8SPN5; -.
DR   STRING; 9544.ENSMMUP00000033161; -.
DR   Ensembl; ENSMMUT00000024836; ENSMMUP00000023245; ENSMMUG00000017666.
DR   Ensembl; ENSMMUT00000086924; ENSMMUP00000062986; ENSMMUG00000017666.
DR   GeneID; 704676; -.
DR   KEGG; mcc:704676; -.
DR   CTD; 6035; -.
DR   VEuPathDB; HostDB:ENSMMUG00000017666; -.
DR   VGNC; VGNC:76700; RNASE1.
DR   eggNOG; ENOG502SQ4K; Eukaryota.
DR   GeneTree; ENSGT00940000160869; -.
DR   HOGENOM; CLU_117006_0_0_1; -.
DR   InParanoid; Q8SPN5; -.
DR   OMA; SNSTYCN; -.
DR   OrthoDB; 1549558at2759; -.
DR   TreeFam; TF333393; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000017666; Expressed in lung and 21 other tissues.
DR   ExpressionAtlas; Q8SPN5; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IBA:GO_Central.
DR   GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GO_Central.
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; Glycoprotein; Hydrolase; Lyase; Nuclease;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..152
FT                   /note="Ribonuclease pancreatic"
FT                   /id="PRO_0000030926"
FT   ACT_SITE        36
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        143
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         65..69
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        50..108
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        82..134
FT                   /evidence="ECO:0000250"
FT   DISULFID        89..96
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   152 AA;  17030 MW;  0B7A5B6F35404FE4 CRC64;
     MALDKSVILL PLLVLVLLVL GCLGRESRAK KFQRQHMDSG SSPSSNSTYC NQMMKRRSMT
     HGRCKPVNTF VHEPLVDVQN VCFQEKVTCK NGQTNCFKSK SSMHITDCRL TNGSRYPNCA
     YRTSPKERHI IVACEGSPHV PVHFDASVED ST