RNAS1_PERLE
ID RNAS1_PERLE Reviewed; 148 AA.
AC Q9WUV5;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 83.
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;
OS Peromyscus leucopus (White-footed mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Peromyscus.
OX NCBI_TaxID=10041;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10508551; DOI=10.1006/mpev.1999.0674;
RA Dubois J.-Y.F., Catzeflis F.M., Beintema J.J.;
RT "The phylogenetic position of 'Acomyinae' (Rodentia, Mammalia) as sister
RT group of a Murinae + Gerbillinae clade: evidence from the nuclear
RT ribonuclease gene.";
RL Mol. Phylogenet. Evol. 13:181-192(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. 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}.
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DR EMBL; AJ005770; CAB41483.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9WUV5; -.
DR SMR; Q9WUV5; -.
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 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 2: Evidence at transcript level;
KW Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..148
FT /note="Ribonuclease pancreatic"
FT /id="PRO_0000030936"
FT ACT_SITE 143
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 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 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 148 AA; 16490 MW; D42DDFA51183BD2D CRC64;
MGLEKSLILF PLLVLVVGWV QPSLGKETSA MKFERHDVDS DSSSSSPTYC NQMMKRREMT
KGSCKPVNTF VHESLQDIHA VCSQKNVKCK NGQTNCYKSR SALRITDCRL TGSSKYPNCE
YKTSQQQKHI IVACEGNPSV PVHFDASA
