RNS1G_RATFU
ID RNS1G_RATFU Reviewed; 152 AA.
AC Q8VD90;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Ribonuclease pancreatic gamma-type;
DE EC=4.6.1.18;
DE AltName: Full=RNase 1 gamma;
DE Flags: Precursor;
OS Rattus fuscipes (Bush rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10119;
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; AJ315457; CAC86438.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8VD90; -.
DR SMR; Q8VD90; -.
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 3: Inferred from homology;
KW Disulfide bond; Endonuclease; Hydrolase; Lyase; Nuclease; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..152
FT /note="Ribonuclease pancreatic gamma-type"
FT /id="PRO_0000234939"
FT REGION 26..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 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; 16950 MW; F5486274BE56EFD3 CRC64;
MGLEKSFILF SLLVLVLGCV QPSLVGESKE SPSEKFKRRH MDEEGPYQSS PTYCNQMMKD
RGMTSGRCKP LNTFVHESWA KVKAICSQDK VTCKNGKSNC HKSISTLNIT DCLLMGSSKY
PKCDYSTTAR QKHSIIACDG NPYVPVHYDA TV
