RNS1D_RAT
ID RNS1D_RAT Reviewed; 150 AA.
AC Q8VD88;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Ribonuclease pancreatic delta-type;
DE EC=4.6.1.18;
DE AltName: Full=RNase 1 delta;
DE Flags: Precursor;
GN Name=Rnase1d; Synonyms=Rnase1;
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; AJ315462; CAC86443.1; -; Genomic_DNA.
DR RefSeq; NP_001013250.1; NM_001013232.1.
DR AlphaFoldDB; Q8VD88; -.
DR SMR; Q8VD88; -.
DR STRING; 10116.ENSRNOP00000035095; -.
DR iPTMnet; Q8VD88; -.
DR PhosphoSitePlus; Q8VD88; -.
DR PaxDb; Q8VD88; -.
DR GeneID; 364303; -.
DR KEGG; rno:364303; -.
DR UCSC; RGD:1310106; rat.
DR CTD; 364303; -.
DR RGD; 1310106; Rnase1.
DR eggNOG; ENOG502SQ4K; Eukaryota.
DR InParanoid; Q8VD88; -.
DR PhylomeDB; Q8VD88; -.
DR PRO; PR:Q8VD88; -.
DR Proteomes; UP000002494; Unplaced.
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:0009617; P:response to bacterium; ISO:RGD.
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; Hydrolase; Lyase; Nuclease;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..150
FT /note="Ribonuclease pancreatic delta-type"
FT /id="PRO_0000234934"
FT ACT_SITE 37
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton donor"
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 BINDING 111
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 51..110
FT /evidence="ECO:0000250"
FT DISULFID 65..121
FT /evidence="ECO:0000250"
FT DISULFID 83..136
FT /evidence="ECO:0000250"
FT DISULFID 90..98
FT /evidence="ECO:0000250"
SQ SEQUENCE 150 AA; 16936 MW; EBE4938DFEF929E6 CRC64;
MGLEKSFILF SLLVLVLGWV QPSLGRKPSV QDFKRQHMDP DSPPNSRPTY CNQMMKRRGM
TKGSCKRVNT FLHESWATVK AICSQRQMTC KTSSRNNCHK SSSTLHITDC RLKGSSKYPN
CDYTTTNSQK HIIIACEGNP LVPVHFDASV
