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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
 
 
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