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RNASL_LITCT
ID   RNASL_LITCT             Reviewed;         111 AA.
AC   P14626;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Ribonuclease, liver;
DE            EC=4.6.1.18;
OS   Lithobates catesbeianus (American bullfrog) (Rana catesbeiana).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8400;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Liver;
RX   PubMed=2613682; DOI=10.1093/oxfordjournals.jbchem.a122924;
RA   Nitta R., Katayama N., Okabe Y., Iwama M., Watanabe H., Abe Y., Okazaki T.,
RA   Ohgi K., Irie M.;
RT   "Primary structure of a ribonuclease from bullfrog (Rana catesbeiana)
RT   liver.";
RL   J. Biochem. 106:729-735(1989).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
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DR   PIR; JX0085; JX0085.
DR   AlphaFoldDB; P14626; -.
DR   SMR; P14626; -.
DR   BRENDA; 4.6.1.18; 5278.
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   SMART; SM00092; RNAse_Pc; 1.
DR   SUPFAM; SSF54076; SSF54076; 1.
DR   PROSITE; PS00127; RNASE_PANCREATIC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Endonuclease; Hydrolase; Lyase;
KW   Nuclease; Pyrrolidone carboxylic acid; Secreted.
FT   CHAIN           1..111
FT                   /note="Ribonuclease, liver"
FT                   /id="PRO_0000057172"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        104
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         5
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:2613682"
FT   DISULFID        19..72
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        52..97
FT                   /evidence="ECO:0000250"
FT   DISULFID        94..111
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   111 AA;  12461 MW;  D64BA72456C10788 CRC64;
     QNWAKFKEKH IRSTSSIDCN TIMDKAIYIV GGKCKERNTF IISSEDNVKA ICSGVSPDRK
     ELSTTSFKLN TCIRDSITPR PCPYHPSPDN NKICVKCEKQ LPVHFVGIGK C
 
 
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