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