RNASO_LITCT
ID RNASO_LITCT Reviewed; 133 AA.
AC P11916; Q9PWR7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 4.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Oocytes ribonuclease;
DE EC=3.1.27.-;
DE AltName: Full=RC-RNase;
DE AltName: Full=Sialic acid-binding lectin;
DE Short=SBL-C;
DE Flags: Precursor;
GN Name=RCR;
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9497370; DOI=10.1074/jbc.273.11.6395;
RA Huang H.C., Wang S.C., Leu Y.J., Lu S.C., Liao Y.D.;
RT "The Rana catesbeiana rcr gene encoding a cytotoxic ribonuclease. Tissue
RT distribution, cloning, purification, cytotoxicity, and active residues for
RT RNase activity.";
RL J. Biol. Chem. 273:6395-6401(1998).
RN [2]
RP PROTEIN SEQUENCE OF 23-133, AND PYROGLUTAMATE FORMATION AT GLN-23.
RC TISSUE=Egg;
RX PubMed=3304421; DOI=10.1021/bi00382a018;
RA Titani K., Takio K., Kuwada M., Nitta K., Sakakibara F., Kawauchi H.,
RA Takayanagi G., Hakomori S.;
RT "Amino acid sequence of sialic acid binding lectin from frog (Rana
RT catesbeiana) eggs.";
RL Biochemistry 26:2189-2194(1987).
RN [3]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 81-101.
RX PubMed=1373237; DOI=10.1093/nar/20.6.1371;
RA Liao Y.-D.;
RT "A pyrimidine-guanine sequence-specific ribonuclease from Rana catesbeiana
RT (bullfrog) oocytes.";
RL Nucleic Acids Res. 20:1371-1377(1992).
RN [4]
RP CHARACTERIZATION.
RC TISSUE=Egg;
RX PubMed=8448385; DOI=10.1093/glycob/3.1.37;
RA Nitta K., Oyama F., Oyama R., Sekiguchi K., Kawauchi H., Takayanagi Y.,
RA Hakomori S., Titani K.;
RT "Ribonuclease activity of sialic acid-binding lectin from Rana catesbeiana
RT eggs.";
RL Glycobiology 3:37-45(1993).
RN [5]
RP STRUCTURE BY NMR OF 23-133.
RX PubMed=8953220; DOI=10.1007/bf00410331;
RA Chen C., Hom K., Huang R.F., Chou P.J., Liao Y.D., Huang T.;
RT "The secondary structure of a pyrimidine-guanine sequence-specific
RT ribonuclease possessing cytotoxic activity from the oocytes of Rana
RT catesbeiana.";
RL J. Biomol. NMR 8:331-344(1996).
RN [6]
RP STRUCTURE BY NMR OF 23-133.
RX PubMed=9761686; DOI=10.1006/jmbi.1998.2082;
RA Chang C.-F., Chen C., Chen Y.-C., Hom K., Huang R.-F., Huang T.H.;
RT "The solution structure of a cytotoxic ribonuclease from the oocytes of
RT Rana catesbeiana (bullfrog).";
RL J. Mol. Biol. 283:231-244(1998).
CC -!- FUNCTION: Preferentially cleaves single-stranded RNA at pyrimidine
CC residues with a 3'flanking guanine. Hydrolyzes poly(U) and poly(C) as
CC substrates, and prefers the former. The S-lectins in frog eggs may be
CC involved in the fertilization and development of the frog embryo. This
CC lectin agglutinates various animal cells, including normal lymphocytes,
CC erythrocytes, and fibroblasts of animal and human origin. It is
CC cytotoxic against several tumor cells.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF039104; AAD10702.1; -; mRNA.
DR PIR; A27121; A27121.
DR PDB; 1BC4; NMR; -; A=24-133.
DR PDB; 1KM8; X-ray; 1.90 A; A=23-133.
DR PDB; 1KM9; X-ray; 1.96 A; A=23-133.
DR PDB; 1M07; X-ray; 1.80 A; A/B=23-133.
DR PDBsum; 1BC4; -.
DR PDBsum; 1KM8; -.
DR PDBsum; 1KM9; -.
DR PDBsum; 1M07; -.
DR AlphaFoldDB; P11916; -.
DR BMRB; P11916; -.
DR SMR; P11916; -.
DR EvolutionaryTrace; P11916; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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 3D-structure; Direct protein sequencing; Disulfide bond; Endonuclease;
KW Hydrolase; Lectin; Nuclease; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:3304421"
FT CHAIN 23..133
FT /note="Oocytes ribonuclease"
FT /id="PRO_0000030911"
FT ACT_SITE 32
FT /note="Proton acceptor"
FT ACT_SITE 125
FT /note="Proton donor"
FT BINDING 57..61
FT /ligand="substrate"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:3304421"
FT DISULFID 41..93
FT DISULFID 56..103
FT DISULFID 74..118
FT DISULFID 115..132
FT HELIX 25..32
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:1M07"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:1M07"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:1BC4"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:1M07"
FT HELIX 67..71
FT /evidence="ECO:0007829|PDB:1M07"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:1BC4"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:1M07"
FT STRAND 122..131
FT /evidence="ECO:0007829|PDB:1M07"
SQ SEQUENCE 133 AA; 14762 MW; A7D62594F7D16F0C CRC64;
MCAKSLLLVF GILLGLSHLS LSQNWATFQQ KHIINTPIIN CNTIMDNNIY IVGGQCKRVN
TFIISSATTV KAICTGVINM NVLSTTRFQL NTCTRTSITP RPCPYSSRTE TNYICVKCEN
QYPVHFAGIG RCP
