ID   RNP30_LITPI             Reviewed;         104 AA.
AC   P22069;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Protein P-30;
DE            EC=3.1.27.-;
DE   AltName: Full=Onconase;
OS   Lithobates pipiens (Northern leopard frog) (Rana pipiens).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Lithobates.
OX   NCBI_TaxID=8404;
RN   [1]
RP   PROTEIN SEQUENCE, AND PYROGLUTAMATE FORMATION AT GLN-1.
RC   TISSUE=Embryo;
RX   PubMed=1985896; DOI=10.1016/s0021-9258(18)52427-3;
RA   Ardelt W., Mikulski S.M., Shogen K.;
RT   "Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and
RT   early embryos. Homology to pancreatic ribonucleases.";
RL   J. Biol. Chem. 266:245-251(1991).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX   PubMed=8120892; DOI=10.1016/0022-2836(94)90017-5;
RA   Mosimann S.C., Ardelt W., James M.N.G.;
RT   "Refined 1.7 A X-ray crystallographic structure of P-30 protein, an
RT   amphibian ribonuclease with anti-tumor activity.";
RL   J. Mol. Biol. 236:1141-1153(1994).
CC   -!- FUNCTION: Basic protein with antiproliferative/cytotoxic activity
CC       against several tumor cell lines in vitro, as well as antitumor in
CC       vivo. It exhibits a ribonuclease-like activity against high molecular
CC       weight ribosomal RNA.
CC   -!- DEVELOPMENTAL STAGE: Early embryos (up to four blastomere stage).
CC   -!- SIMILARITY: Belongs to the pancreatic ribonuclease family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC       Note=Onconase;
CC       URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_other_804";
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DR   PDB; 1ONC; X-ray; 1.70 A; A=2-104.
DR   PDB; 1PU3; NMR; -; A=1-104.
DR   PDB; 1YV4; X-ray; 1.51 A; A=1-104.
DR   PDB; 1YV6; X-ray; 1.78 A; A=1-104.
DR   PDB; 1YV7; X-ray; 1.90 A; A=1-102.
DR   PDB; 2GMK; X-ray; 1.65 A; A=1-104.
DR   PDB; 2I5S; X-ray; 1.90 A; X=1-104.
DR   PDB; 2KB6; NMR; -; A=1-104.
DR   PDB; 2LT5; NMR; -; A=2-104.
DR   PDB; 3FD7; X-ray; 1.53 A; A/B=1-104.
DR   PDB; 3HG6; X-ray; 1.70 A; A=2-104.
DR   PDB; 3PHN; X-ray; 1.46 A; A=2-104.
DR   PDB; 3SNF; X-ray; 1.10 A; A=1-104.
DR   PDB; 3U00; X-ray; 1.65 A; A=2-104.
DR   PDB; 3U01; X-ray; 1.12 A; A=2-104.
DR   PDB; 7OR6; X-ray; 2.12 A; AAA/BBB=2-104.
DR   PDB; 7ORD; X-ray; 2.14 A; AAA/BBB=2-104.
DR   PDBsum; 1ONC; -.
DR   PDBsum; 1PU3; -.
DR   PDBsum; 1YV4; -.
DR   PDBsum; 1YV6; -.
DR   PDBsum; 1YV7; -.
DR   PDBsum; 2GMK; -.
DR   PDBsum; 2I5S; -.
DR   PDBsum; 2KB6; -.
DR   PDBsum; 2LT5; -.
DR   PDBsum; 3FD7; -.
DR   PDBsum; 3HG6; -.
DR   PDBsum; 3PHN; -.
DR   PDBsum; 3SNF; -.
DR   PDBsum; 3U00; -.
DR   PDBsum; 3U01; -.
DR   PDBsum; 7OR6; -.
DR   PDBsum; 7ORD; -.
DR   AlphaFoldDB; P22069; -.
DR   BMRB; P22069; -.
DR   SMR; P22069; -.
DR   BRENDA; 4.6.1.18; 5287.
DR   EvolutionaryTrace; P22069; -.
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; Nuclease; Pyrrolidone carboxylic acid.
FT   CHAIN           1..104
FT                   /note="Protein P-30"
FT                   /id="PRO_0000057174"
FT   ACT_SITE        10
FT                   /note="Proton acceptor"
FT   ACT_SITE        97
FT                   /note="Proton donor"
FT   BINDING         31..35
FT                   /ligand="substrate"
FT   MOD_RES         1
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000269|PubMed:1985896"
FT   DISULFID        19..68
FT   DISULFID        30..75
FT   DISULFID        48..90
FT   DISULFID        87..104
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          11..16
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   HELIX           19..22
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          23..25
FT                   /evidence="ECO:0007829|PDB:3FD7"
FT   TURN            26..30
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   HELIX           41..45
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   HELIX           46..48
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          63..70
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          77..84
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          86..91
FT                   /evidence="ECO:0007829|PDB:3SNF"
FT   STRAND          94..102
FT                   /evidence="ECO:0007829|PDB:3SNF"
SQ   SEQUENCE   104 AA;  11845 MW;  22A753C2F9E566B4 CRC64;
     QDWLTFQKKH ITNTRDVDCD NIMSTNLFHC KDKNTFIYSR PEPVKAICKG IIASKNVLTT
     SEFYLSDCNV TSRPCKYKLK KSTNKFCVTC ENQAPVHFVG VGSC