ID RNMG_ASPRE Reviewed; 176 AA. AC P67876; P04389; P19792; DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 02-SEP-2026, entry version 80. DE RecName: Full=Ribonuclease mitogillin; DE EC=3.1.27.-; DE AltName: Full=Restrictocin; DE Flags: Precursor; GN Name=ret; OS Aspergillus restrictus. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; Aspergillus. OX NCBI_TaxID=5064; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 34475 / NRRL 2869; RX PubMed=2020539; DOI=10.1093/nar/19.5.1001; RA Lamy B., Davies J.; RT "Isolation and nucleotide sequence of the Aspergillus restrictus gene RT coding for the ribonucleolytic toxin restrictocin and its expression in RT Aspergillus nidulans: the leader sequence protects producing strains from RT suicide."; RL Nucleic Acids Res. 19:1001-1006(1991). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 34475 / NRRL 2869; RX PubMed=1943712; DOI=10.1111/j.1365-2958.1991.tb01930.x; RA Lamy B., Moutaouakil M., Latge J.P., Davies J.; RT "Secretion of a potential virulence factor, a fungal ribonucleotoxin, RT during human aspergillosis infections."; RL Mol. Microbiol. 5:1811-1815(1991). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RC STRAIN=ATCC 34475 / NRRL 2869; RA Yang R., Kenealy W.R.; RT "Regulation and sequence of the restrictocin gene of Aspergillus RT restrictus."; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP PROTEIN SEQUENCE OF 28-176. RX PubMed=3994994; DOI=10.1021/bi00325a008; RA Fernandez-Luna J.L., Lopez-Otin C., Soriano F., Mendez E.; RT "Complete amino acid sequence of the Aspergillus cytotoxin mitogillin."; RL Biochemistry 24:861-867(1985). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 28-176. RX PubMed=8805570; DOI=10.1016/s0969-2126(96)00090-1; RA Yang X., Moffat K.; RT "Insights into specificity of cleavage and mechanism of cell entry from the RT crystal structure of the highly specific Aspergillus ribotoxin, RT restrictocin."; RL Structure 4:837-852(1996). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-176. RX PubMed=11685244; DOI=10.1038/nsb1101-968; RA Yang X., Gerczei T., Glover L.T., Correll C.C.; RT "Crystal structures of restrictocin-inhibitor complexes with implications RT for RNA recognition and base flipping."; RL Nat. Struct. Biol. 8:968-973(2001). CC -!- FUNCTION: This purine-specific ribonuclease cleaves 28S RNA in CC eukaryotic ribosomes, inhibits protein synthesis, and shows antitumor CC activity. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- SIMILARITY: Belongs to the ribonuclease U2 family. {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; X56176; CAA39637.1; -; Genomic_DNA. DR EMBL; M55508; AAA32706.1; -; mRNA. DR EMBL; M65257; AAA32707.1; -; Genomic_DNA. DR PIR; S22294; NRASMR. DR PDB; 1AQZ; X-ray; 1.70 A; A/B=28-176. DR PDB; 1JBR; X-ray; 2.15 A; A/B=28-176. DR PDB; 1JBS; X-ray; 1.97 A; A/B=28-176. DR PDB; 1JBT; X-ray; 2.70 A; A/B=28-176. DR AlphaFoldDB; P67876; -. DR SMR; P67876; -. DR Allergome; 3050; Asp r 1. DR BRENDA; 4.6.1.23; 8124. DR EvolutionaryTrace; P67876; -. DR PRO; PR:P67876; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004521; F:RNA endonuclease activity; IEA:InterPro. DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro. DR CDD; cd00606; fungal_RNase; 1. DR FunFam; 3.10.450.30:FF:000001; Ribonuclease mitogillin; 1. DR Gene3D; 3.10.450.30; Microbial ribonucleases; 1. DR InterPro; IPR004025; Fun_ribotoxin. DR InterPro; IPR000026; N1-like. DR InterPro; IPR016191; Ribonuclease/ribotoxin. DR InterPro; IPR048269; RNase_U2. DR Pfam; PF00545; Ribonuclease; 1. DR PIRSF; PIRSF037430; RNase_U2; 1. DR PRINTS; PR01704; FUNRIBOTOXIN. DR SUPFAM; SSF53933; Microbial ribonucleases; 1. DR PDBsum; 1AQZ; -. DR PDBsum; 1JBR; -. DR PDBsum; 1JBS; -. DR PDBsum; 1JBT; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase; KW Nuclease; Protein synthesis inhibitor; Secreted; Signal. FT SIGNAL 1..27 FT /evidence="ECO:0000269|PubMed:3994994" FT CHAIN 28..176 FT /note="Ribonuclease mitogillin" FT /id="PRO_0000030838" FT ACT_SITE 76 FT ACT_SITE 122 FT /note="Proton acceptor" FT ACT_SITE 163 FT /note="Proton donor" FT DISULFID 32..174 FT DISULFID 102..158 FT CONFLICT 52 FT /note="S -> N (in Ref. 3; AAA32707)" FT /evidence="ECO:0000305" FT CONFLICT 142 FT /note="D -> N (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 29..35 FT /evidence="ECO:0007829|PDB:1AQZ" FT TURN 39..42 FT /evidence="ECO:0007829|PDB:1JBS" FT STRAND 46..52 FT /evidence="ECO:0007829|PDB:1AQZ" FT HELIX 53..62 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 65..68 FT /evidence="ECO:0007829|PDB:1JBS" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:1JBS" FT STRAND 75..78 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:1JBT" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1AQZ" FT HELIX 100..103 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 118..124 FT /evidence="ECO:0007829|PDB:1AQZ" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1AQZ" FT HELIX 140..142 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 157..165 FT /evidence="ECO:0007829|PDB:1AQZ" FT STRAND 171..173 FT /evidence="ECO:0007829|PDB:1AQZ" SQ SEQUENCE 176 AA; 19595 MW; AAD431C57939E42C CRC64; MVAIKNLFLL AATAVSVLAA PSPLDARATW TCINQQLNPK TNKWEDKRLL YSQAKAESNS HHAPLSDGKT GSSYPHWFTN GYDGNGKLIK GRTPIKFGKA DCDRPPKHSQ NGMGKDDHYL LEFPTFPDGH DYKFDSKKPK EDPGPARVIY TYPNKVFCGI VAHQRGNQGD LRLCSH //