RNAG_AGRAE
ID RNAG_AGRAE Reviewed; 156 AA.
AC C0HLG3; A0A5B9CUE1;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 3.
DT 03-AUG-2022, entry version 11.
DE RecName: Full=Ribonuclease ageritin {ECO:0000303|PubMed:28232091};
DE EC=4.6.1.23 {ECO:0000269|PubMed:28232091, ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206};
DE AltName: Full=Ribotoxin {ECO:0000303|PubMed:31444206};
DE Flags: Precursor;
GN Name=AGT1 {ECO:0000303|PubMed:31444206}; ORFNames=AAE3_01767;
OS Agrocybe aegerita (Black poplar mushroom) (Agaricus aegerita).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Bolbitiaceae; Cyclocybe.
OX NCBI_TaxID=1973307;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=AAE-3;
RX PubMed=31444206; DOI=10.1128/aem.01549-19;
RA Tayyrov A., Azevedo S., Herzog R., Vogt E., Arzt S., Luethy P., Mueller P.,
RA Ruehl M., Hennicke F., Kuenzler M.;
RT "Heterologous production and functional characterization of ageritin, a
RT novel type of ribotoxin highly expressed during fruiting of the edible
RT mushroom Agrocybe aegerita.";
RL Appl. Environ. Microbiol. 85:0-0(2019).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RX PubMed=32998313; DOI=10.3390/ijms21197158;
RA Baglivo I., Ragucci S., D'Incecco P., Landi N., Russo R., Faoro F.,
RA Pedone P.V., Di Maro A.;
RT "Gene organization, expression, and localization of ribotoxin-like protein
RT ageritin in fruiting body and mycelium of Agrocybe aegerita.";
RL Int. J. Mol. Sci. 21:0-0(2020).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAE-3;
RX PubMed=29334897; DOI=10.1186/s12864-017-4430-y;
RA Gupta D.K., Ruehl M., Mishra B., Kleofas V., Hofrichter M., Herzog R.,
RA Pecyna M.J., Sharma R., Kellner H., Hennicke F., Thines M.;
RT "The genome sequence of the commercially cultivated mushroom Agrocybe
RT aegerita reveals a conserved repertoire of fruiting-related genes and a
RT versatile suite of biopolymer-degrading enzymes.";
RL BMC Genomics 19:48-48(2018).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 22-46, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28232091; DOI=10.1016/j.bbagen.2017.02.023;
RA Landi N., Pacifico S., Ragucci S., Iglesias R., Piccolella S., Amici A.,
RA Di Giuseppe A.M.A., Di Maro A.;
RT "Purification, characterization and cytotoxicity assessment of Ageritin:
RT The first ribotoxin from the basidiomycete mushroom Agrocybe aegerita.";
RL Biochim. Biophys. Acta 1861:1113-1121(2017).
RN [5]
RP PROTEIN SEQUENCE OF 61-69; 117-135 AND 141-156, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=30541087; DOI=10.1093/jb/mvy113;
RA Landi N., Ragucci S., Russo R., Pedone P.V., Chambery A., Di Maro A.;
RT "Structural insights into nucleotide and protein sequence of Ageritin: a
RT novel prototype of fungal ribotoxin.";
RL J. Biochem. 165:415-422(2019).
RN [6] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MASS SPECTROMETRY.
RX PubMed=30262416; DOI=10.1016/j.bbagen.2018.09.010;
RA Ruggiero A., Garcia-Ortega L., Ragucci S., Russo R., Landi N., Berisio R.,
RA Di Maro A.;
RT "Structural and enzymatic properties of Ageritin, a novel metal-dependent
RT ribotoxin-like protein with antitumor activity.";
RL Biochim. Biophys. Acta 1862:2888-2894(2018).
CC -!- FUNCTION: Fungal ribonuclease involved in fungal defense. Highly
CC specific and highly toxic fungal endonuclease that cleaves a single
CC phosphodiester bond in the 28S RNA of eukaryotic ribosomes at a
CC universally conserved GAGA tetraloop of the sarcin-ricin loop (SRL).
CC The damage of the SRL inhibits the binding of translation elongation
CC factors and halts protein biosynthesis, ultimately resulting in the
CC death of the target cells (PubMed:31444206, PubMed:28232091,
CC PubMed:30262416). Shows antitumor activity (PubMed:28232091,
CC PubMed:30262416). Exerts cytotoxicity and induces apoptosis towards rat
CC glial cells and human glioma cells, and also displays some activity
CC towards human neurolastoma cell lines (PubMed:28232091). Shows a strong
CC entomotoxicity against Aedes aegypti larvae, yet no nematotoxicity
CC against nematodes (PubMed:31444206). {ECO:0000269|PubMed:28232091,
CC ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 28S rRNA containing guanosine-adenosine pair + H2O = an [RNA
CC fragment]-3'-adenosine-3'-phosphate + a 5'-a hydroxy-guanosine-3'-
CC [RNA fragment].; EC=4.6.1.23; Evidence={ECO:0000269|PubMed:28232091,
CC ECO:0000269|PubMed:30262416, ECO:0000269|PubMed:31444206};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:30262416};
CC -!- ACTIVITY REGULATION: In contrast to most ribotoxins, activity is
CC completely inhibited by EDTA. {ECO:0000269|PubMed:30262416}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Highly thermostable. Has a melting temperature of 78 degrees Celsius
CC at pH 7.4. {ECO:0000269|PubMed:30262416};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30262416}.
CC -!- SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000269|PubMed:32998313}.
CC Note=Possibly sequestered into the vacuole to avoid its toxic activity
CC on ribosomes. {ECO:0000305|PubMed:32998313}.
CC -!- DEVELOPMENTAL STAGE: Highly Expressed during fruiting body formation.
CC {ECO:0000269|PubMed:31444206}.
CC -!- MASS SPECTROMETRY: Mass=14802.84; Mass_error=1.04; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:30541087};
CC -!- MASS SPECTROMETRY: Mass=14802.94; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:30262416};
CC -!- BIOTECHNOLOGY: The strong larvicidal activity of ageritin makes this
CC protein a promising candidate for novel biopesticide development.
CC {ECO:0000305|PubMed:31444206}.
CC -!- SIMILARITY: Belongs to the ribotoxin-like family. {ECO:0000305}.
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DR EMBL; MK411345; QEE04510.1; -; mRNA.
DR AlphaFoldDB; C0HLG3; -.
DR SMR; C0HLG3; -.
DR BRENDA; 4.6.1.23; 8897.
DR GO; GO:0005775; C:vacuolar lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0004521; F:endoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0033902; F:rRNA endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Hydrolase; Lyase; Magnesium;
KW Metal-binding; Nuclease; Signal; Vacuole.
FT SIGNAL 1..21
FT /evidence="ECO:0000305|PubMed:32998313"
FT CHAIN 22..156
FT /note="Ribonuclease ageritin"
FT /evidence="ECO:0000269|PubMed:30262416"
FT /id="PRO_0000446086"
FT ACT_SITE 98
FT /evidence="ECO:0000305|PubMed:30541087"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 139
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 39
FT /note="C -> M (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="F -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="K -> V (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="A -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 156 AA; 16910 MW; A18DDC3863F6BDE6 CRC64;
MSESSTFTTA VVPEGEGVAP MAETVQYYNS YSDASIASCA FVDSGKDKID KTKLVTYTSR
LAASPAYQKV VGVGLKTAAG SIVPYVRLDM DNTGKGIHFN ATKLSDSSAK LAAVLKTTVS
MTEAQRTQLY MEYIKGIENR SAQFIWDWWR TGKAPA
