RIP_FLAVE
ID RIP_FLAVE Reviewed; 25 AA.
AC P83324;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 02-JUN-2021, entry version 36.
DE RecName: Full=Ribosome-inactivating protein velutin;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Fragment;
OS Flammulina velutipes (Agaricus velutipes).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Physalacriaceae; Flammulina.
OX NCBI_TaxID=38945;
RN [1]
RP PROTEIN SEQUENCE, AND FUNCTION.
RX PubMed=11324720; DOI=10.1016/s0024-3205(01)01023-2;
RA Wang H., Ng T.B.;
RT "Isolation and characterization of velutin, a novel low-molecular-weight
RT ribosome-inactivating protein from winter mushroom (Flammulina velutipes)
RT fruiting bodies.";
RL Life Sci. 68:2151-2158(2001).
CC -!- FUNCTION: Inhibits protein synthesis but does not possess ribonuclease
CC activity. Also inhibits HIV-1 reverse transcriptase, beta-glucosidase
CC and beta-glucuronidase. {ECO:0000269|PubMed:11324720}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific
CC adenosine on the 28S rRNA.; EC=3.2.2.22;
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000305}.
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DR GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Protein synthesis inhibitor; Toxin.
FT CHAIN 1..>25
FT /note="Ribosome-inactivating protein velutin"
FT /id="PRO_0000221420"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 25
SQ SEQUENCE 25 AA; 2898 MW; EB73FCF9AA0993DB CRC64;
XHPDLFXXRP DNTASPKFED PRLNP