RIPX_CUCPE
ID RIPX_CUCPE Reviewed; 20 AA.
AC P80750;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Ribosome-inactivating protein;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Fragment;
OS Cucurbita pepo (Vegetable marrow) (Summer squash).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX NCBI_TaxID=3663;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Mesocarp;
RX PubMed=9022685; DOI=10.1111/j.1432-1033.1996.0585r.x;
RA Yoshinari S., Yokota S., Sawmoto H., Koresawa S., Tamura M., Endo Y.;
RT "Purification, characterization and subcellular localization of a type-1
RT ribosome-inactivating protein from the sarcocarp of Cucurbita pepo.";
RL Eur. J. Biochem. 242:585-591(1996).
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. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR AlphaFoldDB; P80750; -.
DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Plant defense;
KW Protein synthesis inhibitor; Toxin.
FT CHAIN 1..>20
FT /note="Ribosome-inactivating protein"
FT /id="PRO_0000221399"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 20
SQ SEQUENCE 20 AA; 2235 MW; 8E753D217FDEAA6D CRC64;
NVRFDLSGAT SSSYKTFIKN