ID   RIPS_TRIKI              Reviewed;         289 AA.
AC   P24478;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Ribosome-inactivating protein karasurin-C;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
DE   Contains:
DE     RecName: Full=Ribosome-inactivating protein karasurin-A;
DE   Flags: Precursor;
OS   Trichosanthes kirilowii (Chinese snake gourd) (Chinese cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Trichosanthes.
OX   NCBI_TaxID=3677;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Root tuber;
RX   PubMed=9212998; DOI=10.1248/bpb.20.711;
RA   Mizukami H., Iida K., Kondo T., Ogihara Y.;
RT   "Cloning and bacterial expression of a gene encoding ribosome-inactivating
RT   proteins, karasurin-A and karasurin-C, from Trichosanthes kirilowii var.
RT   japonica.";
RL   Biol. Pharm. Bull. 20:711-713(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 22-270.
RX   PubMed=8951169; DOI=10.1248/bpb.19.1485;
RA   Kondo T., Mizukami H., Takeda T., Ogihara Y.;
RT   "Amino acid sequences and ribosome-inactivating activities of karasurin-B
RT   and karasurin-C.";
RL   Biol. Pharm. Bull. 19:1485-1489(1996).
RN   [3]
RP   PROTEIN SEQUENCE OF 24-270.
RX   PubMed=1914000; DOI=10.1248/cpb.39.1244;
RA   Toyokawa S., Takeda T., Kato Y., Wakabayashi K., Ogihara Y.;
RT   "The complete amino acid sequence of an abortifacient protein, karasurin.";
RL   Chem. Pharm. Bull. 39:1244-1249(1991).
CC   -!- FUNCTION: Abortion-inducing protein. It inactivates eukaryotic 60S
CC       ribosomal subunits.
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   EMBL; AB000666; BAA21786.1; -; Genomic_DNA.
DR   PIR; JC5606; JC5606.
DR   PIR; JU0393; JU0393.
DR   AlphaFoldDB; P24478; -.
DR   SMR; P24478; -.
DR   BRENDA; 3.2.2.22; 6463.
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:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.420.10; -; 1.
DR   Gene3D; 4.10.470.10; -; 1.
DR   InterPro; IPR036041; Ribosome-inact_prot_sf.
DR   InterPro; IPR017989; Ribosome_inactivat_1/2.
DR   InterPro; IPR001574; Ribosome_inactivat_prot.
DR   InterPro; IPR017988; Ribosome_inactivat_prot_CS.
DR   InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR   InterPro; IPR016139; Ribosome_inactivat_prot_sub2.
DR   PANTHER; PTHR33453; PTHR33453; 1.
DR   Pfam; PF00161; RIP; 1.
DR   PRINTS; PR00396; SHIGARICIN.
DR   SUPFAM; SSF56371; SSF56371; 1.
DR   PROSITE; PS00275; SHIGA_RICIN; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Direct protein sequencing; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:8951169"
FT   CHAIN           22..270
FT                   /note="Ribosome-inactivating protein karasurin-C"
FT                   /id="PRO_0000030767"
FT   CHAIN           24..270
FT                   /note="Ribosome-inactivating protein karasurin-A"
FT                   /id="PRO_0000030768"
FT   PROPEP          271..289
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000030769"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   289 AA;  31704 MW;  883D3E3242887B26 CRC64;
     MIRFLVFSLL ILTLFLTAPA VEGDVSFRLS GATSSSYGVF ISNLRKALPY ERKLYDIPLL
     RSTLPGSQRY ALIHLTNYAD ETISVAIDVT NVYVMGYRAG DTSYFFNEAS ATEAAKYVFK
     DAKRKVTLPY SGNYERLQIA AGKIRENIPL GLPALDSAIT TLFYYNANSA ASALMVLIQS
     TSEAARYKFI EQQIGKRVDK TFLPSLAIIS LENSWSALSK QIQIASTNNG QFETPVVLIN
     AQNQRVTITN VDAGVVTSNI ALLLNRNNMA AIDDDVPMAQ SFGCGSYAI