ID   RIP1_TRIAN              Reviewed;         294 AA.
AC   P56626; Q9ZQY7;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Type I ribosome-inactivating protein trichoanguina;
DE            Short=RIP;
DE            EC=3.2.2.22;
DE   AltName: Full=Trichoanguin;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Precursor;
GN   Name=TCA;
OS   Trichosanthes anguina (Snake gourd).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Trichosanthes.
OX   NCBI_TaxID=50544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND CHARACTERIZATION.
RC   STRAIN=cv. Anguina; TISSUE=Seed;
RX   PubMed=9931318; DOI=10.1042/bj3380211;
RA   Chow L.-P., Chou M.-H., Ho C.-Y., Chuang C.-C., Pan F.-M., Wu S.-H.,
RA   Lin J.-Y.;
RT   "Purification, characterization and molecular cloning of trichoanguin, a
RT   novel type I ribosome-inactivating protein from the seeds of Trichosanthes
RT   anguina.";
RL   Biochem. J. 338:211-219(1999).
RN   [2]
RP   PROTEIN SEQUENCE OF 20-264.
RC   TISSUE=Seed;
RX   PubMed=11725098; DOI=10.1007/bf02253098;
RA   Chow L.-P., Kamo M., Lin J.-Y., Wang S.-H., Ueno Y., Tsugita A.;
RT   "Amino acid sequence of trichoanguina, a ribosomal-inactivating protein
RT   from Trichosanthes anguina seeds.";
RL   J. Biomed. Sci. 3:178-186(1996).
CC   -!- FUNCTION: Inhibits protein synthesis by depurinating 28S rRNA in
CC       ribosomes.
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}.
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; AF055086; AAD02686.1; -; mRNA.
DR   PIR; JC4840; JC4840.
DR   AlphaFoldDB; P56626; -.
DR   SMR; P56626; -.
DR   PRIDE; P56626; -.
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.
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; 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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:11725098"
FT   CHAIN           20..264
FT                   /note="Type I ribosome-inactivating protein trichoanguina"
FT                   /id="PRO_0000030763"
FT   PROPEP          265..294
FT                   /id="PRO_0000030764"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        70
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        220
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        51
FT                   /note="C -> Y (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        65
FT                   /note="W -> R (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        84
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        152
FT                   /note="A -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="C -> S (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="N -> H (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  32235 MW;  DA4F8B7CE3290994 CRC64;
     MALSFFFLAI SLGSPTAIGD VSFDLSTATK KSYSSFITQL RDALPTQGTV CGIPLLPSTA
     SGSQWFRFFN LTNYNDETVT VAVNVTNVYI VAYRADAVSY FFEDTPAEAF KLIFAGTKTV
     KLPYSGNYDK LQSVVGKQRD MIELGIPALS SAITNMVYYD YQSTAAALLV LIQCTAEAAR
     YKYIEQQVSS HISSNFYPNQ AVISLENKWG ALSKQIQIAN RTGHGQFENP VELYNPDGTR
     FSVTNTSAGV VKGNIKLLLY YKASVGSEYD IPTTILHPGA MGMLHNQNGN YVTM