ID   RIP2_PHYDI              Reviewed;         265 AA.
AC   P34967;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Protein synthesis inhibitor PD-S2;
DE            EC=3.2.2.22;
DE   AltName: Full=Ribosome-inactivating protein PD-S2;
DE   AltName: Full=rRNA N-glycosidase;
OS   Phytolacca dioica (Bella sombra tree) (Phytolacca arborea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Phytolaccaceae; Phytolacca.
OX   NCBI_TaxID=29725;
RN   [1]
RP   PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-120.
RC   TISSUE=Seed;
RX   PubMed=9074624; DOI=10.1016/s0167-4838(96)00182-3;
RA   Del Vecchio Blanco F., Bolognesi A., Malorni A., Sande M.J.W., Savino G.,
RA   Parente A.;
RT   "Complete amino-acid sequence of PD-S2, a new ribosome-inactivating protein
RT   from seeds of Phytolacca dioica L.";
RL   Biochim. Biophys. Acta 1338:137-144(1997).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-32.
RC   TISSUE=Seed;
RX   PubMed=8218414; DOI=10.1016/0167-4781(93)90035-c;
RA   Parente A., de Luca P., Bolognesi A., Barbieri L., Battelli M.G.,
RA   Abbondanza A., Sande M.J.W., Gigliano G.S., Tazzari P.L., Stirpe F.;
RT   "Purification and partial characterization of single-chain ribosome-
RT   inactivating proteins from the seeds of Phytolacca dioica L.";
RL   Biochim. Biophys. Acta 1216:43-49(1993).
CC   -!- FUNCTION: Inhibits protein synthesis in animal cells. Useful as
CC       immunotoxin for pharmacological applications.
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   -!- TISSUE SPECIFICITY: Seeds.
CC   -!- PTM: Glycosylated. {ECO:0000269|PubMed:9074624}.
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   PIR; S38528; S38528.
DR   AlphaFoldDB; P34967; -.
DR   SMR; P34967; -.
DR   iPTMnet; P34967; -.
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; 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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..265
FT                   /note="Protein synthesis inhibitor PD-S2"
FT                   /id="PRO_0000221406"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:9074624"
FT   DISULFID        34..262
FT                   /evidence="ECO:0000250"
FT   DISULFID        88..110
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   265 AA;  29587 MW;  EAD68733A166DCA3 CRC64;
     VSTITFDVGS ATISKYTTFL ESLRNQAKDP SLKCYGIPML PNTNPNPKYL LVELNAKLSS
     GEVKSITLML RRHNLYVMGY SDPYDNKCRY HIFKDISSTT ERKDVETTLC PNASSRVSKN
     ISYDSSYPAL ENKAGRSRSQ VQLGIQILNS DIGKISGVKS FTDKTEAEFL LVAIQMVSEA
     TRFKYIENQV KTNFNRAFYP NAKVLNLEET WGKISMAIHG AKNGAFSKPL ELQNADGSKW
     IVLRVDEIKP DVALLKYVSG SCQAT