ID   RIPD2_PHYDI             Reviewed;         266 AA.
AC   P85208;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=Dioicin-2;
DE            EC=3.2.2.22;
DE   AltName: Full=Ribosome-inactivating protein {ECO:0000303|PubMed:18704492};
DE   AltName: Full=rRNA N-glycosidase {ECO:0000303|PubMed:18704492};
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] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   DEVELOPMENTAL STAGE, MASS SPECTROMETRY, AND DISULFIDE BONDS.
RC   TISSUE=Leaf {ECO:0000269|PubMed:18704492};
RX   PubMed=18704492; DOI=10.1007/s00425-008-0796-z;
RA   Parente A., Conforto B., Di Maro A., Chambery A., De Luca P., Bolognesi A.,
RA   Iriti M., Faoro F.;
RT   "Type 1 ribosome-inactivating proteins from Phytolacca dioica L. leaves:
RT   differential seasonal and age expression, and cellular localization.";
RL   Planta 228:963-975(2008).
CC   -!- FUNCTION: Nicks pBR322 dsDNA. Has adenine polynucleotide glycosidase
CC       activity on herring sperm ssDNA. {ECO:0000269|PubMed:18704492}.
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         Evidence={ECO:0000269|PubMed:18704492};
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC       {ECO:0000269|PubMed:18704492}. Golgi apparatus
CC       {ECO:0000269|PubMed:18704492}. Vacuole {ECO:0000269|PubMed:18704492}.
CC   -!- DEVELOPMENTAL STAGE: Detected in fully expanded leaves of 8 to 34 month
CC       old plants, levels peak in autumn. Also present in developing leaves
CC       (10-60 days old) of adult plants. {ECO:0000269|PubMed:18704492}.
CC   -!- MASS SPECTROMETRY: Mass=29910.00; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:18704492};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000255}.
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DR   AlphaFoldDB; P85208; -.
DR   SMR; P85208; -.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
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; Golgi apparatus; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Secreted; Toxin; Vacuole.
FT   CHAIN           1..266
FT                   /note="Dioicin-2"
FT                   /id="PRO_0000372680"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250|UniProtKB:P20656"
FT   DISULFID        32..263
FT                   /evidence="ECO:0000269|PubMed:18704492"
FT   DISULFID        85..102
FT                   /evidence="ECO:0000269|PubMed:18704492"
SQ   SEQUENCE   266 AA;  29914 MW;  3D8363C8CC46C53A CRC64;
     NIVFDVENAT PETYSSFLTS LREAVKDKKS TCHGMIMATT TTELPKYVLV DLKLGSEKDA
     KTFTLAIRRG NLYLEGYSDI YNEKCRYRIF EDSESDAQQT VCPGDLTLPG SQNKIPYKKS
     YQSMESKGGD RTKLGLGQIT LESRMNKIYG KDATDQKQFQ KNEAEFLLIA VQMITEASRF
     KYIENKVKDS FDDAIGYKPD PKAISLETSW DKISNAIAKV NTPGNSIVTL PKGLLDENKK
     PWTTATMDEL KNDIMGLLTH VTCKIK