ID   RIP3_MAIZE              Reviewed;         300 AA.
AC   P25891;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ribosome-inactivating protein 3;
DE   AltName: Full=B-32 protein;
DE   AltName: Full=rRNA N-glycosidase;
DE            EC=3.2.2.22;
GN   Name=CRIP3;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1633495; DOI=10.2307/3869575;
RA   Bass H.W., Webster C., Obrian G.R., Roberts J.K.M., Boston R.S.;
RT   "A maize ribosome-inactivating protein is controlled by the transcriptional
RT   activator Opaque-2.";
RL   Plant Cell 4:225-234(1992).
CC   -!- FUNCTION: Possesses features of some constitutive defense agent. The
CC       coordinate Opaque-2-controlled synthesis of this protein and the major
CC       seed storage proteins (zeins) may provide the germinating seedling with
CC       both nutritional benefits and protection against pathogen invasion of
CC       the surrounding endosperm.
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   -!- SUBUNIT: Monomer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Accumulates to high levels in seeds.
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; M83926; AAA33453.1; -; mRNA.
DR   PDB; 2PQG; X-ray; 2.38 A; A/B=22-286.
DR   PDBsum; 2PQG; -.
DR   AlphaFoldDB; P25891; -.
DR   SMR; P25891; -.
DR   STRING; 4577.GRMZM2G063536_P01; -.
DR   PRIDE; P25891; -.
DR   MaizeGDB; 30000; -.
DR   BRENDA; 3.2.2.22; 6752.
DR   EvolutionaryTrace; P25891; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P25891; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   DisProt; DP02707; -.
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   3D-structure; Cytoplasm; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Reference proteome; Toxin.
FT   CHAIN           1..300
FT                   /note="Ribosome-inactivating protein 3"
FT                   /id="PRO_0000221404"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000250"
FT   STRAND          23..28
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           36..48
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   STRAND          71..78
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           130..133
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           146..156
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           192..204
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           212..220
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           232..238
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           241..253
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   HELIX           270..273
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   TURN            274..276
FT                   /evidence="ECO:0007829|PDB:2PQG"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:2PQG"
SQ   SEQUENCE   300 AA;  33257 MW;  6877DBE944F7A127 CRC64;
     MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH CTDHKGIFQP
     VLPPEKKVPE LWLYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK DGDTHLLGDN
     PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV QMQMQMPEAA
     DLAAAAAADP QADTKSKLVK LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK
     WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTACATA ASADNDDDEA