ID   RIP9_MAIZE              Reviewed;         304 AA.
AC   P25892;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=Ribosome-inactivating protein 9;
DE            EC=3.2.2.22;
DE   AltName: Full=B-32 protein;
DE   AltName: Full=rRNA N-glycosidase;
GN   Name=CRIP9;
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], AND PROTEIN SEQUENCE OF 282-301.
RC   STRAIN=cv. Wisconsin 64A;
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}.
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; M83927; AAA33454.1; -; mRNA.
DR   AlphaFoldDB; P25892; -.
DR   SMR; P25892; -.
DR   PRIDE; P25892; -.
DR   MaizeGDB; 30000; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P25892; 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   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   Cytoplasm; Direct protein sequencing; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Reference proteome; Toxin.
FT   CHAIN           1..304
FT                   /note="Ribosome-inactivating protein 9"
FT                   /id="PRO_0000221405"
FT   ACT_SITE        208
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   304 AA;  33514 MW;  978789A2DD2BBF3C CRC64;
     MAETNPELSD LMAQTNKKIV PKFTEIFPVE DVNYPYSAFI ASVRKDVIKH CTDHKGIFQP
     VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK AGDTHLLGDN
     PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV QMQMQMPEAA
     ELAAAAAAAD PQADTKSKLV KLVVMVCEGL RFNTVSRTVD AGFNSQHGVT LTVTQGKQVQ
     KWDRISKAAF EWADHPTAVI PDMQKLGIKD KNEAARIVAL VKNQTTAAAA AATAASADND
     DDEA