ID   RIPX_MAIZE              Reviewed;         301 AA.
AC   P28522;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ribosome-inactivating protein;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
DE   Contains:
DE     RecName: Full=Ribosome-inactivating protein alpha chain;
DE   Contains:
DE     RecName: Full=Ribosome-inactivating protein beta chain;
DE   Flags: Precursor;
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 13-49; 155-161 AND
RP   187-215.
RX   PubMed=1744135; DOI=10.1016/s0021-9258(18)54513-0;
RA   Walsh T.A., Morgan A.E., Hey T.D.;
RT   "Characterization and molecular cloning of a proenzyme form of a ribosome-
RT   inactivating protein from maize. Novel mechanism of proenzyme activation by
RT   proteolytic removal of a 2.8-kilodalton internal peptide segment.";
RL   J. Biol. Chem. 266:23422-23427(1991).
CC   -!- FUNCTION: Potent catalytic inactivator of eukaryotic protein synthesis.
CC       It may be a component of natural defense mechanisms involved in
CC       protecting the kernel against soil-borne fungal infections.
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: Synthesized and stored in the kernel as a 34 kDa inactive
CC       precursor. During germination, this neutral precursor is converted into
CC       a basic, active form by limited proteolysis, which removes 25 AA of net
CC       charge -6 from the center of the polypeptide chain. Additional
CC       processing also occurs at the N- and C-termini of the polypeptide. A
CC       two-chain active RIP (comprised of 16.5 and 8.5 kDa fragments that
CC       remain tightly associated) is produced from this processing event.
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; M77122; AAA33508.1; -; mRNA.
DR   PIR; A41590; RLZMRI.
DR   PDB; 2K6H; NMR; -; A=17-162, A=190-288.
DR   PDB; 2PQI; X-ray; 2.50 A; A/B/C=22-162, A/B/C=190-288.
DR   PDB; 2PQJ; X-ray; 2.80 A; A/B/C=22-162, A/B/C=190-288.
DR   PDBsum; 2K6H; -.
DR   PDBsum; 2PQI; -.
DR   PDBsum; 2PQJ; -.
DR   AlphaFoldDB; P28522; -.
DR   SMR; P28522; -.
DR   PaxDb; P28522; -.
DR   PRIDE; P28522; -.
DR   MaizeGDB; 30000; -.
DR   eggNOG; ENOG502S89M; Eukaryota.
DR   EvolutionaryTrace; P28522; -.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P28522; baseline and differential.
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   3D-structure; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Reference proteome; Toxin; Zymogen.
FT   PROPEP          1..16
FT                   /note="Or 12 (in 10% of the molecules)"
FT                   /id="PRO_0000030758"
FT   CHAIN           17..161
FT                   /note="Ribosome-inactivating protein alpha chain"
FT                   /id="PRO_0000030759"
FT   PROPEP          162..186
FT                   /evidence="ECO:0000269|PubMed:1744135"
FT                   /id="PRO_0000030760"
FT   CHAIN           187..?257
FT                   /note="Ribosome-inactivating protein beta chain"
FT                   /id="PRO_0000030761"
FT   PROPEP          ?258..301
FT                   /id="PRO_0000030762"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000250"
FT   STRAND          27..30
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           36..48
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          51..54
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   STRAND          72..78
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           90..92
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   TURN            101..103
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           115..117
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   HELIX           130..134
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          135..137
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   HELIX           139..141
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          142..145
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   HELIX           146..157
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           194..204
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           206..210
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           212..220
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   TURN            221..223
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          224..226
FT                   /evidence="ECO:0007829|PDB:2K6H"
FT   HELIX           232..238
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           241..253
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           260..263
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   HELIX           270..276
FT                   /evidence="ECO:0007829|PDB:2PQI"
FT   STRAND          277..280
FT                   /evidence="ECO:0007829|PDB:2PQI"
SQ   SEQUENCE   301 AA;  33330 MW;  C73F599A2121D360 CRC64;
     MAEITLEPSD LMAQTNKRIV PKFTEIFPVE DANYPYSAFI ASVRKDVIKH CTDHKGIFQP
     VLPPEKKVPE LWFYTELKTR TSSITLAIRM DNLYLVGFRT PGGVWWEFGK DGDTHLLGDN
     PRWLGFGGRY QDLIGNKGLE TVTMGRAEMT RAVNDLAKKK KMATLEEEEV KMQMQMPEAA
     DLAAAAAADP QADTKSKLVK LVVMVCEGLR FNTVSRTVDA GFNSQHGVTL TVTQGKQVQK
     WDRISKAAFE WADHPTAVIP DMQKLGIKDK NEAARIVALV KNQTTAAAAT AASADNDDDE
     A