ID   RIP1_BRYDI              Reviewed;         290 AA.
AC   P33185; Q9S8I9;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 3.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Ribosome-inactivating protein bryodin I;
DE            EC=3.2.2.22;
DE   AltName: Full=BD1;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Precursor;
OS   Bryonia dioica (Red bryony) (Bryonia cretica subsp. dioica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Bryonieae; Bryonia.
OX   NCBI_TaxID=3652;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, MUTAGENESIS OF GLU-212, AND X-RAY CRYSTALLOGRAPHY (2.1
RP   ANGSTROMS).
RC   TISSUE=Leaf;
RX   PubMed=9115985; DOI=10.1021/bi962474+;
RA   Gawlak S.L., Neubauer M., Klei H.E., Chang C.Y.Y., Einspahr H.M.,
RA   Siegall C.B.;
RT   "Molecular, biological, and preliminary structural analysis of recombinant
RT   bryodin 1, a ribosome-inactivating protein from the plant Bryonia dioica.";
RL   Biochemistry 36:3095-3103(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Siegall C.B.;
RT   "Cloning and expression of a gene encoding bryodin 1 from Bryonia dioica.";
RL   Patent number US5541110, 30-JUL-1996.
RN   [3]
RP   PROTEIN SEQUENCE OF 24-66.
RC   TISSUE=Seed;
RX   PubMed=2753596; DOI=10.1111/j.1399-3011.1989.tb01280.x;
RA   Montecucchi P.-C., Lazzarini A.M., Barbieri L., Stirpe F., Soria M.,
RA   Lappi D.;
RT   "N-terminal sequence of some ribosome-inactivating proteins.";
RL   Int. J. Pept. Protein Res. 33:263-267(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 24-43.
RC   TISSUE=Root;
RX   PubMed=7849072; DOI=10.1021/bc00029a008;
RA   Siegall C.B., Gawlak S.L., Chace D., Wolff E.A., Mixan B., Marquardt H.;
RT   "Characterization of ribosome-inactivating proteins isolated from Bryonia
RT   dioica and their utility as carcinoma-reactive immunoconjugates.";
RL   Bioconj. Chem. 5:423-429(1994).
CC   -!- FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein
CC       synthesis in animal cells.
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   -!- PTM: Appears to undergo proteolytic cleavage in the C-terminal to
CC       produce a shorter protein.
CC   -!- BIOTECHNOLOGY: Especially useful as immunotoxin for pharmacological
CC       applications as it has low toxicity in rats and mice but is potent once
CC       inside target cells.
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; I24020; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR   PIR; S16491; S16491.
DR   PDB; 1BRY; X-ray; 2.10 A; Y/Z=24-270.
DR   PDBsum; 1BRY; -.
DR   AlphaFoldDB; P33185; -.
DR   SMR; P33185; -.
DR   EvolutionaryTrace; P33185; -.
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; Direct protein sequencing; Glycoprotein; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:2753596,
FT                   ECO:0000269|PubMed:7849072"
FT   CHAIN           24..270
FT                   /note="Ribosome-inactivating protein bryodin I"
FT                   /id="PRO_0000030754"
FT   PROPEP          271..290
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000030755"
FT   ACT_SITE        183
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        212
FT   CARBOHYD        214
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         212
FT                   /note="E->K: 10-fold reduction in activity."
FT                   /evidence="ECO:0000269|PubMed:9115985"
FT   CONFLICT        61..65
FT                   /note="RSSIS -> LRHXI (in Ref. 3; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          25..29
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           34..46
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           66..69
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          70..76
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          82..88
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   TURN            89..91
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          94..99
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           109..114
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   TURN            115..117
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          123..127
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           134..141
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           152..163
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           167..180
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           182..186
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           188..196
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           206..213
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           215..225
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   TURN            226..230
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          231..239
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   STRAND          245..250
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           254..257
FT                   /evidence="ECO:0007829|PDB:1BRY"
FT   HELIX           266..268
FT                   /evidence="ECO:0007829|PDB:1BRY"
SQ   SEQUENCE   290 AA;  31789 MW;  E966CD9C031A42DB CRC64;
     MIKLLVLWLL ILTIFLKSPT VEGDVSFRLS GATTTSYGVF IKNLREALPY ERKVYNIPLL
     RSSISGSGRY TLLHLTNYAD ETISVAVDVT NVYIMGYLAG DVSYFFNEAS ATEAAKFVFK
     DAKKKVTLPY SGNYERLQTA AGKIRENIPL GLPALDSAIT TLYYYTASSA ASALLVLIQS
     TAESARYKFI EQQIGKRVDK TFLPSLATIS LENNWSALSK QIQIASTNNG QFESPVVLID
     GNNQRVSITN ASARVVTSNI ALLLNRNNIA AIGEDISMTL IGFEHGLYGI