ID   RIPLY_SILCH             Reviewed;         234 AA.
AC   P85101;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Ribosome-inactivating protein lychnin;
DE            EC=3.2.2.22;
OS   Silene chalcedonica (Maltese-cross) (Lychnis chalcedonica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Sileneae; Silene; Silene subgen. Lychnis;
OC   Silene sect. Lychnis.
OX   NCBI_TaxID=39855;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, MASS SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Seed {ECO:0000269|PubMed:16972795};
RX   PubMed=16972795; DOI=10.1515/bc.2006.156;
RA   Chambery A., de Donato A., Bolognesi A., Polito L., Stirpe F., Parente A.;
RT   "Sequence determination of lychnin, a type 1 ribosome-inactivating protein
RT   from Lychnis chalcedonica seeds.";
RL   Biol. Chem. 387:1261-1266(2006).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION, AND FUNCTION.
RX   PubMed=2248976; DOI=10.1016/0167-4781(90)90002-j;
RA   Bolognesi A., Barbieri L., Abbondanza A., Falasca A.I., Carnicelli D.,
RA   Battelli M.G., Stirpe F.;
RT   "Purification and properties of new ribosome-inactivating proteins with RNA
RT   N-glycosidase activity.";
RL   Biochim. Biophys. Acta 1087:293-302(1990).
RN   [3]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=12832768; DOI=10.1107/s0907444903010680;
RA   Fermani S., Falini G., Ripamonti A., Bolognesi A., Polito L., Stirpe F.;
RT   "Crystallization and preliminary X-ray diffraction analysis of two
RT   ribosome-inactivating proteins: lychnin and dianthin 30.";
RL   Acta Crystallogr. D 59:1227-1229(2003).
RN   [4] {ECO:0007744|PDB:2G5X}
RP   X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS).
RA   Fermani S., Falini G., Tosi G., Ripamonti A., Polito L., Bolognesi A.,
RA   Stirpe F.;
RT   "Crystal structure of lychnin a type 1 ribosome inactivating protein
RT   (rip).";
RL   Submitted (FEB-2006) to the PDB data bank.
CC   -!- FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein
CC       synthesis in animal cells. Inhibits cell-free translation in rabbit
CC       reticulocyte lysate system with an IC(50) of 0.17 nM.
CC       {ECO:0000269|PubMed:2248976}.
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:2248976};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12832768}.
CC   -!- MASS SPECTROMETRY: Mass=26131.14; Mass_error=0.46; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:16972795};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000255}.
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DR   PDB; 2G5X; X-ray; 1.70 A; A=1-234.
DR   PDBsum; 2G5X; -.
DR   AlphaFoldDB; P85101; -.
DR   SMR; P85101; -.
DR   EvolutionaryTrace; P85101; -.
DR   GO; GO:0030597; F:RNA glycosylase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; Disulfide bond; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..234
FT                   /note="Ribosome-inactivating protein lychnin"
FT                   /id="PRO_0000283747"
FT   ACT_SITE        170
FT                   /evidence="ECO:0000250|UniProtKB:P10297"
FT   DISULFID        32..115
FT                   /evidence="ECO:0000269|PubMed:16972795"
SQ   SEQUENCE   234 AA;  26132 MW;  3F8B2CBD614EB80F CRC64;
     RPSWTVDSDS AKYSSFLDSL REEFGRGTPK VCNIPVTKKA NNDKFVLVNL VLPFNRNTIT
     LAFRASDAYL VGFQDRDSKT NKLRANFFSD EYRALSGKYK SIFTDAEVLA PALPCASTYT
     DLQNKAGVSR EKLSLGVSSL QTAFTAVYGK VFTGKNVAKF ALISIQMVAE AARFKYIEDQ
     VINRGMYSSF EAGARITLLE NNWSKISEQY HKSCKLGGGQ FTEEEMKLGL LLYN