ID   RIP5_SAPOF              Reviewed;         253 AA.
AC   Q41389;
DT   08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ribosome-inactivating protein saporin-5;
DE            Short=SAP-5;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
GN   Name=SAP5;
OS   Saponaria officinalis (Common soapwort) (Lychnis saponaria).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Saponaria.
OX   NCBI_TaxID=3572;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=8454624; DOI=10.1016/s0021-9258(18)53284-1;
RA   Barthelemy I., Martineau D., Ong M., Matsunami R., Ling N., Benatti L.,
RA   Cavallaro U., Soria M., Lappi D.A.;
RT   "The expression of saporin, a ribosome-inactivating protein from the plant
RT   Saponaria officinalis, in Escherichia coli.";
RL   J. Biol. Chem. 268:6541-6548(1993).
CC   -!- FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein
CC       synthesis in animal cells. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; X69131; CAA48885.1; -; Genomic_DNA.
DR   EMBL; X69132; CAA48886.1; -; Genomic_DNA.
DR   PIR; S16487; S16487.
DR   PIR; S28539; S28539.
DR   PIR; S38527; S38527.
DR   AlphaFoldDB; Q41389; -.
DR   SMR; Q41389; -.
DR   Allergome; 2805; Sap o RIP.
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   3: Inferred from homology;
KW   Hydrolase; Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..253
FT                   /note="Ribosome-inactivating protein saporin-5"
FT                   /id="PRO_0000221413"
FT   ACT_SITE        176
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   253 AA;  28557 MW;  539693E13D0F594D CRC64;
     VTSITLDLVN PTAGQYSSFV DKIRNNVKDP NLKYGGTDIA VIGPPSKEKF LRINFQSSRG
     TVSLGLKRDN LYVVAYLAMD NTNVNRAYYF RSEITSAELT ALFPEATTAN QKALEYTEDY
     QSIEKNAQIT QGDKSRKELG LGIDLLLTSM EAVNKKARVV KNEARFLLIA IQMTAEVARF
     RYIQNLVTKN FPNKFDSDNK VIQFEVSWRK ISTAIYGDAK NGVFNKDYDF GFGKVRQVKD
     LQMGLLMYLG KPK