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RIP3_SAPOF
ID   RIP3_SAPOF              Reviewed;         236 AA.
AC   P27560;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Ribosome-inactivating protein saporin-3;
DE            Short=SAP-3;
DE            Short=SO-3;
DE            EC=3.2.2.22;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Fragment;
GN   Name=SAP3;
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].
RX   PubMed=1719367; DOI=10.1007/bf00267470;
RA   Fordham-Skelton A.P., Taylor P.E., Hartley M.R., Croy R.R.D.;
RT   "Characterisation of saporin genes: in vitro expression and ribosome
RT   inactivation.";
RL   Mol. Gen. Genet. 229:460-466(1991).
CC   -!- FUNCTION: Ribosome-inactivating protein of type 1, inhibits protein
CC       synthesis in animal cells. Useful as immunotoxin for pharmacological
CC       applications.
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; X59256; CAA41949.1; -; Genomic_DNA.
DR   PIR; S17932; S17932.
DR   AlphaFoldDB; P27560; -.
DR   SMR; P27560; -.
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..236
FT                   /note="Ribosome-inactivating protein saporin-3"
FT                   /id="PRO_0000221412"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   236 AA;  26591 MW;  DE3D68BA50FCE054 CRC64;
     DPNLKYGGTD IAVIGPPSRD KFLRLNFQSS RGTVSLGLKR ENLYVVAYLA MDNANVNRAY
     YFGTEITSAE LTTLLPEATV ANQKALEYTE DYQSIEKNAK ITEGDKTRKE LGLGINLLST
     LMDAVNKKAR VVKNEARFLL IAIQMTAEAA RFRYIQNLVT KNFPNKFNSE DKVIQFQVNW
     SKISKAIYGD AKNGVFNKDY DFGFGKVRQV KDLQMGLLMY LGTTPNNAAD RYRAEL
 
 
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