ID RIP6_SAPOF Reviewed; 299 AA. AC P20656; Q41392; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 02-SEP-2026, entry version 118. DE RecName: Full=Ribosome-inactivating protein saporin-6; DE Short=SAP-6; DE Short=SO-6; DE EC=3.2.2.22; DE AltName: Full=rRNA N-glycosidase; DE Flags: Precursor; GN Name=SAP6; 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 [MRNA] OF 1-283, AND PROTEIN SEQUENCE OF 25-115; RP 206-213 AND 234-277. RC TISSUE=Leaf; RX PubMed=2547612; DOI=10.1111/j.1432-1033.1989.tb14951.x; RA Benatti L., Saccardo M.B., Dani M., Nitti G., Sassano M., Lorenzetti R., RA Lappi D.A., Soria M.; RT "Nucleotide sequence of cDNA coding for saporin-6, a type-1 ribosome- RT inactivating protein from Saponaria officinalis."; RL Eur. J. Biochem. 183:465-470(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-277. 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). RN [3] RP NUCLEOTIDE SEQUENCE OF 275-299. RC TISSUE=Leaf; RX PubMed=1936274; DOI=10.1016/0014-5793(91)81303-p; RA Benatti L., Nitti G., Solinas M., Valsasina B., Vitale A., Ceriotti A., RA Soria M.R.; RT "A Saporin-6 cDNA containing a precursor sequence coding for a carboxyl- RT terminal extension."; RL FEBS Lett. 291:285-288(1991). RN [4] RP PROTEIN SEQUENCE OF 25-61. RX PubMed=3925952; DOI=10.1016/0006-291x(85)91981-3; RA Lappi D.A., Esch F.S., Barbieri L., Stirpe F., Soria M.; RT "Characterization of a Saponaria officinalis seed ribosome-inactivating RT protein: immunoreactivity and sequence homologies."; RL Biochem. Biophys. Res. Commun. 129:934-942(1985). RN [5] RP PROTEIN SEQUENCE OF 25-72 AND 114-154. RX PubMed=2325629; DOI=10.1007/bf00280379; RA Fordham-Skelton A.P., Yarwood A., Croy R.R.D.; RT "Synthesis of saporin gene probes from partial protein sequence data: use RT of inosine-oligonucleotides, genomic DNA and the polymerase chain RT reaction."; RL Mol. Gen. Genet. 221:134-138(1990). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-277, AND ACTIVE SITE. RX PubMed=10745075; DOI=10.1016/s0014-5793(00)01325-9; RA Savino C., Federici L., Ippoliti R., Lendaro E., Tsernoglou D.; RT "The crystal structure of saporin SO6 from Saponaria officinalis and its RT interaction with the ribosome."; RL FEBS Lett. 470:239-243(2000). 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 -!- TISSUE SPECIFICITY: Seeds and leaves of the plant. 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; X15655; CAA33685.1; -; mRNA. DR EMBL; S57638; AAB25863.1; -; mRNA. DR EMBL; X69135; CAA48889.1; -; Genomic_DNA. DR EMBL; X64917; CAA46110.1; -; mRNA. DR PIR; S05205; S05205. DR PIR; S16487; S16487. DR PIR; S18307; S18307. DR PIR; S29931; S29931. DR PIR; S38527; S38527. DR PDB; 1QI7; X-ray; 2.00 A; A=25-277. DR AlphaFoldDB; P20656; -. DR MDposit; P20656; -. DR PCDDB; P20656; -. DR SMR; P20656; -. DR Allergome; 2805; Sap o RIP. DR GlyCosmos; P20656; 1 site, No reported glycans. DR EvolutionaryTrace; P20656; -. DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro. DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1. DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1. DR PANTHER; PTHR33453:SF34; RIBOSOME-INACTIVATING PROTEIN; 1. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1. DR PROSITE; PS00275; SHIGA_RICIN; 1. DR PDBsum; 1QI7; -. 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..24 FT /evidence="ECO:0000269|PubMed:2325629, FT ECO:0000269|PubMed:2547612, ECO:0000269|PubMed:3925952" FT CHAIN 25..277 FT /note="Ribosome-inactivating protein saporin-6" FT /id="PRO_0000030776" FT PROPEP 278..299 FT /evidence="ECO:0000255" FT /id="PRO_0000030777" FT ACT_SITE 200 FT /evidence="ECO:0000269|PubMed:10745075" FT CARBOHYD 283 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VARIANT 72 FT /note="E -> D" FT VARIANT 115 FT /note="R -> K" FT CONFLICT 60 FT /note="G -> S (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 123 FT /note="S -> L (in Ref. 2 and 5)" FT /evidence="ECO:0000305" FT CONFLICT 212 FT /note="I -> T (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 37..51 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:1QI7" FT TURN 92..94 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 97..103 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:1QI7" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 120..126 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 144..151 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 160..163 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 167..175 FT /evidence="ECO:0007829|PDB:1QI7" FT TURN 176..179 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 184..195 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 196..200 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 205..213 FT /evidence="ECO:0007829|PDB:1QI7" FT TURN 214..216 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 223..230 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 232..242 FT /evidence="ECO:0007829|PDB:1QI7" FT STRAND 247..261 FT /evidence="ECO:0007829|PDB:1QI7" FT HELIX 262..265 FT /evidence="ECO:0007829|PDB:1QI7" SQ SEQUENCE 299 AA; 33607 MW; 4BC312958BB4E79B CRC64; MKIYVVATIA WILLQFSAWT TTDAVTSITL DLVNPTAGQY SSFVDKIRNN VKDPNLKYGG TDIAVIGPPS KEKFLRINFQ SSRGTVSLGL KRDNLYVVAY LAMDNTNVNR AYYFRSEITS AESTALFPEA TTANQKALEY TEDYQSIEKN AQITQGDQSR KELGLGIDLL STSMEAVNKK ARVVKDEARF LLIAIQMTAE AARFRYIQNL VIKNFPNKFN SENKVIQFEV NWKKISTAIY GDAKNGVFNK DYDFGFGKVR QVKDLQMGLL MYLGKPKSSN EANSTVRHYG PLKPTLLIT //