RIP6_SAPOF
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 25-MAY-2022, entry version 111.
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}.
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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 PDBsum; 1QI7; -.
DR AlphaFoldDB; P20656; -.
DR SMR; P20656; -.
DR Allergome; 2805; Sap o RIP.
DR EvolutionaryTrace; P20656; -.
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..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..196
FT /evidence="ECO:0007829|PDB:1QI7"
FT HELIX 199..203
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
