RIP2_SAPOF
ID RIP2_SAPOF Reviewed; 292 AA.
AC P27559; Q41390; Q9SAP5;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Ribosome-inactivating protein saporin-2;
DE Short=SAP-2;
DE Short=SO-2;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
GN Name=SAP2;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-284.
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).
RN [3]
RP PROTEIN SEQUENCE OF 25-54.
RX PubMed=8218413; DOI=10.1016/0167-4781(93)90034-b;
RA Ferreras J.M., Barbieri L., Girbes T., Battelli M.G., Rojo M.A.,
RA Arias F.J., Rocher M.A., Soriano F., Mendez E., Stirpe F.;
RT "Distribution and properties of major ribosome-inactivating proteins (28 S
RT rRNA N-glycosidases) of the plant Saponaria officinalis L.
RT (Caryophyllaceae).";
RL Biochim. Biophys. Acta 1216:31-42(1993).
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; X59255; CAA41948.1; -; Genomic_DNA.
DR EMBL; X69132; CAA48886.1; -; Genomic_DNA.
DR EMBL; X69133; CAA48887.1; -; Genomic_DNA.
DR PIR; S16487; S16487.
DR PIR; S17933; RLQHG2.
DR PIR; S38527; S38527.
DR AlphaFoldDB; P27559; -.
DR SMR; P27559; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Plant defense;
KW Protein synthesis inhibitor; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:8218413"
FT CHAIN 25..292
FT /note="Ribosome-inactivating protein saporin-2"
FT /id="PRO_0000030774"
FT ACT_SITE 200
FT /evidence="ECO:0000250"
FT VARIANT 72
FT /note="D -> E"
SQ SEQUENCE 292 AA; 32811 MW; FA143C0E1BE88976 CRC64;
MKIYVVATIA WILLQFSAWT TTDAVTSITL DLVNPTAGQY SSFVDKIRNN VKDPNLKYGG
TDIAVIGPPS KDKFLRINFQ SSRGTVSLGL KRDNLYVVAY LAMDNTNVNR AYYFKSEITS
AELTALFPEA TTANQKALEY TEDYQSIEKN AQITQGDKSR KELGLGIDLL LTFMEAVNKK
ARVVKNEARF LLIAIQMTAE VARFRYIQNL VTKNFPNKFD SDNKVIQFEV SWRKISTAIY
GDAKNGVFNK DYDFGFGKVR QVKDLQMGLL MYLGKPKSSN EANSTAYATT VL