RIPG_SURMU
ID RIPG_SURMU Reviewed; 316 AA.
AC P33186;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Ribosome-inactivating protein gelonin;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
DE AltName: Allergen=Gel m RIP {ECO:0000305};
DE Flags: Precursor;
GN Name=GEL;
OS Suregada multiflora (False lime) (Gelonium multiflorum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Gelonieae;
OC Suregada.
OX NCBI_TaxID=3979;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7916721; DOI=10.1016/0378-1119(93)90097-m;
RA Nolan P.A., Garrison D.A., Better M.;
RT "Cloning and expression of a gene encoding gelonin, a ribosome-inactivating
RT protein from Gelonium multiflorum.";
RL Gene 134:223-227(1993).
RN [2]
RP PROTEIN SEQUENCE OF 47-93.
RC TISSUE=Seed;
RX PubMed=2753596; DOI=10.1111/j.1399-3011.1989.tb01280.x;
RA Montecucchi P.-C., Lazzarini A.M., Barbieri L., Stirpe F., Soria M.,
RA Lappi D.;
RT "N-terminal sequence of some ribosome-inactivating proteins.";
RL Int. J. Pept. Protein Res. 33:263-267(1989).
RN [3]
RP ALLERGEN.
RX PubMed=16238796; DOI=10.1111/j.1365-2222.2005.02338.x;
RA Szalai K., Schoell I., Foerster-Waldl E., Polito L., Bolognesi A.,
RA Untersmayr E., Riemer A.B., Boltz-Nitulescu G., Stirpe F.,
RA Jensen-Jarolim E.;
RT "Occupational sensitization to ribosome-inactivating proteins in
RT researchers.";
RL Clin. Exp. Allergy 35:1354-1360(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=7608981; DOI=10.1006/jmbi.1995.0383;
RA Hosur M.V., Nair B., Satyamurthy P., Misquith S., Surolia A., Kannan K.K.;
RT "X-ray structure of gelonin at 1.8-A resolution.";
RL J. Mol. Biol. 250:368-380(1995).
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 -!- SUBUNIT: Homodimer.
CC -!- ALLERGEN: Causes an allergic reaction in human. Natural protein was
CC found to bind to IgE of two patients who had been working with
CC ribosome-inactivating proteins for two years in a research laboratory
CC setting. {ECO:0000269|PubMed:16238796}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; L12243; AAA16312.1; -; mRNA.
DR PIR; JT0753; JT0753.
DR PDB; 3KTZ; X-ray; 1.60 A; A/B=47-297.
DR PDB; 3KU0; X-ray; 1.90 A; A/B=47-297.
DR PDBsum; 3KTZ; -.
DR PDBsum; 3KU0; -.
DR AlphaFoldDB; P33186; -.
DR SMR; P33186; -.
DR Allergome; 2798; Gel m RIP.
DR EvolutionaryTrace; P33186; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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; Allergen; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Plant defense; Protein synthesis inhibitor;
KW Signal; Toxin.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT PROPEP 27..46
FT /evidence="ECO:0000269|PubMed:2753596"
FT /id="PRO_0000030786"
FT CHAIN 47..297
FT /note="Ribosome-inactivating protein gelonin"
FT /id="PRO_0000030787"
FT PROPEP 298..316
FT /note="Removed in mature form"
FT /id="PRO_0000030788"
FT ACT_SITE 212
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 90..96
FT CONFLICT 90
FT /note="C -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="P -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 60..73
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:3KTZ"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:3KTZ"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 121..126
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 138..143
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:3KTZ"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 211..215
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:3KTZ"
FT TURN 225..228
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 235..252
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 259..267
FT /evidence="ECO:0007829|PDB:3KTZ"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 279..282
FT /evidence="ECO:0007829|PDB:3KTZ"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:3KTZ"
SQ SEQUENCE 316 AA; 35419 MW; 1252F3E710901B85 CRC64;
MKGNMKVYWI KIAVATWFCC TTIVLGSTAR IFSLPTNDEE ETSKTLGLDT VSFSTKGATY
ITYVNFLNEL RVKLKPEGNS HGIPLLRKKC DDPGKCFVLV ALSNDNGQLA EIAIDVTSVY
VVGYQVRNRS YFFKDAPDAA YEGLFKNTIK TRLHFGGSYP SLEGEKAYRE TTDLGIEPLR
IGIKKLDENA IDNYKPTEIA SSLLVVIQMV SEAARFTFIE NQIRNNFQQR IRPANNTISL
ENKWGKLSFQ IRTSGANGMF SEAVELERAN GKKYYVTAVD QVKPKIALLK FVDKDPKTSL
AAELIIQNYE SLVGFD
