RIP0_DIACA
ID RIP0_DIACA Reviewed; 293 AA.
AC P24476;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Ribosome-inactivating protein dianthin-30 {ECO:0000303|PubMed:12832768, ECO:0000303|PubMed:15681236, ECO:0000303|PubMed:16238796, ECO:0000303|PubMed:1840496};
DE Short=RIP DAP-30 {ECO:0000303|PubMed:1936243};
DE EC=3.2.2.22 {ECO:0000250|UniProtKB:P84853};
DE AltName: Full=Antiviral protein DAP-30 {ECO:0000303|PubMed:1936243};
DE AltName: Full=rRNA N-glycosidase {ECO:0000303|PubMed:15681236};
DE AltName: Allergen=Dia c RIP {ECO:0000305};
DE Flags: Precursor;
OS Dianthus caryophyllus (Carnation) (Clove pink).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX NCBI_TaxID=3570;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leaf {ECO:0000312|EMBL:CAA41953.1};
RX PubMed=1840496; DOI=10.1016/0167-4781(91)90046-o;
RA Legname G., Bellosta P., Gromo G., Modena D., Keen J.N., Roberts L.M.,
RA Lord J.M.;
RT "Nucleotide sequence of cDNA coding for dianthin 30, a ribosome
RT inactivating protein from Dianthus caryophyllus.";
RL Biochim. Biophys. Acta 1090:119-122(1991).
RN [2]
RP PROTEIN SEQUENCE OF 24-82, FUNCTION, AND MISCELLANEOUS.
RC TISSUE=Leaf {ECO:0000303|PubMed:1936243};
RX PubMed=1936243; DOI=10.1016/0014-5793(91)81122-o;
RA Lee-Huang S., Kung H.-F., Huang P.L., Huang P.L., Li B.-Q., Huang P.,
RA Huang H.I., Chen H.-C.;
RT "A new class of anti-HIV agents: GAP31, DAPs 30 and 32.";
RL FEBS Lett. 291:139-144(1991).
RN [3]
RP CRYSTALLIZATION, AND SUBUNIT.
RX PubMed=12832768; DOI=10.1107/s0907444903010680;
RA Fermani S., Falini G., Ripamonti A., Bolognesi A., Polito L., Stirpe F.;
RT "Crystallization and preliminary X-ray diffraction analysis of two
RT ribosome-inactivating proteins: lychnin and dianthin 30.";
RL Acta Crystallogr. D 59:1227-1229(2003).
RN [4]
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 [5] {ECO:0007744|PDB:1RL0}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 24-278, SUBUNIT, AND TISSUE
RP SPECIFICITY.
RX PubMed=15681236; DOI=10.1016/j.jsb.2004.11.007;
RA Fermani S., Falini G., Ripamonti A., Polito L., Stirpe F., Bolognesi A.;
RT "The 1.4 anstroms structure of dianthin 30 indicates a role of surface
RT potential at the active site of type 1 ribosome inactivating proteins.";
RL J. Struct. Biol. 149:204-212(2005).
CC -!- FUNCTION: Single-chain ribosome-inactivating protein.
CC {ECO:0000269|PubMed:1936243}.
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 Evidence={ECO:0000250|UniProtKB:P84853};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12832768,
CC ECO:0000269|PubMed:15681236}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves (at protein level).
CC {ECO:0000269|PubMed:15681236}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Natural protein was
CC found to bind to IgE of three patients who had been working with
CC ribosome-inactivating proteins for two to three years in a research
CC laboratory setting. {ECO:0000269|PubMed:16238796}.
CC -!- MISCELLANEOUS: Possesses high antiviral potency, but relatively high
CC toxicity to normal cells in culture and to intact animals. Capable of
CC inhibiting HIV-1 infection and replication (PubMed:1936243). Allergy
CC may occur upon exposure to this protein, which needs to be taken into
CC account when considering it for therapeutic purposes (PubMed:16238796).
CC {ECO:0000269|PubMed:1936243, ECO:0000305|PubMed:16238796}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; X59260; CAA41953.1; -; mRNA.
DR PIR; S17519; S17519.
DR PDB; 1LP8; X-ray; 1.65 A; A=24-277.
DR PDB; 1LPC; X-ray; 1.70 A; A=24-277.
DR PDB; 1LPD; X-ray; 1.70 A; A=24-277.
DR PDB; 1RL0; X-ray; 1.40 A; A=24-278.
DR PDBsum; 1LP8; -.
DR PDBsum; 1LPC; -.
DR PDBsum; 1LPD; -.
DR PDBsum; 1RL0; -.
DR AlphaFoldDB; P24476; -.
DR SMR; P24476; -.
DR Allergome; 2796; Dia c RIP.
DR BRENDA; 3.2.2.22; 1925.
DR EvolutionaryTrace; P24476; -.
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 GO; GO:0050688; P:regulation of defense response to virus; 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; Antiviral protein; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Plant defense; Protein synthesis inhibitor;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1936243"
FT CHAIN 24..293
FT /note="Ribosome-inactivating protein dianthin-30"
FT /evidence="ECO:0000305|PubMed:1936243"
FT /id="PRO_0000030789"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:P20656"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 63
FT /note="A -> E (in Ref. 1; CAA41953)"
FT /evidence="ECO:0000305"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:1LP8"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:1RL0"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 109..113
FT /evidence="ECO:0007829|PDB:1RL0"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 144..150
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:1RL0"
FT TURN 175..179
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 184..197
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 199..203
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1RL0"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 232..241
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 242..244
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 247..256
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:1RL0"
FT HELIX 262..265
FT /evidence="ECO:0007829|PDB:1RL0"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:1LP8"
SQ SEQUENCE 293 AA; 32717 MW; AC85AAAC8725D4F2 CRC64;
MKIYLVAAIA WILFQSSSWT TDAATAYTLN LANPSASQYS SFLDQIRNNV RDTSLIYGGT
DVAVIGAPST TDKFLRLNFQ GPRGTVSLGL RRENLYVVAY LAMDNANVNR AYYFKNQITS
AELTALFPEV VVANQKQLEY GEDYQAIEKN AKITTGDQSR KELGLGINLL ITMIDGVNKK
VRVVKDEARF LLIAIQMTAE AARFRYIQNL VTKNFPNKFD SENKVIQFQV SWSKISTAIF
GDCKNGVFNK DYDFGFGKVR QAKDLQMGLL KYLGRPKSSS IEANSTDDTA DVL
