RIP2_PHYAM
ID RIP2_PHYAM Reviewed; 310 AA.
AC Q40772;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Antiviral protein II/III {ECO:0000305};
DE EC=3.2.2.22 {ECO:0000269|PubMed:10403789};
DE AltName: Full=Antiviral protein II {ECO:0000303|PubMed:10403789, ECO:0000303|PubMed:8034016};
DE AltName: Full=Antiviral protein III {ECO:0000303|PubMed:10403789, ECO:0000303|PubMed:12754107};
DE AltName: Full=PAP-II {ECO:0000303|PubMed:10403789, ECO:0000303|PubMed:8034016};
DE AltName: Full=PAP-III {ECO:0000303|PubMed:10403789, ECO:0000303|PubMed:12754107};
DE AltName: Full=Ribosome-inactivating protein;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
GN Name=PAP2; Synonyms=PAPII;
OS Phytolacca americana (American pokeweed) (Phytolacca decandra).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Phytolaccaceae; Phytolacca.
OX NCBI_TaxID=3527;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Leaf {ECO:0000303|PubMed:8034016};
RX PubMed=8034016; DOI=10.1016/0014-5793(94)00565-6;
RA Poyet J.-L., Radom J., Hoeveler A.;
RT "Isolation and characterization of a cDNA clone encoding the pokeweed
RT antiviral protein II from Phytolacca americana and its expression in E.
RT coli.";
RL FEBS Lett. 347:268-272(1994).
RN [2]
RP PROTEIN SEQUENCE OF 26-55.
RC TISSUE=Leaf;
RX PubMed=6091760; DOI=10.1016/0167-4838(84)90219-x;
RA Bjorn M.J., Larrick J., Piatak M., Wilson K.J.;
RT "Characterization of translational inhibitors from Phytolacca americana.
RT Amino-terminal sequence determination and antibody-inhibitor conjugates.";
RL Biochim. Biophys. Acta 790:154-163(1984).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND MISCELLANEOUS.
RX PubMed=10403789; DOI=10.1006/bbrc.1999.0922;
RA Rajamohan F., Venkatachalam T.K., Irvin J.D., Uckun F.M.;
RT "Pokeweed antiviral protein isoforms PAP-I, PAP-II, and PAP-III depurinate
RT RNA of human immunodeficiency virus (HIV)-1.";
RL Biochem. Biophys. Res. Commun. 260:453-458(1999).
RN [4] {ECO:0007744|PDB:1LLN}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 26-287 OF PAP-III, TISSUE
RP SPECIFICITY, DISULFIDE BONDS, AND REACTION MECHANISM.
RX PubMed=12754107; DOI=10.1016/s0006-2952(03)00144-8;
RA Kurinov I.V., Uckun F.M.;
RT "High resolution X-ray structure of potent anti-HIV pokeweed antiviral
RT protein-III.";
RL Biochem. Pharmacol. 65:1709-1717(2003).
CC -!- FUNCTION: Possesses antiviral potency. Inhibits viral infection of
CC plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein
CC synthesis in both prokaryotes and eukaryotes (PubMed:8034016,
CC PubMed:10403789). {ECO:0000269|PubMed:10403789,
CC ECO:0000269|PubMed:8034016}.
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:0000269|PubMed:10403789};
CC -!- TISSUE SPECIFICITY: PAP-II is expressed in early summer leaves (at
CC protein level) (PubMed:10403789). PAP-III is expressed in late summer
CC leaves (at protein level) (PubMed:10403789, PubMed:12754107).
CC {ECO:0000269|PubMed:10403789, ECO:0000269|PubMed:12754107}.
CC -!- DEVELOPMENTAL STAGE: Expressed progressively with the aging of the
CC plant.
CC -!- MISCELLANEOUS: 2 forms exist, PAP-II and PAP-III, that differ in their
CC seasonal expression and chromatographic profiles. Both depurinate
CC genomic RNA of immunodeficiency virus type-I (HIV-I) and bacteriophage
CC (MS 2) RNA. PAP-II and PAP-III inhibit the replication of HIV-1 in
CC human peripheral blood mononuclear cells with IC(50) values of 26 nM
CC and 17 nM, respectively. {ECO:0000269|PubMed:10403789}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; X78628; CAA55342.1; -; mRNA.
DR PIR; S32610; S32610.
DR PIR; S46239; S46239.
DR PDB; 1LLN; X-ray; 1.60 A; A=26-287.
DR PDBsum; 1LLN; -.
DR AlphaFoldDB; Q40772; -.
DR SMR; Q40772; -.
DR BRENDA; 3.2.2.22; 4806.
DR EvolutionaryTrace; Q40772; -.
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:0051607; P:defense response to virus; 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; Antiviral defense; Direct protein sequencing; Disulfide bond;
KW Hydrolase; Plant defense; Protein synthesis inhibitor; Signal; Toxin.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:6091760"
FT CHAIN 26..?
FT /note="Antiviral protein II/III"
FT /id="PRO_0000030783"
FT PROPEP ?..310
FT /id="PRO_0000030784"
FT ACT_SITE 94
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 142
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 197
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 200
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT DISULFID 57..284
FT /evidence="ECO:0000269|PubMed:12754107,
FT ECO:0007744|PDB:1LLN"
FT DISULFID 106..123
FT /evidence="ECO:0000269|PubMed:12754107,
FT ECO:0007744|PDB:1LLN"
FT STRAND 27..31
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 36..50
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 161..167
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 180..200
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 204..206
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 231..235
FT /evidence="ECO:0007829|PDB:1LLN"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1LLN"
FT HELIX 268..273
FT /evidence="ECO:0007829|PDB:1LLN"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1LLN"
SQ SEQUENCE 310 AA; 34694 MW; 4D3BB001D7259D9F CRC64;
MKMKVLEVVG LAISIWLMLT PPASSNIVFD VENATPETYS NFLTSLREAV KDKKLTCHGM
IMATTLTEQP KYVLVDLKFG SGTFTLAIRR GNLYLEGYSD IYNGKCRYRI FKDSESDAQE
TVCPGDKSKP GTQNNIPYEK SYKGMESKGG ARTKLGLGKI TLKSRMGKIY GKDATDQKQY
QKNEAEFLLI AVQMVTEASR FKYIENKVKA KFDDANGYQP DPKAISLEKN WDSVSKVIAK
VGTSGDSTVT LPGDLKDENN KPWTTATMND LKNDIMALLT HVTCKVKSSM FPEIMSYYYR
TSISNLGEFE
