RIP1_PHYAM
ID RIP1_PHYAM Reviewed; 313 AA.
AC P10297;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Antiviral protein I;
DE EC=3.2.2.22 {ECO:0000269|PubMed:10403789, ECO:0000269|PubMed:10595542, ECO:0000269|PubMed:2930487};
DE AltName: Full=PAP-C {ECO:0000303|PubMed:2930487};
DE AltName: Full=PAP-I {ECO:0000303|PubMed:10403789};
DE AltName: Full=PAP-R {ECO:0000303|PubMed:2248976};
DE AltName: Full=Ribosome-inactivating protein;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
GN Name=PAP1;
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 PROTEIN SEQUENCE OF 23-62.
RC TISSUE=Leaf;
RX PubMed=1912488; DOI=10.1007/bf00037047;
RA Lin Q., Chen Z.C., Antoniw J.F., White R.F.;
RT "Isolation and characterization of a cDNA clone encoding the anti-viral
RT protein from Phytolacca americana.";
RL Plant Mol. Biol. 17:609-614(1991).
RN [2]
RP PROTEIN SEQUENCE OF 23-65, FUNCTION, CATALYTIC ACTIVITY, AND TOXIC DOSE.
RC TISSUE=Leaf {ECO:0000303|PubMed:2930487};
RX PubMed=2930487; DOI=10.1042/bj2570801;
RA Barbieri L., Bolognesi A., Cenini P., Falasca A.I., Minghetti A.,
RA Garofano L., Guicciardi A., Lappi D., Miller S.P.;
RT "Ribosome-inactivating proteins from plant cells in culture.";
RL Biochem. J. 257:801-807(1989).
RN [3]
RP PROTEIN SEQUENCE OF 23-54.
RC TISSUE=Leaf;
RX PubMed=6885760; DOI=10.1016/s0021-9258(17)44535-2;
RA Houston L.L., Ramakrishnan S., Hermodson M.A.;
RT "Seasonal variations in different forms of pokeweed antiviral protein, a
RT potent inactivator of ribosomes.";
RL J. Biol. Chem. 258:9601-9604(1983).
RN [4]
RP PROTEIN SEQUENCE OF 23-54, AND FUNCTION.
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 [5]
RP PROTEIN SEQUENCE OF 23-54, FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Root {ECO:0000303|PubMed:2248976};
RX PubMed=2248976; DOI=10.1016/0167-4781(90)90002-j;
RA Bolognesi A., Barbieri L., Abbondanza A., Falasca A.I., Carnicelli D.,
RA Battelli M.G., Stirpe F.;
RT "Purification and properties of new ribosome-inactivating proteins with RNA
RT N-glycosidase activity.";
RL Biochim. Biophys. Acta 1087:293-302(1990).
RN [6]
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 [7] {ECO:0007744|PDB:1PAF, ECO:0007744|PDB:1PAG}
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-284 AND IN COMPLEX WITH
RP SUBSTRATE ANALOG.
RX PubMed=8411176; DOI=10.1006/jmbi.1993.1547;
RA Monzingo A.F., Collins E.J., Ernst S.R., Irvin J.D., Robertus J.D.;
RT "The 2.5 A structure of pokeweed antiviral protein.";
RL J. Mol. Biol. 233:705-715(1993).
RN [8] {ECO:0007744|PDB:1QCG, ECO:0007744|PDB:1QCI, ECO:0007744|PDB:1QCJ}
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 23-284 AND IN COMPLEX WITH ADENINE
RP AND INHIBITOR.
RX PubMed=10493577; DOI=10.1110/ps.8.9.1765;
RA Kurinov I.V., Myers D.E., Irvin J.D., Uckun F.M.;
RT "X-ray crystallographic analysis of the structural basis for the
RT interactions of pokeweed antiviral protein with its active site inhibitor
RT and ribosomal RNA substrate analogs.";
RL Protein Sci. 8:1765-1772(1999).
RN [9] {ECO:0007744|PDB:1D6A}
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-284 IN COMPLEX WITH GUANINE,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, TISSUE SPECIFICITY, AND DISULFIDE
RP BONDS.
RX PubMed=10595542; DOI=10.1110/ps.8.11.2399;
RA Kurinov I.V., Rajamohan F., Venkatachalam T.K., Uckun F.M.;
RT "X-ray crystallographic analysis of the structural basis for the
RT interaction of pokeweed antiviral protein with guanine residues of
RT ribosomal RNA.";
RL Protein Sci. 8:2399-2405(1999).
CC -!- FUNCTION: Possesses antiviral potency. Inhibits viral infection of
CC plants (tobacco mosaic virus) (PubMed:10403789). Inhibits protein
CC synthesis (PubMed:2930487, PubMed:6091760, PubMed:2248976,
CC PubMed:10403789, PubMed:10595542). Releases both adenine and guanine
CC from Escherichia coli rRNA in vitro. Activity on guanine is 20 times
CC slower than that on adenine (PubMed:10595542).
CC {ECO:0000269|PubMed:10403789, ECO:0000269|PubMed:10595542,
CC ECO:0000269|PubMed:2248976, ECO:0000269|PubMed:2930487,
CC ECO:0000269|PubMed:6091760}.
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, ECO:0000269|PubMed:10595542,
CC ECO:0000269|PubMed:2930487};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10595542}.
CC -!- TISSUE SPECIFICITY: Expressed in spring leaves (at protein level)
CC (PubMed:10403789, PubMed:10595542). Expressed in roots (at protein
CC level) (PubMed:2248976). {ECO:0000269|PubMed:10595542,
CC ECO:0000269|PubMed:2248976}.
CC -!- TOXIC DOSE: LD(50) is 1.89 mg/kg by intraperitoneal injection into mice
CC (at 48 hours post-injection). {ECO:0000269|PubMed:2930487}.
CC -!- TOXIC DOSE: LD(50) is 0.95 mg/kg by intraperitoneal injection into mice
CC (at 14 days post-injection). {ECO:0000269|PubMed:2930487}.
CC -!- MISCELLANEOUS: Depurinates genomic RNA of immunodeficiency virus type-I
CC (HIV-I) and bacteriophage (MS 2) RNA. Inhibits the replication of HIV-1
CC in human peripheral blood mononuclear cells with IC(50) value of 14 nM.
CC {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; X55383; CAA39054.1; -; mRNA.
DR PIR; S17757; S17757.
DR PDB; 1D6A; X-ray; 2.10 A; A/B=23-284.
DR PDB; 1PAF; X-ray; 2.50 A; A/B=23-284.
DR PDB; 1PAG; X-ray; 2.80 A; A/B=23-284.
DR PDB; 1QCG; X-ray; 2.10 A; A/B=23-284.
DR PDB; 1QCI; X-ray; 2.00 A; A/B=23-284.
DR PDB; 1QCJ; X-ray; 2.10 A; A/B=23-284.
DR PDBsum; 1D6A; -.
DR PDBsum; 1PAF; -.
DR PDBsum; 1PAG; -.
DR PDBsum; 1QCG; -.
DR PDBsum; 1QCI; -.
DR PDBsum; 1QCJ; -.
DR AlphaFoldDB; P10297; -.
DR SMR; P10297; -.
DR BRENDA; 3.2.2.22; 4806.
DR EvolutionaryTrace; P10297; -.
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 InterPro; IPR016331; Shiga-like_toxin_subunit_A.
DR PANTHER; PTHR33453; PTHR33453; 1.
DR Pfam; PF00161; RIP; 1.
DR PIRSF; PIRSF001924; Shigella_toxin_subunit_A; 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..22
FT /evidence="ECO:0000269|PubMed:1912488,
FT ECO:0000269|PubMed:2248976, ECO:0000269|PubMed:2930487,
FT ECO:0000269|PubMed:6091760, ECO:0000269|PubMed:6885760"
FT CHAIN 23..285
FT /note="Antiviral protein I"
FT /id="PRO_0000030781"
FT PROPEP 286..313
FT /id="PRO_0000030782"
FT ACT_SITE 94
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 145
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 198
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT ACT_SITE 201
FT /evidence="ECO:0000250|UniProtKB:P84531"
FT BINDING 95
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10493577,
FT ECO:0000269|PubMed:10595542, ECO:0000269|PubMed:8411176,
FT ECO:0007744|PDB:1D6A, ECO:0007744|PDB:1PAG,
FT ECO:0007744|PDB:1QCI, ECO:0007744|PDB:1QCJ"
FT BINDING 143
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10493577,
FT ECO:0000269|PubMed:10595542, ECO:0000269|PubMed:8411176,
FT ECO:0007744|PDB:1D6A, ECO:0007744|PDB:1PAG,
FT ECO:0007744|PDB:1QCJ"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10493577,
FT ECO:0007744|PDB:1QCJ"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:10493577,
FT ECO:0000269|PubMed:10595542, ECO:0000269|PubMed:8411176,
FT ECO:0007744|PDB:1D6A, ECO:0007744|PDB:1PAG,
FT ECO:0007744|PDB:1QCI"
FT DISULFID 56..281
FT /evidence="ECO:0000269|PubMed:10595542,
FT ECO:0007744|PDB:1D6A"
FT DISULFID 107..128
FT /evidence="ECO:0000269|PubMed:10595542,
FT ECO:0007744|PDB:1D6A"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 35..49
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:1D6A"
FT STRAND 83..89
FT /evidence="ECO:0007829|PDB:1QCI"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:1QCI"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:1QCI"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:1PAF"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 164..174
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 182..201
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:1QCI"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 221..239
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 244..252
FT /evidence="ECO:0007829|PDB:1QCI"
FT STRAND 258..263
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:1QCI"
FT HELIX 268..270
FT /evidence="ECO:0007829|PDB:1QCI"
SQ SEQUENCE 313 AA; 35219 MW; 2C57B2861EBA57F5 CRC64;
MKSMLVVTIS IWLILAPTST WAVNTIIYNV GSTTISKYAT FLNDLRNEAK DPSLKCYGIP
MLPNTNTNPK YVLVELQGSN KKTITLMLRR NNLYVMGYSD PFETNKCRYH IFNDISGTER
QDVETTLCPN ANSRVSKNIN FDSRYPTLES KAGVKSRSQV QLGIQILDSN IGKISGVMSF
TEKTEAEFLL VAIQMVSEAA RFKYIENQVK TNFNRAFNPN PKVLNLQETW GKISTAIHDA
KNGVLPKPLE LVDASGAKWI VLRVDEIKPD VALLNYVGGS CQTTYNQNAM FPQLIMSTYY
NYMVNLGDLF EGF
