ID   RIPS_PHYAM              Reviewed;         261 AA.
AC   P23339;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Antiviral protein S;
DE            EC=3.2.2.22;
DE   AltName: Full=PAP-S;
DE   AltName: Full=Ribosome-inactivating protein;
DE   AltName: Full=rRNA N-glycosidase;
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   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=1368643; DOI=10.1271/bbb1961.54.3301;
RA   Kung S.S., Kimura M., Funatsu G.;
RT   "The complete amino acid sequence of antiviral protein from the seeds of
RT   pokeweed (Phytolacca americana).";
RL   Agric. Biol. Chem. 54:3301-3318(1990).
CC   -!- FUNCTION: Inhibits viral infection of plants, and protein synthesis in
CC       vitro.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   PIR; JE0401; JE0401.
DR   PDB; 1GIK; X-ray; 1.80 A; A=1-261.
DR   PDB; 1J1Q; X-ray; 1.80 A; A=1-261.
DR   PDB; 1J1R; X-ray; 1.90 A; A=1-261.
DR   PDB; 1J1S; X-ray; 2.00 A; A=1-261.
DR   PDBsum; 1GIK; -.
DR   PDBsum; 1J1Q; -.
DR   PDBsum; 1J1R; -.
DR   PDBsum; 1J1S; -.
DR   AlphaFoldDB; P23339; -.
DR   SMR; P23339; -.
DR   EvolutionaryTrace; P23339; -.
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; Toxin.
FT   CHAIN           1..261
FT                   /note="Antiviral protein S"
FT                   /id="PRO_0000221415"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..258
FT                   /evidence="ECO:0000269|PubMed:1368643"
FT   DISULFID        84..105
FT                   /evidence="ECO:0000269|PubMed:1368643"
FT   STRAND          3..10
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           13..27
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          34..36
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:1J1Q"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   TURN            68..70
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          73..80
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          83..88
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           95..104
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:1J1Q"
FT   HELIX           122..129
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           134..136
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           141..151
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           159..172
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           174..178
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           180..188
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           198..205
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           207..215
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           218..220
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          221..229
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   STRAND          235..240
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:1GIK"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:1J1Q"
SQ   SEQUENCE   261 AA;  29200 MW;  D88B99962FE8399D CRC64;
     INTITFDAGN ATINKYATFM ESLRNEAKDP SLKCYGIPML PNTNSTIKYL LVKLQGASLK
     TITLMLRRNN LYVMGYSDPY DNKCRYHIFN DIKGTEYSDV ENTLCPSSNP RVAKPINYNG
     LYPTLEKKAG VTSRNEVQLG IQILSSDIGK ISGQGSFTEK IEAKFLLVAI QMVSEAARFK
     YIENQVKTNF NRDFSPNDKV LDLEENWGKI STAIHNSKNG ALPKPLELKN ADGTKWIVLR
     VDEIKPDVGL LNYVNGTCQA T