RIPA_PHYAM
ID RIPA_PHYAM Reviewed; 294 AA.
AC Q03464;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Antiviral protein alpha;
DE EC=3.2.2.22;
DE AltName: Full=PAP-alpha;
DE AltName: Full=Ribosome-inactivating protein;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
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 [GENOMIC DNA].
RC TISSUE=Leaf, Root, and Seed;
RX PubMed=1281438; DOI=10.1007/bf00027159;
RA Kataoka J., Habuka N., Masuta C., Miyano M., Koiwai A.;
RT "Isolation and analysis of a genomic clone encoding a pokeweed antiviral
RT protein.";
RL Plant Mol. Biol. 20:879-886(1992).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=7925458; DOI=10.1111/j.1432-1033.1994.00369.x;
RA Ago H., Kataoka J., Tsuge H., Hakuba N., Inagaki E., Noma M., Miyano M.;
RT "X-ray structure of a pokeweed antiviral protein, coded by a new genomic
RT clone, at 0.23-nm resolution. A model structure provides a suitable
RT electrostatic field for substrate binding.";
RL Eur. J. Biochem. 225:369-374(1994).
CC -!- FUNCTION: Inhibits viral infection of plants, and protein synthesis in
CC vitro. Has also been shown to inhibit the replication of mammalian
CC viruses. The protein may provide a means of cellular suicide upon
CC invasion by a virus.
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: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; D10600; BAA01451.1; -; Genomic_DNA.
DR PIR; S28421; S28421.
DR PDB; 1APA; X-ray; 2.30 A; A=22-285.
DR PDBsum; 1APA; -.
DR AlphaFoldDB; Q03464; -.
DR SMR; Q03464; -.
DR EvolutionaryTrace; Q03464; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; Cell wall; Disulfide bond; Hydrolase;
KW Plant defense; Protein synthesis inhibitor; Secreted; Signal; Toxin.
FT SIGNAL 1..24
FT /evidence="ECO:0000250"
FT CHAIN 25..285
FT /note="Antiviral protein alpha"
FT /id="PRO_0000030779"
FT PROPEP 286..294
FT /id="PRO_0000030780"
FT ACT_SITE 199
FT /evidence="ECO:0000250"
FT DISULFID 58..282
FT DISULFID 108..130
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 37..51
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:1APA"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 147..154
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 165..175
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 198..202
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 204..212
FT /evidence="ECO:0007829|PDB:1APA"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 222..240
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:1APA"
FT STRAND 259..264
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:1APA"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:1APA"
SQ SEQUENCE 294 AA; 33069 MW; F2EC27724FA85596 CRC64;
MKMMVVVVVM MLSWLILKPP STWAINTITF DVGNATINKY ATFMKSIHNQ AKDPTLKCYG
IPMLPNTNLT PKYLLVTLQD SSLKTITLML KRNNLYVMGY ADTYNGKCRY HIFKDISNTT
ERNDVMTTLC PNPSSRVGKN INYDSSYPAL EKKVGRPRSQ VQLGIQILNS GIGKIYGVDS
FTEKTEAEFL LVAIQMVSEA ARFKYIENQV KTNFNRAFYP NAKVLNLEES WGKISTAIHN
AKNGALTSPL ELKNANGSKW IVLRVDDIEP DVGLLKYVNG TCQATYQSAM FPHL
