ID   RIP4_PHYHE              Reviewed;         312 AA.
AC   Q6EH50;
DT   14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=Heterotepalin-4 {ECO:0000303|PubMed:17258249};
DE            EC=3.2.2.22;
DE   AltName: Full=Ribosome-inactivating protein {ECO:0000250|UniProtKB:P10297};
DE   AltName: Full=rRNA N-glycosidase {ECO:0000250|UniProtKB:P10297};
DE   Flags: Precursor;
GN   Name=RIP1 {ECO:0000312|EMBL:AAQ95991.1};
OS   Phytolacca heterotepala (Mexican pokeweed).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Phytolaccaceae; Phytolacca.
OX   NCBI_TaxID=248308;
RN   [1] {ECO:0000312|EMBL:AAQ95991.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Delli Bovi P., Corrado G.;
RL   Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 23-37; 38-46; 71-81; 91-106; 109-120; 145-151; 158-173;
RP   174-183; 203-209; 222-231; 232-240; 247-257 AND 262-283, FUNCTION,
RP   CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   TISSUE=Leaf {ECO:0000269|PubMed:17258249};
RX   PubMed=17258249; DOI=10.1016/j.phytochem.2006.12.002;
RA   Di Maro A., Chambery A., Daniele A., Casoria P., Parente A.;
RT   "Isolation and characterization of heterotepalins, type 1 ribosome-
RT   inactivating proteins from Phytolacca heterotepala leaves.";
RL   Phytochemistry 68:767-776(2007).
CC   -!- FUNCTION: Inhibits protein synthesis in vitro.
CC       {ECO:0000269|PubMed:17258249}.
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:17258249};
CC   -!- MASS SPECTROMETRY: Mass=29326; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17258249};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000255}.
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DR   EMBL; AY327475; AAQ95991.1; -; mRNA.
DR   AlphaFoldDB; Q6EH50; -.
DR   SMR; Q6EH50; -.
DR   GO; GO:0016787; F:hydrolase activity; IDA:UniProtKB.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
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; IDA:UniProtKB.
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; 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.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:17258249"
FT   CHAIN           23..283
FT                   /note="Heterotepalin-4"
FT                   /evidence="ECO:0000269|PubMed:17258249"
FT                   /id="PRO_0000352792"
FT   PROPEP          284..312
FT                   /evidence="ECO:0000269|PubMed:17258249"
FT                   /id="PRO_0000352793"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000250|UniProtKB:P20656"
FT   DISULFID        56..280
FT                   /evidence="ECO:0000250|UniProtKB:P10297"
FT   DISULFID        107..128
FT                   /evidence="ECO:0000250|UniProtKB:P10297"
FT   CONFLICT        266
FT                   /note="I -> M (in Ref. 1; AAQ95991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   312 AA;  35153 MW;  4C55B0D9FB8F189B CRC64;
     MKSMLVVTIS VWLILAPTST WAVNTIIYNV GSTTISKYAT FLDDLRNEAK DPNLKCYGIP
     MLPNTNSNPK YVLVELQGSN KKTITLMLRR NNLYVMGYSD PFDTSKCRYH IFNDISGTER
     QDVETTLCPN SNSRVSKNIN YDSRYPTLES KVGVKSRSQV QLGIQILDSD IGKISGVTSF
     SEKTEAEFLL VAIQISEAAR FKYIENQVKT NFNRAFNPNP KVLNLEETWG KISTAIHDAK
     NGVLPKPLEL VDASGAKWIV LRVDEIKPDV ALLNYVSGSC QTTYNQNAMF PQLIMSTYYN
     YMANLGDLFE EF