ID   RIP2_HORVU              Reviewed;         280 AA.
AC   P04399;
DT   20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-1987, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Protein synthesis inhibitor II;
DE            EC=3.2.2.22;
DE   AltName: Full=Ribosome-inactivating protein II;
DE   AltName: Full=rRNA N-glycosidase;
GN   Name=RIP30A;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   PROTEIN SEQUENCE, AND ACETYLATION AT ALA-1.
RA   Asano K., Svensson B., Svendsen I., Poulsen F.M., Roepstorff P.;
RT   "The complete primary structure of protein synthesis inhibitor II from
RT   barley seeds.";
RL   Carlsberg Res. Commun. 51:129-141(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 164-280.
RC   STRAIN=cv. Piggy;
RX   PubMed=1899089; DOI=10.1016/s0021-9258(18)52331-0;
RA   Leah R., Tommerup H., Svendsen I., Mundy J.;
RT   "Biochemical and molecular characterization of three barley seed proteins
RT   with antifungal properties.";
RL   J. Biol. Chem. 266:1564-1573(1991).
RN   [3]
RP   ANTIFUNGAL ACTIVITY.
RX   PubMed=3942788; DOI=10.1016/0304-4165(86)90076-0;
RA   Roberts W.K., Selitrennikoff C.P.;
RT   "Isolation and partial characterization of two antifungal proteins from
RT   barley.";
RL   Biochim. Biophys. Acta 880:161-170(1986).
CC   -!- FUNCTION: Inhibits the elongation phase of protein synthesis. It
CC       inactivates fungal ribosomes even more effectively than mammalian
CC       ribosomes and is thought to function as a constitutive antifungal agent
CC       in plants.
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   -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Starchy endosperm of mature
CC       seeds.
CC   -!- MISCELLANEOUS: Three similar RIP 30 isoforms I, II, and III have been
CC       described in Barley.
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; M62906; AAA32951.1; -; mRNA.
DR   PIR; A03373; RLBH.
DR   AlphaFoldDB; P04399; -.
DR   SMR; P04399; -.
DR   BRENDA; 3.2.2.22; 2687.
DR   ExpressionAtlas; P04399; baseline.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; 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   Acetylation; Antimicrobial; Cytoplasm; Direct protein sequencing;
KW   Fungicide; Hydrolase; Plant defense; Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..280
FT                   /note="Protein synthesis inhibitor II"
FT                   /id="PRO_0000221402"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|Ref.1"
SQ   SEQUENCE   280 AA;  29863 MW;  A5BDBE8642BF4198 CRC64;
     AAKMAKNVDK PLFTATFNVQ ASSADYATFI AGIRNKLRNP AHFSHNEPVL PPVEPNVPPS
     RWFHVVLKAS PTSAGLTLAI RADNIYLEGF KSSDGTWWEL TPGLIPGATY VGFGGTYRDL
     LGDTDKLTNV ALGRQQLEDA VTALHGRTKA DKASGPKQQQ AREAVTTLLL MVNEATRFQT
     VSGFVAGLLH PKAVEKKSGK IGNEMKAQVN GWQDLSAALL KTDVKPPPGK SPAKFTPIEK
     MGVRTAEQAA ATLGILLFVE VPGGLTVAKA LELFHASGGK