RIP1_HORVU
ID RIP1_HORVU Reviewed; 281 AA.
AC P22244;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Protein synthesis inhibitor I;
DE EC=3.2.2.22;
DE AltName: Full=Ribosome-inactivating protein I;
DE AltName: Full=rRNA N-glycosidase;
GN Name=RIP30;
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 NUCLEOTIDE SEQUENCE [MRNA].
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).
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; M62905; AAA32950.1; -; mRNA.
DR PIR; B38664; B38664.
DR PDB; 4FB9; X-ray; 1.75 A; A/B/C/D=2-281.
DR PDB; 4FBA; X-ray; 1.85 A; A/B/C/D=2-281.
DR PDB; 4FBB; X-ray; 1.80 A; A/B/C/D=2-281.
DR PDB; 4FBC; X-ray; 1.70 A; A/B/C/D=2-281.
DR PDB; 4FBH; X-ray; 2.30 A; A=1-281.
DR PDBsum; 4FB9; -.
DR PDBsum; 4FBA; -.
DR PDBsum; 4FBB; -.
DR PDBsum; 4FBC; -.
DR PDBsum; 4FBH; -.
DR AlphaFoldDB; P22244; -.
DR SMR; P22244; -.
DR ExpressionAtlas; P22244; baseline and differential.
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 3D-structure; Acetylation; Antimicrobial; Cytoplasm; Fungicide; Hydrolase;
KW Plant defense; Protein synthesis inhibitor; Toxin.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..281
FT /note="Protein synthesis inhibitor I"
FT /id="PRO_0000221401"
FT ACT_SITE 175
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 24..38
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 63..74
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:4FBC"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 125..130
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 135..146
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:4FBH"
FT HELIX 156..172
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 247..253
FT /evidence="ECO:0007829|PDB:4FBC"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:4FBC"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4FBC"
SQ SEQUENCE 281 AA; 29973 MW; DD7B49FD08EA94F8 CRC64;
MAAKMAKNVD KPLFTATFNV QASSADYATF IAGIRNKLRN PAHFSHNRPV LPPVEPNVPP
SRWFHVVLKA SPTSAGLTLA IRADNIYLEG FKSSDGTWWE LTPGLIPGAT YVGFGGTYRD
LLGDTDKLTN VALGRQQLAD AVTALHGRTK ADKPSGPKQQ QAREAVTTLL LMVNEATRFQ
TVSGFVAGLL HPKAVEKKSG KIGNEMKAQV NGWQDLSAAL LKTDVKPPPG KSPAKFAPIE
KMGVRTAVQA ANTLGILLFV EVPGGLTVAK ALELFHASGG K
