ID   RIP1_LUFAE              Reviewed;          47 AA.
AC   P56568; Q8GRS9;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   04-NOV-2026, entry version 66.
DE   RecName: Full=Ribosome-inactivating protein luffin P1;
DE            EC=3.2.2.22;
DE   AltName: Full=Arginine/glutamate-rich polypeptide;
DE            Short=AGRP;
DE   Contains:
DE     RecName: Full=Luffin P1a;
DE   Contains:
DE     RecName: Full=Luffin P1b;
DE   Contains:
DE     RecName: Full=Luffin P1c;
OS   Luffa aegyptiaca (Sponge gourd) (Luffa cylindrica).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Sicyoeae; Luffa.
OX   NCBI_TaxID=3670;
RN   [1]
RP   PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=9214759; DOI=10.1271/bbb.61.984;
RA   Kimura M., Park S.-S., Sakai R., Yamasaki N., Funatsu G.;
RT   "Primary structure of 6.5k-arginine/glutamate-rich polypeptide from the
RT   seeds of sponge gourd (Luffa cylindrica).";
RL   Biosci. Biotechnol. Biochem. 61:984-988(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 5-45, PROTEIN SEQUENCE OF 3-13, FUNCTION,
RP   CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   TISSUE=Seed;
RX   PubMed=12948831; DOI=10.1016/s0196-9781(03)00173-6;
RA   Li F., Yang X.-X., Xia H.-C., Zeng R., Hu W.-G., Li Z., Zhang Z.-C.;
RT   "Purification and characterization of Luffin P1, a ribosome-inactivating
RT   peptide from the seeds of Luffa cylindrica.";
RL   Peptides 24:799-805(2003).
CC   -!- FUNCTION: Inhibits protein synthesis in animal cells.
CC       {ECO:0000269|PubMed:12948831}.
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:12948831};
CC   -!- SUBUNIT: Homotetramer.
CC   -!- MASS SPECTROMETRY: [Luffin P1a]: Mass=5693.39; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:9214759};
CC   -!- MASS SPECTROMETRY: [Luffin P1c]: Mass=5226.1; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:12948831};
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DR   EMBL; AF537345; AAN06821.1; -; mRNA.
DR   EMBL; AY135368; AAN10153.1; -; mRNA.
DR   PIR; JC5557; JC5557.
DR   PDB; 2L37; NMR; -; A=3-45.
DR   PDB; 6O3S; NMR; -; A=1-47.
DR   AlphaFoldDB; P56568; -.
DR   SMR; P56568; -.
DR   EvolutionaryTrace; P56568; -.
DR   GO; GO:0030598; F:rRNA N-glycosylase activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IDA:UniProtKB.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
DR   Gene3D; 6.10.250.890; -; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Disulfide bond; Glycosidase;
KW   Hydrolase; Plant defense; Protein synthesis inhibitor; Toxin.
FT   PEPTIDE         1..47
FT                   /note="Luffin P1a"
FT                   /id="PRO_0000032204"
FT   PEPTIDE         1..45
FT                   /note="Luffin P1b"
FT                   /id="PRO_0000032205"
FT   PEPTIDE         3..45
FT                   /note="Luffin P1c"
FT                   /id="PRO_0000032206"
FT   SITE            2..3
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   SITE            45..46
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000305"
FT   DISULFID        12..33
FT   DISULFID        16..29
FT   HELIX           6..19
FT                   /evidence="ECO:0007829|PDB:2L37"
FT   HELIX           24..41
FT                   /evidence="ECO:0007829|PDB:2L37"
SQ   SEQUENCE   47 AA;  5698 MW;  588B0EC82273AC05 CRC64;
     PRGSPRTEYE ACRVRCQVAE HGVERQRRCQ QVCEKRLRER EGRREVD
//