RIP1_LUFAE
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 25-MAY-2022, entry version 62.
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 PDBsum; 2L37; -.
DR PDBsum; 6O3S; -.
DR AlphaFoldDB; P56568; -.
DR SMR; P56568; -.
DR EvolutionaryTrace; P56568; -.
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; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
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
