ID RIP1_MOMCH Reviewed; 286 AA. AC P16094; P24697; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-1992, sequence version 2. DT 27-MAR-2024, entry version 121. DE RecName: Full=Ribosome-inactivating protein momordin I; DE EC=3.2.2.22; DE AltName: Full=Alpha-momorcharin; DE Short=Alpha-MMC; DE AltName: Full=rRNA N-glycosidase; DE Flags: Precursor; OS Momordica charantia (Bitter gourd) (Balsam pear). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica. OX NCBI_TaxID=3673; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Seed; RX PubMed=2001404; DOI=10.1016/0167-4781(91)90070-3; RA Ho W.K.K., Liu S.C., Shaw P.C., Yeung H.W., Ng T.B., Chan W.Y.; RT "Cloning of the cDNA of alpha-momorcharin: a ribosome inactivating RT protein."; RL Biochim. Biophys. Acta 1088:311-314(1991). RN [2] RP PROTEIN SEQUENCE OF 24-38. RC TISSUE=Seed; RX PubMed=2753596; DOI=10.1111/j.1399-3011.1989.tb01280.x; RA Montecucchi P.-C., Lazzarini A.M., Barbieri L., Stirpe F., Soria M., RA Lappi D.; RT "N-terminal sequence of some ribosome-inactivating proteins."; RL Int. J. Pept. Protein Res. 33:263-267(1989). RN [3] RP PROTEIN SEQUENCE OF 24-70. RC TISSUE=Seed; RX PubMed=3262509; DOI=10.1111/j.1432-1033.1988.tb14317.x; RA Casellas P., Dussossoy D., Falasca A.I., Barbieri L., Guillemot J.-C., RA Ferrara P., Bolognesi A., Cenini P., Stirpe F.; RT "Trichokirin, a ribosome-inactivating protein from the seeds of RT Trichosanthes kirilowii Maximowicz. Purification, partial characterization RT and use for preparation of immunotoxins."; RL Eur. J. Biochem. 176:581-588(1988). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=8075985; DOI=10.1016/s0969-2126(00)00004-6; RA Ren J., Wang Y., Dong Y., Stuart D.I.; RT "The N-glycosidase mechanism of ribosome-inactivating proteins implied by RT crystal structures of alpha-momorcharin."; RL Structure 2:7-16(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.16 ANGSTROMS). RX PubMed=8143869; DOI=10.1016/0014-5793(94)80491-5; RA Husain J., Tickle I.J., Wood S.P.; RT "Crystal structure of momordin, a type I ribosome inactivating protein from RT the seeds of Momordica charantia."; RL FEBS Lett. 342:154-158(1994). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=7619070; DOI=10.1042/bj3090285; RA Huang Q., Liu S., Tang Y., Jin S., Wang Y.; RT "Studies on crystal structures, active-centre geometry and depurinating RT mechanism of two ribosome-inactivating proteins."; RL Biochem. J. 309:285-298(1995). 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 -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1 CC RIP subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X57682; CAA40869.1; -; mRNA. DR PIR; S14273; RLPUGG. DR PDB; 1AHA; X-ray; 2.20 A; A=24-269. DR PDB; 1AHB; X-ray; 2.20 A; A=24-269. DR PDB; 1AHC; X-ray; 2.00 A; A=24-269. DR PDB; 1F8Q; X-ray; 2.20 A; A=24-286. DR PDB; 1MOM; X-ray; 2.16 A; A=24-269. DR PDB; 1MRG; X-ray; 1.80 A; A=24-286. DR PDB; 1MRH; X-ray; 2.00 A; A=24-286. DR PDB; 1MRI; X-ray; 2.20 A; A=24-286. DR PDB; 4YP2; X-ray; 1.35 A; B=24-269. DR PDB; 5CF9; X-ray; 1.52 A; B=24-269. DR PDB; 6LOQ; X-ray; 1.33 A; A=1-286. DR PDB; 6LOR; X-ray; 1.35 A; A=1-286. DR PDB; 6LOV; X-ray; 1.35 A; A=1-286. DR PDB; 6LOW; X-ray; 1.39 A; A=1-286. DR PDB; 6LOY; X-ray; 1.35 A; A=1-286. DR PDB; 6LOZ; X-ray; 1.08 A; A=1-286. DR PDB; 6LP0; X-ray; 1.52 A; A=1-286. DR PDBsum; 1AHA; -. DR PDBsum; 1AHB; -. DR PDBsum; 1AHC; -. DR PDBsum; 1F8Q; -. DR PDBsum; 1MOM; -. DR PDBsum; 1MRG; -. DR PDBsum; 1MRH; -. DR PDBsum; 1MRI; -. DR PDBsum; 4YP2; -. DR PDBsum; 5CF9; -. DR PDBsum; 6LOQ; -. DR PDBsum; 6LOR; -. DR PDBsum; 6LOV; -. DR PDBsum; 6LOW; -. DR PDBsum; 6LOY; -. DR PDBsum; 6LOZ; -. DR PDBsum; 6LP0; -. DR AlphaFoldDB; P16094; -. DR SMR; P16094; -. DR Allergome; 2800; Mom c RIP. DR GlyConnect; 535; 3 N-Linked glycans (1 site). DR OrthoDB; 524353at2759; -. DR BRENDA; 3.2.2.22; 3398. DR EvolutionaryTrace; P16094; -. DR Proteomes; UP000504603; Unplaced. 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:0006952; P:defense response; IEA:UniProtKB-KW. DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW. DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1. DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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; -; 1. DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00161; RIP; 1. DR PRINTS; PR00396; SHIGARICIN. DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1. DR PROSITE; PS00275; SHIGA_RICIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycoprotein; Hydrolase; KW Plant defense; Protein synthesis inhibitor; Reference proteome; Signal; KW Toxin. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:2753596, FT ECO:0000269|PubMed:3262509" FT CHAIN 24..269 FT /note="Ribosome-inactivating protein momordin I" FT /id="PRO_0000030770" FT PROPEP 270..286 FT /note="Removed in mature form" FT /id="PRO_0000030771" FT ACT_SITE 183 FT CARBOHYD 250 FT /note="N-linked (GlcNAc...) asparagine" FT /id="CAR_000082" FT STRAND 25..29 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 34..46 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 57..60 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 66..69 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 70..76 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 82..88 FT /evidence="ECO:0007829|PDB:6LOZ" FT TURN 89..91 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 109..114 FT /evidence="ECO:0007829|PDB:6LOZ" FT TURN 115..117 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 134..141 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 152..162 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 167..180 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 182..186 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 188..196 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 206..225 FT /evidence="ECO:0007829|PDB:6LOZ" FT TURN 226..230 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 231..239 FT /evidence="ECO:0007829|PDB:6LOZ" FT STRAND 242..244 FT /evidence="ECO:0007829|PDB:1MRG" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 254..257 FT /evidence="ECO:0007829|PDB:6LOZ" FT HELIX 266..268 FT /evidence="ECO:0007829|PDB:6LOQ" SQ SEQUENCE 286 AA; 31532 MW; E1B013ABEBC216CF CRC64; MSRFSVLSFL ILAIFLGGSI VKGDVSFRLS GADPRSYGMF IKDLRNALPF REKVYNIPLL LPSVSGAGRY LLMHLFNYDG KTITVAVDVT NVYIMGYLAD TTSYFFNEPA AELASQYVFR DARRKITLPY SGNYERLQIA AGKPREKIPI GLPALDSAIS TLLHYDSTAA AGALLVLIQT TAEAARFKYI EQQIQERAYR DEVPSLATIS LENSWSGLSK QIQLAQGNNG IFRTPIVLVD NKGNRVQITN VTSKVVTSNI QLLLNTRNIA EGDNGDVSTT HGFSSY //