RIP1_MOMCH
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 25-MAY-2022, entry version 118.
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; 898359at2759; -.
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; -; 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; 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
