RIP3_MOMCH
ID RIP3_MOMCH Reviewed; 286 AA.
AC P24817; Q41257; Q9FSH2; Q9FUV7;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2004, sequence version 2.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Ribosome-inactivating protein beta-momorcharin;
DE Short=B-MMC;
DE EC=3.2.2.22;
DE AltName: Full=MAP 30;
DE AltName: Full=rRNA N-glycosidase;
DE Flags: Precursor;
GN Name=MAP30; Synonyms=RIP;
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 [GENOMIC DNA].
RC TISSUE=Leaf;
RX PubMed=7665070; DOI=10.1016/0378-1119(95)00186-a;
RA Lee-Huang S., Huang P.L., Chen H.-C., Huang P.L., Bourinbaiar A.,
RA Huang H.I., Kung H.-F.;
RT "Anti-HIV and anti-tumor activities of recombinant MAP30 from bitter
RT melon.";
RL Gene 161:151-156(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RA Quanhong Y., Rihe P., Aisheng X.;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE OF 23-286.
RA Wei Y.-F., Cai L.-B., Zhuang W.;
RT "Cloning rip gene and identification of its resistance to Aspergillus
RT flavus.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE OF 23-286.
RA Nguyen Huy H., Nghiem Ngoc M., Dao Huy P., Le Tran B., Nong Van H.;
RT "Expression of a RIP gene from Momordica charantia in E. coli.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 24-67.
RC TISSUE=Seed;
RX PubMed=1699801; DOI=10.1016/0014-5793(90)80438-o;
RA Lee-Huang S., Huang P.L., Nara P.L., Chen H.-C., Kung H.-F., Huang P.,
RA Huang H.I., Huang P.L.;
RT "MAP 30: a new inhibitor of HIV-1 infection and replication.";
RL FEBS Lett. 272:12-18(1990).
RN [6]
RP STRUCTURE BY NMR OF 24-286, AND DNA-BINDING.
RX PubMed=10571185; DOI=10.1016/s0092-8674(00)81529-9;
RA Wang Y.-X., Neamati N., Jacob J., Palmer I., Stahl S.J., Kaufman J.D.,
RA Huang P.L., Huang P.L., Winslow H.E., Pommier Y., Wingfield P.T.,
RA Lee-Huang S., Bax A., Torchia D.A.;
RT "Solution structure of anti-HIV-1 and anti-tumor protein MAP30: structural
RT insights into its multiple functions.";
RL Cell 99:433-442(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 24-272.
RX PubMed=10329776; DOI=10.1107/s0907444999003297;
RA Yuan Y.-R., He Y.-N., Xiong J.-P., Xia Z.-X.;
RT "Three-dimensional structure of beta-momorcharin at 2.55 A resolution.";
RL Acta Crystallogr. D 55:1144-1151(1999).
CC -!- FUNCTION: Irreversibly relaxes supercoiled DNA and catalyzes double-
CC stranded breakage. Acts also as a ribosome inactivating protein.
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 -!- PTM: Bound to a branched hexasaccharide.
CC -!- MISCELLANEOUS: Possesses anti-HIV and antitumoral activities. Inhibits
CC HIV-1 integrase.
CC -!- MISCELLANEOUS: Manganese or zinc required for enhancing substrate
CC binding rather than catalysis.
CC -!- MISCELLANEOUS: The oligosaccharide does not influence the fold of the
CC polypeptide chain and probably does not play a role in the enzymatic
CC function.
CC -!- MISCELLANEOUS: Is not toxic to uninfected normal cells as it cannot
CC enter into them.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC RIP subfamily. {ECO:0000305}.
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DR EMBL; S79450; AAB35194.2; -; Genomic_DNA.
DR EMBL; AF284811; AAG33028.1; -; Genomic_DNA.
DR EMBL; AY523412; AAS17014.1; -; mRNA.
DR EMBL; AJ294541; CAC08217.1; -; Genomic_DNA.
DR PIR; B61318; B61318.
DR PIR; JC4235; JC4235.
DR PDB; 1CF5; X-ray; 2.55 A; A/B=24-272.
DR PDB; 1D8V; NMR; -; A=24-286.
DR PDBsum; 1CF5; -.
DR PDBsum; 1D8V; -.
DR AlphaFoldDB; P24817; -.
DR BMRB; P24817; -.
DR SMR; P24817; -.
DR BRENDA; 3.2.2.22; 3398.
DR EvolutionaryTrace; P24817; -.
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 GO; GO:0050688; P:regulation of defense response to virus; 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; Antiviral protein; Direct protein sequencing; Glycoprotein;
KW Hydrolase; Plant defense; Protein synthesis inhibitor; Reference proteome;
KW Signal; Toxin.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1699801"
FT CHAIN 24..286
FT /note="Ribosome-inactivating protein beta-momorcharin"
FT /id="PRO_0000030773"
FT ACT_SITE 93
FT /evidence="ECO:0000250"
FT ACT_SITE 132
FT /evidence="ECO:0000250"
FT ACT_SITE 181
FT /evidence="ECO:0000250"
FT ACT_SITE 184
FT /evidence="ECO:0000250"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT CONFLICT 23
FT /note="G -> M (in Ref. 3 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="Y -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="S -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="D -> E (in Ref. 4; CAC08217)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="I -> T (in Ref. 1; AAB35194)"
FT /evidence="ECO:0000305"
FT CONFLICT 228
FT /note="G -> A (in Ref. 4; CAC08217)"
FT /evidence="ECO:0000305"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 111..116
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 150..161
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 168..177
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 180..184
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 186..194
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 211..214
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 223..228
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 229..237
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:1D8V"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1CF5"
FT HELIX 252..256
FT /evidence="ECO:0007829|PDB:1CF5"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:1D8V"
FT HELIX 264..269
FT /evidence="ECO:0007829|PDB:1CF5"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1D8V"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:1D8V"
SQ SEQUENCE 286 AA; 32031 MW; 6B2DF55A41D8F921 CRC64;
MVKCLLLSFL IIAIFIGVPT AKGDVNFDLS TATAKTYTKF IEDFRATLPF SHKVYDIPLL
YSTISDSRRF ILLNLTSYAY ETISVAIDVT NVYVVAYRTR DVSYFFKESP PEAYNILFKG
TRKITLPYTG NYENLQTAAH KIRENIDLGL PALSSAITTL FYYNAQSAPS ALLVLIQTTA
EAARFKYIER HVAKYVATNF KPNLAIISLE NQWSALSKQI FLAQNQGGKF RNPVDLIKPT
GERFQVTNVD SDVVKGNIKL LLNSRASTAD ENFITTMTLL GESVVN
