ID   RIPP_MIRJA              Reviewed;         278 AA.
AC   P21326;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 2.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Antiviral protein MAP;
DE            EC=3.2.2.22;
DE   AltName: Full=MAP-S;
DE   AltName: Full=Ribosome-inactivating protein;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Precursor;
OS   Mirabilis jalapa (Garden four-o'clock).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Nyctaginaceae; Mirabilis.
OX   NCBI_TaxID=3538;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2022657; DOI=10.1016/s0021-9258(18)92992-3;
RA   Kataoka J., Habuka N., Furuno M., Miyano M., Takanami Y., Koiwai A.;
RT   "DNA sequence of Mirabilis antiviral protein (MAP), a ribosome-inactivating
RT   protein with an antiviral property, from mirabilis jalapa L. and its
RT   expression in Escherichia coli.";
RL   J. Biol. Chem. 266:8426-8430(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8451171; DOI=10.1093/nar/21.4.1035;
RA   Kataoka J., Miyano M., Habuka N., Masuta C., Koiwai A.;
RT   "A genomic gene for MAP, a ribosome-inactivating protein from Mirabilis
RT   jalapa, contains an intron.";
RL   Nucleic Acids Res. 21:1035-1035(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 29-278.
RX   PubMed=2708328; DOI=10.1016/s0021-9258(18)83474-3;
RA   Habuka N., Murakami Y., Noma M., Kudo T., Horikoshi K.;
RT   "Amino acid sequence of Mirabilis antiviral protein, total synthesis of its
RT   gene and expression in Escherichia coli.";
RL   J. Biol. Chem. 264:6629-6637(1989).
RN   [4]
RP   PROTEIN SEQUENCE OF 29-278, MASS SPECTROMETRY, AND DISULFIDE BOND.
RC   TISSUE=Seed;
RX   PubMed=11180645; DOI=10.1002/jms.102;
RA   Di Maro A., Ferranti P., Mastronicola M., Polito L., Bolognesi A.,
RA   Stirpe F., Malorni A., Parente A.;
RT   "Reliable sequence determination of ribosome-inactivating proteins by
RT   combining electrospray mass spectrometry and Edman degradation.";
RL   J. Mass Spectrom. 36:38-46(2001).
CC   -!- FUNCTION: Inhibits viral infection of plants, and protein synthesis in
CC       vitro.
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   -!- MASS SPECTROMETRY: Mass=27789; Mass_error=2; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11180645};
CC   -!- SIMILARITY: Belongs to the ribosome-inactivating protein family. Type 1
CC       RIP subfamily. {ECO:0000305}.
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DR   EMBL; D10227; BAA01079.1; -; mRNA.
DR   EMBL; D10569; BAA01425.1; -; Genomic_DNA.
DR   PIR; S35539; A39817.
DR   AlphaFoldDB; P21326; -.
DR   SMR; P21326; -.
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:0051607; P:defense response to virus; 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   Antiviral defense; Direct protein sequencing; Disulfide bond; Hydrolase;
KW   Plant defense; Protein synthesis inhibitor; Signal; Toxin.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000269|PubMed:11180645,
FT                   ECO:0000269|PubMed:2708328"
FT   CHAIN           29..278
FT                   /note="Antiviral protein MAP"
FT                   /id="PRO_0000030778"
FT   ACT_SITE        196
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..248
FT                   /evidence="ECO:0000269|PubMed:11180645"
FT   CONFLICT        35
FT                   /note="I -> L (in Ref. 1; BAA01079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        58
FT                   /note="A -> V (in Ref. 1; BAA01079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        62
FT                   /note="E -> L (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        180
FT                   /note="V -> C (in Ref. 1; BAA01079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="L -> I (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="E -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        218
FT                   /note="D -> G (in Ref. 1; BAA01079)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="E -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   278 AA;  31132 MW;  BDB9E08E65D2F92D CRC64;
     MLTTTKVFFL LLTTWITWYA IVNPQSRAAP TLETIASLDL NNPTTYLSFI TNIRTKVADK
     TEQCTIQKIS KTFTQRYSYI DLIVSSTQKI TLAIDMADLY VLGYSDIANN KGRAFFFKDV
     TEAVANNFFP GATGTNRIKL TFTGSYGDLE KNGGLRKDNP LGIFRLENSI VNIYGKAGDV
     KKQAKFFLLA IQMVSEAARF KYISDKIPSE KYEEVTVDEY MTALENNWAK LSTAVYNSKP
     STTTATKCQL ATSPVTISPW IFKTVEEIKL VMGLLKSS