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RIP3_SURMU
ID   RIP3_SURMU              Reviewed;          55 AA.
AC   P24475;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Antiviral protein GAP-31;
DE            EC=3.2.2.22;
DE   AltName: Full=Ribosome-inactivating protein;
DE   AltName: Full=rRNA N-glycosidase;
DE   Flags: Fragment;
OS   Suregada multiflora (False lime) (Gelonium multiflorum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Gelonieae;
OC   Suregada.
OX   NCBI_TaxID=3979;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Seed;
RX   PubMed=1936243; DOI=10.1016/0014-5793(91)81122-o;
RA   Lee-Huang S., Kung H.-F., Huang P.L., Huang P.L., Li B.-Q., Huang P.,
RA   Huang H.I., Chen H.-C.;
RT   "A new class of anti-HIV agents: GAP31, DAPs 30 and 32.";
RL   FEBS Lett. 291:139-144(1991).
CC   -!- FUNCTION: Single-chain ribosome-inactivating protein, possessing high
CC       antiviral potency and low toxicity to normal cells in culture and to
CC       intact animals. Capable of inhibiting HIV-1 infection and replication.
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}.
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DR   PIR; S17574; S17574.
DR   AlphaFoldDB; P24475; -.
DR   SMR; P24475; -.
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   InterPro; IPR036041; Ribosome-inact_prot_sf.
DR   InterPro; IPR016138; Ribosome_inactivat_prot_sub1.
DR   SUPFAM; SSF56371; SSF56371; 1.
PE   1: Evidence at protein level;
KW   Antiviral defense; Direct protein sequencing; Hydrolase; Plant defense;
KW   Protein synthesis inhibitor; Toxin.
FT   CHAIN           1..>55
FT                   /note="Antiviral protein GAP-31"
FT                   /id="PRO_0000221418"
FT   REGION          29..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         55
SQ   SEQUENCE   55 AA;  5847 MW;  ADA121C22834B5BF CRC64;
     GLDTVSFSTK GATYITYVNF LNELRVKTKP EGNSHGIPSL RKSSDDPGSS FVVAG
 
 
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