RIP9_SAPOF
ID RIP9_SAPOF Reviewed; 253 AA.
AC Q7M1Z2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 59.
DE RecName: Full=Ribosome-inactivating protein saporin-9;
DE Short=SAP-9;
DE Short=SO-9;
DE EC=3.2.2.22;
DE AltName: Full=rRNA N-glycosidase;
GN Name=SAP9;
OS Saponaria officinalis (Common soapwort) (Lychnis saponaria).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Caryophyllaceae; Caryophylleae; Saponaria.
OX NCBI_TaxID=3572;
RN [1] {ECO:0000305, ECO:0000312|PIR:A58923}
RP PROTEIN SEQUENCE, AND MASS SPECTROMETRY.
RC TISSUE=Seed {ECO:0000269|PubMed:11180645};
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: Ribosome-inactivating protein of type 1, inhibits protein
CC synthesis in animal cells. {ECO:0000250|UniProtKB:P20656}.
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 Evidence={ECO:0000250|UniProtKB:P20656};
CC -!- MASS SPECTROMETRY: Mass=28495; 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:0000255}.
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DR PIR; A58923; A58923.
DR AlphaFoldDB; Q7M1Z2; -.
DR SMR; Q7M1Z2; -.
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; 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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hydrolase; Plant defense;
KW Protein synthesis inhibitor; Toxin.
FT CHAIN 1..253
FT /note="Ribosome-inactivating protein saporin-9"
FT /id="PRO_0000253946"
FT ACT_SITE 176
FT /evidence="ECO:0000250|UniProtKB:P33186"
SQ SEQUENCE 253 AA; 28494 MW; 22915D5494842389 CRC64;
VTSITLDLVN PTAGQYSSFV DKIRNNVKDP NLKYGGTDIA VIGPPSKDKF LRINFQSSRG
TVSLGLKRDN LYVVAYLAMD NTNVNRAYYF RSEITSAELT ALFPEATAAN HKALEYTEDY
HSIEKNAQIT EGDKSRKELG LGINLLSSTM DTVNKKVRVV KNEARFLLIA IQMTAEAVRF
RYIQNLVTKN FPNKFNSENK VIKFEVNWKK ISTAIHGDAK NGVFNKDYDF GFGKVRLVKD
LQMGLLMHLG KPK