ID B9T1S2_RICCO Unreviewed; 437 AA.
AC B9T1S2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Ribosome-inactivating protein {ECO:0000256|RuleBase:RU004915};
DE Contains:
DE RecName: Full=Ribosome-inactivating protein chain A {ECO:0000256|RuleBase:RU004915};
DE AltName: Full=rRNA N-glycosidase {ECO:0000256|RuleBase:RU004915};
DE EC=3.2.2.22 {ECO:0000256|RuleBase:RU004915};
DE Contains:
DE RecName: Full=Ribosome-inactivating protein chain B {ECO:0000256|RuleBase:RU004915};
GN ORFNames=RCOM_2160860 {ECO:0000313|EMBL:EEF30194.1};
OS Ricinus communis (Castor bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC Ricinus.
OX NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN [1] {ECO:0000313|Proteomes:UP000008311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX PubMed=20729833; DOI=10.1038/nbt.1674;
RA Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA Rabinowicz P.D.;
RT "Draft genome sequence of the oilseed species Ricinus communis.";
RL Nat. Biotechnol. 28:951-956(2010).
CC -!- FUNCTION: The A chain is responsible for inhibiting protein synthesis
CC through the catalytic inactivation of 60S ribosomal subunits by
CC removing adenine from position 4,324 of 28S rRNA. The B chain binds to
CC cell receptors and probably facilitates the entry into the cell of the
CC A chain; B chains are also responsible for cell agglutination (lectin
CC activity). {ECO:0000256|RuleBase:RU004915}.
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:0000256|ARBA:ARBA00000237,
CC ECO:0000256|RuleBase:RU004915};
CC -!- SUBUNIT: Might form dimers or tetramers of disulfide-linked A and B
CC chains. {ECO:0000256|RuleBase:RU004915}.
CC -!- SIMILARITY: Belongs to the ribosome-inactivating protein family.
CC {ECO:0000256|RuleBase:RU004915}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome-
CC inactivating protein family. Type 2 RIP subfamily.
CC {ECO:0000256|ARBA:ARBA00010414}.
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DR EMBL; EQ974357; EEF30194.1; -; Genomic_DNA.
DR AlphaFoldDB; B9T1S2; -.
DR STRING; 3988.B9T1S2; -.
DR eggNOG; ENOG502QUVN; Eukaryota.
DR InParanoid; B9T1S2; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 3.40.420.10; Ricin (A subunit), domain 1; 1.
DR Gene3D; 4.10.470.10; Ricin (A Subunit), domain 2; 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 InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR PANTHER; PTHR33453; -; 1.
DR PANTHER; PTHR33453:SF34; DUF6598 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000313|EMBL:EEF30194.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004915};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Plant defense {ECO:0000256|RuleBase:RU004915};
KW Protein synthesis inhibitor {ECO:0000256|ARBA:ARBA00023193,
KW ECO:0000256|RuleBase:RU004915};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Toxin {ECO:0000256|ARBA:ARBA00022656, ECO:0000256|RuleBase:RU004915};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..434
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 437 AA; 48802 MW; 9FF399FC46B08867 CRC64;
MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFLKQ YPIINFTTAG ATAQSYTTFI
RAVRSHLTTG ADVRHEIPVL SNRVGLSISQ RFILIELSNH AELSVTLALD VTNVYVVGYR
AGNSAYFFHP DNQEDAEAIT HLFTDVPNPY TFAFGGNYDR LEQLGGLREN IELGTGPLED
AISALYYYST GGTQLPTLAR SFIVCIQMIS EAARFQYIEG EMRTRIRYNR RSAPDPSVIT
LENSWGRLST AIQESNEGAF ASPIQLQRRN GSKFNVYDVS ILIPIIALMV YRCAPPPSSQ
FSLLIRPVVP NFNADVCMDP EPIVRIVGRN DLCVDVRDGR FHNGNAIQLW PCKSNTDANQ
LWTLKRDNTI RSNGKCLTTY GYSPGVYVMI YDCDTAVTDA TRWQIWDNGT IINPRSSLVL
AATRALNKSL FTLSMET
//
