ID B9T1S4_RICCO Unreviewed; 575 AA.
AC B9T1S4;
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_2161680 {ECO:0000313|EMBL:EEF30196.1};
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|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; EEF30196.1; -; Genomic_DNA.
DR RefSeq; XP_002532193.1; XM_002532147.2.
DR AlphaFoldDB; B9T1S4; -.
DR GeneID; 8271864; -.
DR KEGG; rcu:8271864; -.
DR eggNOG; ENOG502QUVN; Eukaryota.
DR InParanoid; B9T1S4; -.
DR OrthoDB; 1039802at2759; -.
DR Proteomes; UP000008311; Unassembled WGS sequence.
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; 2.
DR Gene3D; 2.80.10.50; -; 2.
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; 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; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF56371; Ribosome inactivating proteins (RIP); 1.
DR SUPFAM; SSF50370; Ricin B-like lectins; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Glycosidase {ECO:0000313|EMBL:EEF30196.1};
KW Hydrolase {ECO:0000256|RuleBase:RU004915, ECO:0000313|EMBL:EEF30196.1};
KW Plant defense {ECO:0000256|RuleBase:RU004915};
KW Protein synthesis inhibitor {ECO:0000256|RuleBase:RU004915};
KW Reference proteome {ECO:0000313|Proteomes:UP000008311};
KW Toxin {ECO:0000256|RuleBase:RU004915}.
FT DOMAIN 321..447
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
FT DOMAIN 451..574
FT /note="Ricin B lectin"
FT /evidence="ECO:0000259|SMART:SM00458"
SQ SEQUENCE 575 AA; 64372 MW; 13A334FD06C12223 CRC64;
MKLGGNTIVI WIYAVATWLW FGSTSGWSFT LGDNNIFLKQ YPIINFTTAG ATAQSYTNFI
DAVRSHLTTG DDVRHEIPVL RNRVGLPINQ RFVLVQLSNQ AEHSVTLAMD VTNAYVVGYR
AGNNAYFFRP DSPEDAEAIT HLFTDAQNPY TFAFGGNYDR LEQLGGLREN IELGNGPLED
AISALYYYST GRIQLPTVAR SFIVCIQMIS EAVRFQYIEG EIRTRIRHNR RSAPDPSVIT
LENSWGRLST AIQESNQGAF ASPIQLQRRN GSKFNVYDVS KLIPIIALMV YRCARPPSTQ
FSLLIRPVVP SLNDDVCVDP EPIVRIAGRN GLCVDVRGEE FYDGNPIQLW PCKSNTDWNQ
LWTLRKDGTI RSNGKCLTIY KSSPGKHVMI YNCTTATVGA TRWQIWDNRT IINPISGLVL
AATSGNSGTT LTVQTNIYAV SQGWLPSNNT QPFVTSIVGL NDLCLQANTG KVWLDECTSE
KAEQQWALYA DGSIRPQQNQ DNCLTSDANI RETIVKTLSC STASSGQRWM FKNDGTIWNL
YNGLVLDVKR SDPTLKQIII YPFHGNPNQI WFPLF
//
