ID RICI_RICCO Reviewed; 576 AA. AC P02879; P02880; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 02-SEP-2026, entry version 210. DE RecName: Full=Ricin; DE Contains: DE RecName: Full=Ricin A chain; DE EC=3.2.2.22; DE AltName: Full=rRNA N-glycosidase; DE Contains: DE RecName: Full=Ricin B chain; DE Flags: Precursor; 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; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2999712; DOI=10.1093/nar/13.22.8019; RA Halling K.C., Halling A.C., Murray E.E., Ladin B.F., Houston L.L., RA Weaver R.F.; RT "Genomic cloning and characterization of a ricin gene from Ricinus RT communis."; RL Nucleic Acids Res. 13:8019-8033(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1371405; DOI=10.1007/bf00040667; RA Tregear J.W., Roberts L.M.; RT "The lectin gene family of Ricinus communis: cloning of a functional ricin RT gene and three lectin pseudogenes."; RL Plant Mol. Biol. 18:515-525(1992). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-576. RX PubMed=3838723; DOI=10.1111/j.1432-1033.1985.tb08834.x; RA Lamb A., Roberts L.M., Lord J.M.; RT "Nucleotide sequence of cloned cDNA coding for preproricin."; RL Eur. J. Biochem. 148:265-270(1985). RN [4] RP PROTEIN SEQUENCE OF 36-302. RA Yoshitake S., Funatsu G., Funatsu M.; RT "Isolation and sequences of peptic peptides, and the complete sequence of RT Ile chain of ricin-D."; RL Agric. Biol. Chem. 42:1267-1274(1978). RN [5] RP PROTEIN SEQUENCE OF 315-576. RX AGRICOLA=IND80011393; RA Funatsu G., Kimura M., Funatsu M.; RT "Primary structure of Ala chain of ricin D."; RL Agric. Biol. Chem. 43:2221-2224(1979). RN [6] RP GLYCOSYLATION AT ASN-45 AND ASN-271, AND PARTIAL PROTEIN SEQUENCE. RX PubMed=1368517; DOI=10.1271/bbb1961.54.157; RA Kimura Y., Kusuoku H., Tada M., Takagi S., Funatsu G.; RT "Structural analyses of sugar chains from ricin A-chain variant."; RL Agric. Biol. Chem. 54:157-162(1990). RN [7] RP REVIEW. RX PubMed=11595634; DOI=10.1016/s0041-0101(01)00158-1; RA Olsnes S., Kozlov J.V.; RT "Ricin."; RL Toxicon 39:1723-1728(2001). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=3558397; DOI=10.1016/s0021-9258(18)61201-3; RA Monfort W., Villafranca J.E., Monzingo A.F., Ernst S.R., Katzin B., RA Rutenber E., Xuong N.H., Hamlin R., Robertus J.D.; RT "The three-dimensional structure of ricin at 2.8 A."; RL J. Biol. Chem. 262:5398-5403(1987). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN. RX PubMed=1881881; DOI=10.1002/prot.340100309; RA Katzin B.J., Collins E.J., Robertus J.D.; RT "Structure of ricin A-chain at 2.5 A."; RL Proteins 10:251-259(1991). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF B-CHAIN. RX PubMed=1881882; DOI=10.1002/prot.340100310; RA Rutenber E., Robertus J.D.; RT "Structure of ricin B-chain at 2.5-A resolution."; RL Proteins 10:260-269(1991). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF A-CHAIN. RX PubMed=7990130; DOI=10.1006/jmbi.1994.1739; RA Weston S.A., Tucker A.D., Thatcher D.R., Derbyshire D.J., Pauptit R.A.; RT "X-ray structure of recombinant ricin A-chain at 1.8-A resolution."; RL J. Mol. Biol. 244:410-422(1994). RN [12] {ECO:0007744|PDB:1OBT} RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT HIS-215 IN COMPLEX WITH RP AMP. RX PubMed=8780513; DOI=10.1021/bi960880n; RA Day P.J., Ernst S.R., Frankel A.E., Monzingo A.F., Pascal J.M., RA Molina-Svinth M.C., Robertus J.D.; RT "Structure and activity of an active site substitution of ricin A chain."; RL Biochemistry 35:11098-11103(1996). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF A-CHAIN. RX PubMed=9086280; DOI=10.1006/jmbi.1996.0865; RA Yan X., Hollis T., Svinth M., Day P., Monzingo A.F., Milne G.W., RA Robertus J.D.; RT "Structure-based identification of a ricin inhibitor."; RL J. Mol. Biol. 266:1043-1049(1997). RN [14] RP MUTAGENESIS. RX PubMed=1287657; DOI=10.1093/protein/5.8.775; RA Kin Y., Robertus J.D.; RT "Analysis of several key active site residues of ricin A chain by RT mutagenesis and X-ray crystallography."; RL Protein Eng. 5:775-779(1992). RN [15] RP MUTAGENESIS OF ARG-83; LEU-109; ASP-110; VAL-111 AND ASN-132. RX PubMed=12627168; DOI=10.1038/nbt800; RA Smallshaw J.E., Ghetie V., Rizo J., Fulmer J.R., Trahan L.L., Ghetie M.-A., RA Vitetta E.S.; RT "Genetic engineering of an immunotoxin to eliminate pulmonary vascular leak RT in mice."; RL Nat. Biotechnol. 21:387-391(2003). CC -!- FUNCTION: Ricin is highly toxic to animal cells, and to a lesser extent CC to plant cells. CC -!- FUNCTION: [Ricin A chain]: Acts as a glycosidase that removes a CC specific adenine residue from an exposed loop of the 28S rRNA (A4324 in CC mammals), leading to rRNA breakage. As this loop is involved in CC elongation factor binding, modified ribosomes are catalytically CC inactive and unable to support protein synthesis. Can inactivate a few CC thousand ribosomes per minute, faster than the cell can make new ones. CC Therefore a single molecule can kill an animal cell. CC -!- FUNCTION: [Ricin B chain]: Binds to beta-D-galactopyranoside moieties CC on cell surface glycoproteins and glycolipids and facilitates the entry CC into the cell of the A chain. Also responsible for cell agglutination CC (Lectin activity). CC -!- CATALYTIC ACTIVITY: [Ricin A chain]: CC Reaction=Endohydrolysis of the N-glycosidic bond at one specific CC adenosine on the 28S rRNA.; EC=3.2.2.22; CC -!- SUBUNIT: Disulfide-linked dimer of A and B chains. CC -!- DOMAIN: [Ricin B chain]: Composed of two domains, each domain consists CC of 3 homologous subdomains (alpha, beta, gamma). CC -!- BIOTECHNOLOGY: [Ricin A chain]: A deglycosylated form may be linked to CC monoclonal antibodies to produce immunotoxins exploited in cancer CC treatment. However, a point mutation should be introduced to eliminate CC vascular leak syndrome, a side effect resulting from endothelial CC damage. CC -!- SIMILARITY: In the N-terminal section; belongs to the ribosome- CC inactivating protein family. Type 2 RIP subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=Ref.4; Type=Miscellaneous discrepancy; Note=High number of conflicts with the sequence translated from DNA.; Evidence={ECO:0000305}; CC Sequence=Ref.5; Type=Miscellaneous discrepancy; Note=High number of conflicts with the sequence translated from DNA.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Baneful beans - Issue 31 of CC February 2003; CC URL="https://www.proteinspotlight.org/back_issues/031"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X03179; CAA26939.1; -; Genomic_DNA. DR EMBL; X52908; CAA37095.1; -; Genomic_DNA. DR EMBL; X02388; CAA26230.1; -; mRNA. DR PIR; A24041; RLCSD. DR RefSeq; NP_001310630.1; NM_001323701.1. DR PDB; 1BR5; X-ray; 2.50 A; A=36-302. DR PDB; 1BR6; X-ray; 2.30 A; A=35-302. DR PDB; 1IFS; X-ray; 2.00 A; A=36-298. DR PDB; 1IFT; X-ray; 1.80 A; A=36-298. DR PDB; 1IFU; X-ray; 2.40 A; A=36-298. DR PDB; 1IL3; X-ray; 2.80 A; A=36-302. DR PDB; 1IL4; X-ray; 2.60 A; A=36-302. DR PDB; 1IL5; X-ray; 2.80 A; A/B=36-302. DR PDB; 1IL9; X-ray; 3.10 A; A=36-302. DR PDB; 1J1M; X-ray; 1.50 A; A=36-302. DR PDB; 1OBS; X-ray; 2.20 A; A=36-302. DR PDB; 1OBT; X-ray; 2.80 A; A=36-302. DR PDB; 1RTC; X-ray; 2.30 A; A=36-302. DR PDB; 1UQ4; X-ray; 1.90 A; A=40-302. DR PDB; 1UQ5; X-ray; 1.40 A; A=40-302. DR PDB; 2AAI; X-ray; 2.50 A; A=36-302, B=315-576. DR PDB; 2P8N; X-ray; 1.94 A; A=36-302. DR PDB; 2PJO; X-ray; 1.80 A; A=36-302. DR PDB; 2R2X; X-ray; 2.40 A; A=36-302. DR PDB; 2R3D; X-ray; 2.09 A; A=36-302. DR PDB; 2VC3; X-ray; 1.60 A; A=36-302. DR PDB; 2VC4; X-ray; 1.39 A; A=36-302. DR PDB; 3EJ5; X-ray; 2.50 A; X=40-296. DR PDB; 3HIO; X-ray; 2.00 A; A=36-302. DR PDB; 3LC9; X-ray; 2.28 A; A=36-233. DR PDB; 3MK9; X-ray; 2.08 A; A=36-233. DR PDB; 3PX8; X-ray; 1.29 A; X=39-296. DR PDB; 3PX9; X-ray; 1.89 A; X=39-296. DR PDB; 3RTI; X-ray; 2.80 A; A=36-302, B=315-576. DR PDB; 3RTJ; X-ray; 3.00 A; A=36-302, B=315-576. DR PDB; 3SRP; X-ray; 2.14 A; A=36-302. DR PDB; 4ESI; X-ray; 1.87 A; A=36-302. DR PDB; 4HUO; X-ray; 1.52 A; X=36-302. DR PDB; 4HUP; X-ray; 1.70 A; X=36-302. DR PDB; 4HV3; X-ray; 1.54 A; A=36-302. DR PDB; 4HV7; X-ray; 1.87 A; X=36-302. DR PDB; 4IMV; X-ray; 2.25 A; A=36-233. DR PDB; 4KUC; X-ray; 2.79 A; A/I=36-302. DR PDB; 4LGP; X-ray; 2.40 A; A/C=36-296. DR PDB; 4LGR; X-ray; 1.65 A; A=40-294. DR PDB; 4LGS; X-ray; 2.70 A; A=39-301. DR PDB; 4LHJ; X-ray; 1.80 A; A=39-297. DR PDB; 4LHQ; X-ray; 2.30 A; A/C=39-298. DR PDB; 4MX1; X-ray; 1.59 A; A=36-302. DR PDB; 4MX5; X-ray; 1.52 A; X=36-302. DR PDB; 4Q2V; X-ray; 2.20 A; A=36-302. DR PDB; 4Z9K; X-ray; 1.50 A; A=39-296. DR PDB; 5BOZ; X-ray; 3.10 A; A/B/C/D/E/F=39-299. DR PDB; 5DDZ; X-ray; 1.50 A; A=36-302. DR PDB; 5E1H; X-ray; 2.03 A; A=40-297. DR PDB; 5GU4; X-ray; 1.55 A; A/B=36-302. DR PDB; 5J56; X-ray; 1.80 A; A=36-302. DR PDB; 5J57; X-ray; 1.70 A; A=36-302. DR PDB; 5SV3; X-ray; 2.73 A; B/D=36-233. DR PDB; 5U4L; X-ray; 2.50 A; A=36-302. DR PDB; 5U4M; X-ray; 2.50 A; A=40-294. DR PDB; 6CWG; X-ray; 2.60 A; A/C=36-302. DR PDB; 6OBC; X-ray; 1.76 A; A=40-298. DR PDB; 6OBE; X-ray; 1.73 A; A=38-302. DR PDB; 6OBG; X-ray; 2.00 A; A/B=40-296. DR PDB; 6OBM; X-ray; 2.50 A; A=40-298. DR PDB; 6OBO; X-ray; 1.90 A; A/B=40-296. DR PDB; 6OCA; X-ray; 2.11 A; A/B=38-302. DR PDB; 6OCD; X-ray; 2.10 A; A/C=40-297. DR PDB; 6URW; X-ray; 2.40 A; A=36-302. DR PDB; 6URX; X-ray; 1.99 A; A=36-302. DR PDB; 6URY; X-ray; 1.54 A; A/B=36-302. DR PDB; 7KBI; X-ray; 3.05 A; A=36-302, B=315-576. DR PDB; 7KBK; X-ray; 2.09 A; A=36-302, B=315-576. DR PDB; 7KC9; X-ray; 2.30 A; A/D=36-302, B/E=315-576. DR PDB; 7KD0; X-ray; 2.77 A; A=36-302, B=315-576. DR PDB; 7KD2; X-ray; 2.55 A; A=36-302, B=315-576. DR PDB; 7KDM; X-ray; 2.30 A; A/D=36-302, B/E=315-576. DR PDB; 7KDU; X-ray; 2.81 A; A=36-302, B=315-576. DR PDB; 7MLN; X-ray; 1.52 A; A=36-302. DR PDB; 7MLO; X-ray; 1.65 A; A/B=36-302. DR PDB; 7MLP; X-ray; 1.78 A; A=36-302. DR PDB; 7MLT; X-ray; 1.80 A; A=36-302. DR PDB; 7TGF; X-ray; 1.35 A; A=36-302. DR PDB; 7TGI; X-ray; 2.10 A; A=36-302. DR PDB; 7TH2; X-ray; 1.84 A; A/B=36-302. DR PDB; 7TH3; X-ray; 2.29 A; A=36-302. DR PDB; 7XZS; X-ray; 1.50 A; A=36-302. DR PDB; 7XZT; X-ray; 1.30 A; A=36-302. DR PDB; 7XZU; X-ray; 1.60 A; A=36-302. DR PDB; 7XZW; X-ray; 1.45 A; A=36-302. DR PDB; 7Y02; X-ray; 1.60 A; A=36-302. DR PDB; 7Y03; X-ray; 1.35 A; A=36-302. DR PDB; 7Y05; X-ray; 1.60 A; A=36-302. DR PDB; 7Y06; X-ray; 1.35 A; A=36-302. DR PDB; 7Y07; X-ray; 1.25 A; A=36-302. DR PDB; 7Y08; X-ray; 1.25 A; A=36-302. DR PDB; 7Y4K; X-ray; 1.70 A; A=36-302. DR PDB; 7Y4M; X-ray; 1.45 A; A=36-302. DR PDB; 8I7P; X-ray; 1.60 A; A=36-302. DR PDB; 8T9V; X-ray; 1.95 A; A=39-296. DR PDB; 8TAB; X-ray; 2.26 A; A=39-296. DR PDB; 8TAD; X-ray; 2.76 A; A=39-293. DR PDB; 8TFH; X-ray; 3.29 A; A=39-298, B=315-576. DR PDB; 8TFL; X-ray; 2.89 A; A=40-299, B=316-576. DR PDB; 9E3T; X-ray; 1.80 A; A/B=36-302. DR PDB; 9E40; X-ray; 1.80 A; A=36-302. DR PDB; 9E42; X-ray; 1.80 A; A/B=36-302. DR AlphaFoldDB; P02879; -. DR MDposit; P02879; -. DR MDRepo; P02879; -. DR SMR; P02879; -. DR BioGRID; 1022023; 2. DR DIP; DIP-46421N; -. DR IntAct; P02879; 4. DR MINT; P02879; -. DR BindingDB; P02879; -. DR ChEMBL; CHEMBL4756; -. DR Allergome; 2803; Ric c RIP. DR UniLectin; P02879; -. DR GlyConnect; P02879; 4 N-Linked glycans (2 sites). DR ABCD; P02879; 104 sequenced antibodies. DR GeneID; 8261245; -. DR KEGG; rcu:8261245; -. DR eggNOG; ENOG502QUVN; Eukaryota. DR OrthoDB; 851521at2759; -. DR BioCyc; MetaCyc:MONOMER-18749; -. DR BRENDA; 3.2.2.22; 1204. DR EvolutionaryTrace; P02879; -. DR PRO; PR:P02879; -. DR Proteomes; UP000824732; Chromosome 8. DR GO; GO:0016208; F:AMP binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB. DR GO; GO:0030598; F:rRNA N-glycosylase activity; IEA:UniProtKB-EC. DR GO; GO:0031640; P:killing of cells of another organism; IDA:CACAO. DR GO; GO:0017148; P:negative regulation of translation; IEA:InterPro. DR CDD; cd23480; beta-trefoil_Ricin-like_rpt1; 1. DR CDD; cd23487; beta-trefoil_Ricin_like_rpt2; 1. DR FunFam; 2.80.10.50:FF:000076; Beta-galactoside-specific lectin 1; 1. DR FunFam; 2.80.10.50:FF:000079; Ricin; 1. DR FunFam; 3.40.420.10:FF:000001; Ricin; 1. DR FunFam; 4.10.470.10:FF:000001; Ricin; 1. 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; 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; RIBOSOME-INACTIVATING 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. DR PROSITE; PS00275; SHIGA_RICIN; 1. DR PDBsum; 1BR5; -. DR PDBsum; 1BR6; -. DR PDBsum; 1IFS; -. DR PDBsum; 1IFT; -. DR PDBsum; 1IFU; -. DR PDBsum; 1IL3; -. DR PDBsum; 1IL4; -. DR PDBsum; 1IL5; -. DR PDBsum; 1IL9; -. DR PDBsum; 1J1M; -. DR PDBsum; 1OBS; -. DR PDBsum; 1OBT; -. DR PDBsum; 1RTC; -. DR PDBsum; 1UQ4; -. DR PDBsum; 1UQ5; -. DR PDBsum; 2AAI; -. DR PDBsum; 2P8N; -. DR PDBsum; 2PJO; -. DR PDBsum; 2R2X; -. DR PDBsum; 2R3D; -. DR PDBsum; 2VC3; -. DR PDBsum; 2VC4; -. DR PDBsum; 3EJ5; -. DR PDBsum; 3HIO; -. DR PDBsum; 3LC9; -. DR PDBsum; 3MK9; -. DR PDBsum; 3PX8; -. DR PDBsum; 3PX9; -. DR PDBsum; 3RTI; -. DR PDBsum; 3RTJ; -. DR PDBsum; 3SRP; -. DR PDBsum; 4ESI; -. DR PDBsum; 4HUO; -. DR PDBsum; 4HUP; -. DR PDBsum; 4HV3; -. DR PDBsum; 4HV7; -. DR PDBsum; 4IMV; -. DR PDBsum; 4KUC; -. DR PDBsum; 4LGP; -. DR PDBsum; 4LGR; -. DR PDBsum; 4LGS; -. DR PDBsum; 4LHJ; -. DR PDBsum; 4LHQ; -. DR PDBsum; 4MX1; -. DR PDBsum; 4MX5; -. DR PDBsum; 4Q2V; -. DR PDBsum; 4Z9K; -. DR PDBsum; 5BOZ; -. DR PDBsum; 5DDZ; -. DR PDBsum; 5E1H; -. DR PDBsum; 5GU4; -. DR PDBsum; 5J56; -. DR PDBsum; 5J57; -. DR PDBsum; 5SV3; -. DR PDBsum; 5U4L; -. DR PDBsum; 5U4M; -. DR PDBsum; 6CWG; -. DR PDBsum; 6OBC; -. DR PDBsum; 6OBE; -. DR PDBsum; 6OBG; -. DR PDBsum; 6OBM; -. DR PDBsum; 6OBO; -. DR PDBsum; 6OCA; -. DR PDBsum; 6OCD; -. DR PDBsum; 6URW; -. DR PDBsum; 6URX; -. DR PDBsum; 6URY; -. DR PDBsum; 7KBI; -. DR PDBsum; 7KBK; -. DR PDBsum; 7KC9; -. DR PDBsum; 7KD0; -. DR PDBsum; 7KD2; -. DR PDBsum; 7KDM; -. DR PDBsum; 7KDU; -. DR PDBsum; 7MLN; -. DR PDBsum; 7MLO; -. DR PDBsum; 7MLP; -. DR PDBsum; 7MLT; -. DR PDBsum; 7TGF; -. DR PDBsum; 7TGI; -. DR PDBsum; 7TH2; -. DR PDBsum; 7TH3; -. DR PDBsum; 7XZS; -. DR PDBsum; 7XZT; -. DR PDBsum; 7XZU; -. DR PDBsum; 7XZW; -. DR PDBsum; 7Y02; -. DR PDBsum; 7Y03; -. DR PDBsum; 7Y05; -. DR PDBsum; 7Y06; -. DR PDBsum; 7Y07; -. DR PDBsum; 7Y08; -. DR PDBsum; 7Y4K; -. DR PDBsum; 7Y4M; -. DR PDBsum; 8I7P; -. DR PDBsum; 8T9V; -. DR PDBsum; 8TAB; -. DR PDBsum; 8TAD; -. DR PDBsum; 8TFH; -. DR PDBsum; 8TFL; -. DR PDBsum; 9E3T; -. DR PDBsum; 9E40; -. DR PDBsum; 9E42; -. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydrolase; Lectin; Nucleotide-binding; Plant defense; KW Protein synthesis inhibitor; Reference proteome; Repeat; Signal; Toxin. FT SIGNAL 1..35 FT /evidence="ECO:0000269|Ref.4" FT CHAIN 36..302 FT /note="Ricin A chain" FT /id="PRO_0000030741" FT PROPEP 303..314 FT /note="Linker peptide" FT /evidence="ECO:0000305|Ref.5" FT /id="PRO_0000449523" FT CHAIN 315..576 FT /note="Ricin B chain" FT /evidence="ECO:0000269|Ref.5" FT /id="PRO_0000030743" FT DOMAIN 321..448 FT /note="Ricin B-type lectin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REPEAT 331..373 FT /note="1-alpha" FT REPEAT 374..414 FT /note="1-beta" FT REPEAT 417..449 FT /note="1-gamma" FT DOMAIN 451..575 FT /note="Ricin B-type lectin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174" FT REPEAT 462..497 FT /note="2-alpha" FT REPEAT 501..540 FT /note="2-beta" FT REPEAT 543..570 FT /note="2-gamma" FT ACT_SITE 115 FT /evidence="ECO:0000250|UniProtKB:P84531" FT ACT_SITE 158 FT /evidence="ECO:0000250|UniProtKB:P84531" FT ACT_SITE 212 FT /evidence="ECO:0000250|UniProtKB:P84531" FT ACT_SITE 215 FT /evidence="ECO:0000250|UniProtKB:P84531" FT BINDING 43..45 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000250" FT BINDING 50 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 85 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 115..116 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:8780513, FT ECO:0007744|PDB:1OBT" FT BINDING 156..158 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:8780513, FT ECO:0007744|PDB:1OBT" FT BINDING 176..181 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 230..232 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 324 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000250" FT BINDING 336..340 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 349 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 354 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 360 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 409 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000250" FT BINDING 449 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT /evidence="ECO:0000250" FT BINDING 548..551 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT BINDING 565..569 FT /ligand="a carbohydrate" FT /ligand_id="ChEBI:CHEBI:16646" FT CARBOHYD 45 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:1368517" FT /id="CAR_000080" FT CARBOHYD 271 FT /note="N-linked (GlcNAc...) asparagine; partial" FT /evidence="ECO:0000269|PubMed:1368517" FT /id="CAR_000081" FT DISULFID 294..318 FT /note="Interchain (between A and B chains)" FT DISULFID 334..353 FT DISULFID 377..394 FT DISULFID 465..478 FT DISULFID 504..521 FT MUTAGEN 83 FT /note="R->A: No effect on the toxic activity but suppresses FT the vascular leak syndrome." FT /evidence="ECO:0000269|PubMed:12627168" FT MUTAGEN 109 FT /note="L->A,M: No effect on the toxic activity or the FT vascular leak syndrome." FT /evidence="ECO:0000269|PubMed:12627168" FT MUTAGEN 110 FT /note="D->A,E,N: Suppresses the toxic activity." FT /evidence="ECO:0000269|PubMed:12627168" FT MUTAGEN 111 FT /note="V->A,M: No effect on the toxic activity or the FT vascular leak syndrome." FT /evidence="ECO:0000269|PubMed:12627168" FT MUTAGEN 132 FT /note="N->A: No effect on the toxic activity but Suppresses FT the vascular leak syndrome." FT /evidence="ECO:0000269|PubMed:12627168" FT CONFLICT 76 FT /note="E -> D (in Ref. 3; CAA26230)" FT /evidence="ECO:0000305" FT CONFLICT 551 FT /note="A -> R (in Ref. 3; CAA26230)" FT /evidence="ECO:0000305" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:6URY" FT STRAND 43..47 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 48..50 FT /evidence="ECO:0007829|PDB:1IL3" FT HELIX 53..67 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 68..71 FT /evidence="ECO:0007829|PDB:7MLN" FT STRAND 72..74 FT /evidence="ECO:0007829|PDB:6OBE" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 80..82 FT /evidence="ECO:0007829|PDB:7Y07" FT TURN 83..85 FT /evidence="ECO:0007829|PDB:3HIO" FT HELIX 88..90 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 91..98 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 100..102 FT /evidence="ECO:0007829|PDB:2AAI" FT STRAND 104..110 FT /evidence="ECO:0007829|PDB:7Y07" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 115..121 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 124..127 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 133..138 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 139..141 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 147..151 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 158..165 FT /evidence="ECO:0007829|PDB:7Y07" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:3MK9" FT HELIX 169..171 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 176..188 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 189..191 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 196..207 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 208..212 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 217..229 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 234..236 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 237..255 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 257..259 FT /evidence="ECO:0007829|PDB:7MLT" FT STRAND 260..268 FT /evidence="ECO:0007829|PDB:7Y07" FT STRAND 270..272 FT /evidence="ECO:0007829|PDB:7KC9" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 280..283 FT /evidence="ECO:0007829|PDB:7Y07" FT TURN 284..286 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 295..298 FT /evidence="ECO:0007829|PDB:7Y07" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:8TFL" FT STRAND 324..328 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 338..340 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 347..351 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 352..354 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 359..361 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 363..365 FT /evidence="ECO:0007829|PDB:7KBK" FT TURN 367..369 FT /evidence="ECO:0007829|PDB:7KDU" FT STRAND 371..373 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 376..381 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 388..392 FT /evidence="ECO:0007829|PDB:7KBK" FT TURN 394..396 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 399..402 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 412..414 FT /evidence="ECO:0007829|PDB:7KBK" FT TURN 415..418 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 419..422 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 424..427 FT /evidence="ECO:0007829|PDB:8TFH" FT HELIX 430..432 FT /evidence="ECO:0007829|PDB:7KBI" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 441..443 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 446..449 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 454..459 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 461..463 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 465..469 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 472..476 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 483..485 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 495..497 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 503..506 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 508..511 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 526..528 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 530..532 FT /evidence="ECO:0007829|PDB:7KC9" FT STRAND 538..540 FT /evidence="ECO:0007829|PDB:7KC9" FT TURN 541..543 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 546..549 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 550..552 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 554..556 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 559..562 FT /evidence="ECO:0007829|PDB:7KBK" FT HELIX 568..570 FT /evidence="ECO:0007829|PDB:7KBK" FT STRAND 573..575 FT /evidence="ECO:0007829|PDB:7KBK" SQ SEQUENCE 576 AA; 64091 MW; C14C4B77A8B5470D CRC64; MKPGGNTIVI WMYAVATWLC FGSTSGWSFT LEDNNIFPKQ YPIINFTTAG ATVQSYTNFI RAVRGRLTTG ADVRHEIPVL PNRVGLPINQ RFILVELSNH AELSVTLALD VTNAYVVGYR AGNSAYFFHP DNQEDAEAIT HLFTDVQNRY TFAFGGNYDR LEQLAGNLRE NIELGNGPLE EAISALYYYS TGGTQLPTLA RSFIICIQMI SEAARFQYIE GEMRTRIRYN RRSAPDPSVI TLENSWGRLS TAIQESNQGA FASPIQLQRR NGSKFSVYDV SILIPIIALM VYRCAPPPSS QFSLLIRPVV PNFNADVCMD PEPIVRIVGR NGLCVDVRDG RFHNGNAIQL WPCKSNTDAN QLWTLKRDNT IRSNGKCLTT YGYSPGVYVM IYDCNTAATD ATRWQIWDNG TIINPRSSLV LAATSGNSGT TLTVQTNIYA VSQGWLPTNN TQPFVTTIVG LYGLCLQANS GQVWIEDCSS EKAEQQWALY ADGSIRPQQN RDNCLTSDSN IRETVVKILS CGPASSGQRW MFKNDGTILN LYSGLVLDVR ASDPSLKQII LYPLHGDPNQ IWLPLF //