RICI_RICCO
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 03-AUG-2022, entry version 193.
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://web.expasy.org/spotlight/back_issues/031";
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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=36-302.
DR PDB; 1IFS; X-ray; 2.00 A; A=38-298.
DR PDB; 1IFT; X-ray; 1.80 A; A=38-298.
DR PDB; 1IFU; X-ray; 2.40 A; A=38-298.
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; 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 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 AlphaFoldDB; 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 CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR UniLectin; P02879; -.
DR GlyConnect; 536; 4 N-Linked glycans (2 sites).
DR ABCD; P02879; 89 sequenced antibodies.
DR GeneID; 8261245; -.
DR KEGG; rcu:8261245; -.
DR eggNOG; ENOG502QUVN; Eukaryota.
DR OrthoDB; 818458at2759; -.
DR BioCyc; MetaCyc:MON-18749; -.
DR BRENDA; 3.2.2.22; 1204.
DR EvolutionaryTrace; P02879; -.
DR PRO; PR:P02879; -.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:CACAO.
DR GO; GO:0017148; P:negative regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
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; 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; PTHR33453; 1.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR Pfam; PF00161; RIP; 1.
DR PRINTS; PR00396; SHIGARICIN.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR SUPFAM; SSF56371; SSF56371; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
DR PROSITE; PS00275; SHIGA_RICIN; 1.
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; 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 STRAND 43..48
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:6URX"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:6OBE"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3HIO"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 91..98
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:2AAI"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 140..145
FT /evidence="ECO:0007829|PDB:1BR6"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 158..165
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3MK9"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 176..188
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 196..215
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 237..254
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:6OBM"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:7KC9"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:3PX8"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:3PX8"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:3PX8"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:4HV3"
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 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 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
