CEL3_CUCEC
ID CEL3_CUCEC Reviewed; 442 AA.
AC Q868M7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Galactose/N-acetylgalactosamine-binding lectin CEL-III {ECO:0000305};
DE Short=Gal/GalNAc-binding lectin CEL-III {ECO:0000305};
DE AltName: Full=CEL-III {ECO:0000303|PubMed:27101707, ECO:0000303|PubMed:7798179};
DE AltName: Full=Hemolytic lectin CEL-III {ECO:0000312|EMBL:BAC75827.1};
DE AltName: Full=Lectin CEL-III {ECO:0000303|PubMed:17977832, ECO:0000303|PubMed:23583369};
DE Flags: Precursor;
GN Name=cel3 {ECO:0000312|EMBL:BAC75827.1};
OS Cucumaria echinata (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Dendrochirotacea; Dendrochirotida; Cucumariidae; Cucumaria.
OX NCBI_TaxID=40245 {ECO:0000312|EMBL:BAC75827.1};
RN [1] {ECO:0000312|EMBL:BAC75827.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-24; 28-58; 63-100;
RP 102-103; 105-167; 173-259; 264-303 AND 403-442, MASS SPECTROMETRY, AND
RP PYROGLUTAMATE FORMATION AT GLN-11.
RX PubMed=10561549; DOI=10.1016/s0167-4838(99)00212-5;
RA Nakano M., Tabata S., Sugihara K., Kouzuma Y., Kimura M., Yamasaki N.;
RT "Primary structure of hemolytic lectin CEL-III from marine invertebrate
RT Cucumaria echinata and its cDNA: structural similarity to the B-chain from
RT plant lectin, ricin.";
RL Biochim. Biophys. Acta 1435:167-176(1999).
RN [2]
RP PROTEIN SEQUENCE OF 158-167; 291-300 AND 294-302, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND CIRCULAR DICHROISM
RP ANALYSIS OF THE C-TERMINUS.
RX PubMed=14561725; DOI=10.1093/jb/mvg157;
RA Kouzuma Y., Suzuki Y., Nakano M., Matsuyama K., Tojo S., Kimura M.,
RA Yamasaki T., Aoyagi H., Hatakeyama T.;
RT "Characterization of functional domains of the hemolytic lectin CEL-III
RT from the marine invertebrate Cucumaria echinata.";
RL J. Biochem. 134:395-402(2003).
RN [3]
RP PROTEIN SEQUENCE OF 291-300, FUNCTION, COFACTOR, ACTIVITY REGULATION,
RP SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN.
RX PubMed=11471734; DOI=10.1271/bbb.65.1347;
RA Sallay I., Tojo S., Nomiyama K., Kouzuma Y., Kimura M., Yamasaki N.;
RT "Calcium ions stabilize a protein structure of hemolytic lectin CEL-III
RT from marine invertebrate Cucumaria echinata.";
RL Biosci. Biotechnol. Biochem. 65:1347-1352(2001).
RN [4]
RP FUNCTION, COFACTOR, AND ACTIVITY REGULATION.
RX PubMed=7798179; DOI=10.1093/oxfordjournals.jbchem.a124495;
RA Hatakeyama T., Kohzaki H., Nagatomo H., Yamasaki N.;
RT "Purification and characterization of four Ca(2+)-dependent lectins from
RT the marine invertebrate, Cucumaria echinata.";
RL J. Biochem. 116:209-214(1994).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=7876091; DOI=10.1074/jbc.270.8.3560;
RA Hatakeyama T., Nagatomo H., Yamasaki N.;
RT "Interaction of the hemolytic lectin CEL-III from the marine invertebrate
RT Cucumaria echinata with the erythrocyte membrane.";
RL J. Biol. Chem. 270:3560-3564(1995).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=8663224; DOI=10.1074/jbc.271.28.16915;
RA Hatakeyama T., Furukawa M., Nagatomo H., Yamasaki N., Mori T.;
RT "Oligomerization of the hemolytic lectin CEL-III from the marine
RT invertebrate Cucumaria echinata induced by the binding of carbohydrate
RT ligands.";
RL J. Biol. Chem. 271:16915-16920(1996).
RN [7]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MASS
RP SPECTROMETRY.
RX PubMed=9305736; DOI=10.1016/s0014-5793(97)00976-9;
RA Fujisawa T., Kuwahara H., Hiromasa Y., Niidome T., Aoyagi H.,
RA Hatakeyama T.;
RT "Small-angle X-ray scattering study on CEL-III, a hemolytic lectin from
RT Holothuroidea Cucumaria echinata, and its oligomer induced by the binding
RT of specific carbohydrate.";
RL FEBS Lett. 414:79-83(1997).
RN [8]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9058193; DOI=10.1093/oxfordjournals.jbchem.a021571;
RA Hatakeyama T., Miyamoto Y., Nagatomo H., Sallay I., Yamasaki N.;
RT "Carbohydrate-binding properties of the hemolytic lectin CEL-III from the
RT holothuroidea Cucumaria echinata as analyzed using carbohydrate-coated
RT microplate.";
RL J. Biochem. 121:63-67(1997).
RN [9]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND BIOTECHNOLOGY.
RX PubMed=9133626; DOI=10.1093/oxfordjournals.jbchem.a021622;
RA Oda T., Tsuru M., Hatakeyama T., Nagatomo H., Muramatsu T., Yamasaki N.;
RT "Temperature- and pH-dependent cytotoxic effect of the hemolytic lectin
RT CEL-III from the marine invertebrate Cucumaria echinata on various cell
RT lines.";
RL J. Biochem. 121:560-567(1997).
RN [10]
RP FUNCTION, SUBUNIT, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=9692203; DOI=10.1271/bbb.62.1185;
RA Hatakeyama T., Matsuyama Y., Funada T., Fukuyama S., Kuwahara H.,
RA Aoyagi H., Yamasaki N.;
RT "Chemical modification of the hemolytic lectin CEL-III by succinic
RT anhydride: involvement of amino groups in the oligomerization process.";
RL Biosci. Biotechnol. Biochem. 62:1185-1189(1998).
RN [11]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9805377; DOI=10.1271/bbb.62.1757;
RA Sallay I., Hatakeyama T., Yamasaki N.;
RT "Studies on the carbohydrate binding sites of the hemolytic lectin CEL-III
RT isolated from the marine invertebrate Cucumaria echinata.";
RL Biosci. Biotechnol. Biochem. 62:1757-1761(1998).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=10478454; DOI=10.1271/bbb.63.1279;
RA Kouriki-Nagatomo H., Hatakeyama T., Jelokhani-Niaraki M., Kondo M.,
RA Ehara T., Yamasaki N.;
RT "Molecular mechanism for pore-formation in lipid membranes by the hemolytic
RT lectin CEL-III from marine invertebrate Cucumaria echinata.";
RL Biosci. Biotechnol. Biochem. 63:1279-1284(1999).
RN [13]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9990124; DOI=10.1093/oxfordjournals.jbchem.a022284;
RA Hatakeyama T., Sato T., Taira E., Kuwahara H., Niidome T., Aoyagi H.;
RT "Characterization of the interaction of hemolytic lectin CEL-III from the
RT marine invertebrate, Cucumaria echinata, with artificial lipid membranes:
RT involvement of neutral sphingoglycolipids in the pore-forming process.";
RL J. Biochem. 125:277-284(1999).
RN [14]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10101284; DOI=10.1093/oxfordjournals.jbchem.a022341;
RA Oda T., Shinmura N., Nishioka Y., Komatsu N., Hatakeyama T., Muramatsu T.;
RT "Effect of the hemolytic lectin CEL-III from Holothuroidea Cucumaria
RT echinata on the ANS fluorescence responses in sensitive MDCK and resistant
RT CHO cells.";
RL J. Biochem. 125:713-720(1999).
RN [15]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10923802; DOI=10.1271/bbb.64.1278;
RA Kuwahara H., Funada T., Hatakeyama T., Aoyagi H.;
RT "Effects of chemical modification of carboxyl groups in the hemolytic
RT lectin CEL-III on its hemolytic and carbohydrate-binding activities.";
RL Biosci. Biotechnol. Biochem. 64:1278-1281(2000).
RN [16]
RP FUNCTION, SUBUNIT, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=11983084; DOI=10.1093/oxfordjournals.jbchem.a003161;
RA Kuwahara H., Yamasaki T., Hatakeyama T., Aoyagi H., Fujisawa T.;
RT "Oligomerization process of the hemolytic lectin CEL-III purified from a
RT sea cucumber, Cucumaria echinata.";
RL J. Biochem. 131:751-756(2002).
RN [17]
RP DOMAIN, BIOTECHNOLOGY, AND MUTAGENESIS OF LYS-342; VAL-344; LYS-348;
RP VAL-351; VAL-353; LYS-354; VAL-355 AND LYS-361.
RX PubMed=14999010; DOI=10.1093/jb/mvh007;
RA Hatakeyama T., Suenaga T., Eto S., Niidome T., Aoyagi H.;
RT "Antibacterial activity of peptides derived from the C-terminal region of a
RT hemolytic lectin, CEL-III, from the marine invertebrate Cucumaria
RT echinata.";
RL J. Biochem. 135:65-70(2004).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND BIOTECHNOLOGY.
RX PubMed=18159942; DOI=10.1371/journal.ppat.0030192;
RA Yoshida S., Shimada Y., Kondoh D., Kouzuma Y., Ghosh A.K.,
RA Jacobs-Lorena M., Sinden R.E.;
RT "Hemolytic C-type lectin CEL-III from sea cucumber expressed in transgenic
RT mosquitoes impairs malaria parasite development.";
RL PLoS Pathog. 3:e192-e192(2007).
RN [19]
RP DOMAIN, REGION, AND MUTAGENESIS OF VAL-332; VAL-334; VAL-336; VAL-351;
RP VAL-353 AND VAL-355.
RX PubMed=17965430; DOI=10.1093/jb/mvm195;
RA Hisamatsu K., Tsuda N., Goda S., Hatakeyama T.;
RT "Characterization of the {alpha}-helix region in domain 3 of the haemolytic
RT lectin CEL-III: implications for self-oligomerization and haemolytic
RT processes.";
RL J. Biochem. 143:79-86(2008).
RN [20]
RP FUNCTION, COFACTOR, ACTIVITY REGULATION, REGION, AND CIRCULAR DICHROISM
RP ANALYSIS.
RX PubMed=19420692; DOI=10.1271/bbb.80793;
RA Hisamatsu K., Unno H., Goda S., Hatakeyama T.;
RT "Effects of Ca2+ on refolding of the recombinant hemolytic lectin CEL-
RT III.";
RL Biosci. Biotechnol. Biochem. 73:1203-1205(2009).
RN [21]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF VAL-332; VAL-334; VAL-336; VAL-351;
RP VAL-353 AND VAL-355, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=19356139; DOI=10.2174/092986609787848054;
RA Hisamatsu K., Unno H., Goda S., Hatakeyama T.;
RT "Roles of the valine clusters in domain 3 of the hemolytic lectin CEL-III
RT in its oligomerization and hemolytic abilities.";
RL Protein Pept. Lett. 16:411-414(2009).
RN [22]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22313748; DOI=10.1271/bbb.110635;
RA Shimizu Y., Yamazaki H., Yoshida S., Yonekura M., Kouzuma Y.;
RT "Molecular cloning, functional expression, and characterization of
RT isolectin genes of hemolytic lectin CEL-III from the marine invertebrate
RT Cucumaria echinata.";
RL Biosci. Biotechnol. Biochem. 76:276-282(2012).
RN [23]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP CRYSTALLIZATION.
RX PubMed=23545649; DOI=10.1107/s1744309113004065;
RA Unno H., Hisamatsu K., Nagao T., Tateya Y., Matsumoto N., Goda S.,
RA Hatakeyama T.;
RT "Crystallization and preliminary crystallographic study of oligomers of the
RT haemolytic lectin CEL-III from the sea cucumber Cucumaria echinata.";
RL Acta Crystallogr. F 69:416-420(2013).
RN [24]
RP FUNCTION, SUBUNIT, MUTAGENESIS OF GLN-55; SER-315; SER-325; ILE-340;
RP LYS-342; ILE-345; LYS-348; SER-350; LYS-354; VAL-355; SER-360; LYS-361;
RP ASN-365; TYR-375; ASP-381; GLU-385; ARG-388; ASP-405; LEU-407; ILE-413;
RP LYS-415; ARG-418; LYS-430 AND ASP-435, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=23583369; DOI=10.1016/j.bbagen.2013.04.010;
RA Hisamatsu K., Nagao T., Unno H., Goda S., Hatakeyama T.;
RT "Identification of the amino acid residues involved in the hemolytic
RT activity of the Cucumaria echinata lectin CEL-III.";
RL Biochim. Biophys. Acta 1830:4211-4217(2013).
RN [25]
RP FUNCTION, AND SUBUNIT.
RX PubMed=23470749; DOI=10.1271/bbb.120981;
RA Goda S., Sadakata H., Unno H., Hatakeyama T.;
RT "Effects of detergents on the oligomeric structures of hemolytic lectin
RT CEL-III as determined by small-angle X-ray scattering.";
RL Biosci. Biotechnol. Biochem. 77:679-681(2013).
RN [26]
RP FUNCTION, AND MUTAGENESIS OF ASP-381 AND LYS-415.
RX PubMed=27101707; DOI=10.1080/09168451.2016.1176520;
RA Nagao T., Masaki R., Unno H., Goda S., Hatakeyama T.;
RT "Effects of amino acid mutations in the pore-forming domain of the
RT hemolytic lectin CEL-III.";
RL Biosci. Biotechnol. Biochem. 80:1966-1969(2016).
RN [27] {ECO:0007744|PDB:1VCL}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 11-442 IN COMPLEX WITH CALCIUM;
RP CHLORIDE AND MAGNESIUM, FUNCTION, COFACTOR, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DOMAIN, PYROGLUTAMATE FORMATION AT GLN-11, AND DISULFIDE
RP BONDS.
RX PubMed=15194688; DOI=10.1074/jbc.m404065200;
RA Uchida T., Yamasaki T., Eto S., Sugawara H., Kurisu G., Nakagawa A.,
RA Kusunoki M., Hatakeyama T.;
RT "Crystal structure of the hemolytic lectin CEL-III isolated from the marine
RT invertebrate Cucumaria echinata: implications of domain structure for its
RT membrane pore-formation mechanism.";
RL J. Biol. Chem. 279:37133-37141(2004).
RN [28] {ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 11-442 IN COMPLEX WITH CALCIUM;
RP MAGNESIUM; METHYL ALPHA-GALACTOSIDE AND N-ACETYLGALACTOSAMINE, FUNCTION,
RP COFACTOR, DOMAIN, DISULFIDE BONDS, AND MUTAGENESIS OF TYR-26; ASP-33;
RP ASP-53; GLN-54 AND GLN-55.
RX PubMed=17977832; DOI=10.1074/jbc.m705604200;
RA Hatakeyama T., Unno H., Kouzuma Y., Uchida T., Eto S., Hidemura H.,
RA Kato N., Yonekura M., Kusunoki M.;
RT "C-type lectin-like carbohydrate recognition of the hemolytic lectin CEL-
RT III containing ricin-type -trefoil folds.";
RL J. Biol. Chem. 282:37826-37835(2007).
RN [29] {ECO:0007744|PDB:3W9T}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 11-442 IN COMPLEX WITH CALCIUM;
RP MAGNESIUM; FRUCTOSE AND GALACTOSE, FUNCTION, COFACTOR, SUBUNIT, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND DISULFIDE BONDS.
RX PubMed=24652284; DOI=10.1074/jbc.m113.541896;
RA Unno H., Goda S., Hatakeyama T.;
RT "Hemolytic Lectin CEL-III Heptamerizes via a Large Structural Transition
RT from alpha-Helices to a beta-Barrel during the Transmembrane Pore Formation
RT Process.";
RL J. Biol. Chem. 289:12805-12812(2014).
CC -!- FUNCTION: Galactose/N-acetylgalactosamine (Gal/GalNAc)-binding lectin
CC with hemolytic activity. Favors saccharides that have a beta-1,4
CC linkage at the non-reducing end rather than saccharides having alpha-
CC 1,6 or alpha-1,4 linkages. Binds lactose, lactulose, GalNAc,
CC galactosamine, methyl alpha-galactopyranoside, methyl beta-
CC galactopyranoside, N-acetyllactosamine, p-nitrophenyl beta-D-
CC galactopyranoside (pNP-Gal), p-nitrophenyl N-acetyl-beta-D-
CC galactosaminide (pNP-GalNAc), asialofetuin, and human erythrocyte
CC membrane lipids lactosyl ceramide (LacCer) and globoside
CC globotetraosylceramide (Gb4Cer). Binds moderately to galactose,
CC melibiose, raffinose, fucose, methyl alpha-galactoside and methyl beta-
CC galactoside. Binds weakly to glucose, mannose and N-acetylglucosamine
CC (GlcNAc) (PubMed:7798179, PubMed:7876091, PubMed:8663224,
CC PubMed:9305736, PubMed:9058193, PubMed:9133626, PubMed:9692203,
CC PubMed:9805377, PubMed:10478454, PubMed:9990124, PubMed:10101284,
CC PubMed:10923802, PubMed:11471734, PubMed:11983084, PubMed:14561725,
CC PubMed:15194688, PubMed:17977832, PubMed:23545649, PubMed:23583369,
CC PubMed:23470749, PubMed:27101707, PubMed:24652284, PubMed:22313748,
CC PubMed:19356139, PubMed:18159942, PubMed:19420692). Has hemolytic
CC activity towards human (A, B and O-type), rabbit and rat erythrocytes,
CC but not towards mouse, chicken or horse erythrocytes (PubMed:7798179,
CC PubMed:7876091, PubMed:8663224, PubMed:9058193, PubMed:9692203,
CC PubMed:9805377, PubMed:10923802, PubMed:11471734, PubMed:19420692,
CC PubMed:19356139, PubMed:23583369, PubMed:27101707, PubMed:22313748,
CC PubMed:10101284, PubMed:18159942). Forms ion-permeable transmembrane
CC pores in the erythrocyte membrane as well as in artificial liposomes
CC containing human erythrocyte membrane lipids LacCer, Gb4Cer and
CC galactosyl ceramide (GalCer) leading to destruction of the membrane
CC (PubMed:7876091, PubMed:9133626, PubMed:10478454, PubMed:9990124). Has
CC hemagglutinating activity towards rabbit, human and rat erythrocytes,
CC and at relatively high concentrations towards chicken and horse
CC erythrocytes, but not towards mouse erythrocytes (PubMed:9692203,
CC PubMed:9805377, PubMed:9990124, PubMed:10923802, PubMed:11471734,
CC PubMed:14561725, PubMed:19420692, PubMed:7798179, PubMed:18159942). Has
CC dose-dependent cytotoxic effect on Madin-Darby canine kidney (MDCK),
CC African green monkey kidney (Vero) and human epithelia carcinoma (HeLa)
CC cell lines, but Chinese hamster ovary (CHO), rat sarcoma (XC) and
CC potoroo rat kangaroo kidney (PtK1) cells are highly resistant to the
CC cytotoxic effect of this protein (PubMed:9133626, PubMed:10101284).
CC Impairs malaria parasite development in malaria parasite infected
CC transgenic A.stephensi mosquitoes expressing this protein specifically
CC in their midguts. Binds to ookinetes and leads to strong dose-dependent
CC inhibition of ookinete formation in vitro. Leads to severely impaired
CC oocyst formation and significantly reduced sporozoite production of
CC rodent malaria parasite P.berghei in the salivary glands of the
CC transgenic mosquitoes. The parasite transmission to uninfected mice
CC (vectorial competence) of these mosquitoes is significantly impaired.
CC Leads also to severely impaired oocyst formation of human malaria
CC parasite P.falciparum in transgenic mosquitoes fed on mature
CC P.falciparum gametocyte cultures (PubMed:18159942). May be involved in
CC defense mechanisms acting as a toxic protein to foreign microorganisms
CC (PubMed:7876091, PubMed:9133626). May act in defense against predators
CC (PubMed:24652284). {ECO:0000269|PubMed:10101284,
CC ECO:0000269|PubMed:10478454, ECO:0000269|PubMed:10923802,
CC ECO:0000269|PubMed:11471734, ECO:0000269|PubMed:11983084,
CC ECO:0000269|PubMed:14561725, ECO:0000269|PubMed:15194688,
CC ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:18159942,
CC ECO:0000269|PubMed:19356139, ECO:0000269|PubMed:19420692,
CC ECO:0000269|PubMed:22313748, ECO:0000269|PubMed:23470749,
CC ECO:0000269|PubMed:23545649, ECO:0000269|PubMed:23583369,
CC ECO:0000269|PubMed:24652284, ECO:0000269|PubMed:27101707,
CC ECO:0000269|PubMed:7798179, ECO:0000269|PubMed:7876091,
CC ECO:0000269|PubMed:8663224, ECO:0000269|PubMed:9058193,
CC ECO:0000269|PubMed:9133626, ECO:0000269|PubMed:9305736,
CC ECO:0000269|PubMed:9692203, ECO:0000269|PubMed:9805377,
CC ECO:0000269|PubMed:9990124}.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:11471734, ECO:0000269|PubMed:15194688,
CC ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:19420692,
CC ECO:0000269|PubMed:24652284, ECO:0000269|PubMed:7798179,
CC ECO:0000269|PubMed:9058193};
CC Note=Binds 5 calcium ions per subunit. {ECO:0000269|PubMed:15194688,
CC ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
CC ECO:0000269|PubMed:24652284};
CC Note=Binds 2 magnesium ions per subunit. Magnesium is probably occupied
CC in place of calcium as excess magnesium is used in the experiments.
CC {ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
CC ECO:0000269|PubMed:24652284};
CC -!- ACTIVITY REGULATION: Ca(2+) is required for hemolytic activity and the
CC activity increases with increasing calcium concentration. Hemolytic
CC activity is inhibited by N-acetylgalactosamine (GalNAc), lactose,
CC lactulose, galactosamine, dextran with molecular masses greater than 4
CC kDa, to a lesser extent by inulin and only slightly by sucrose and
CC melezitose, but not by glucose or mannose. The activity is abolished in
CC the presence of 10 mM EDTA (PubMed:11471734, PubMed:19420692,
CC PubMed:7798179, PubMed:9058193, PubMed:7876091). Lactose-binding
CC increases with increasing calcium concentration, but calcium has no
CC effect on hemagglutinating activity (PubMed:9058193, PubMed:11471734).
CC Cytotoxic effect on Madin-Darby canine kidney (MDCK) cell line is
CC strongly inhibited by galactose, lactose and N-acetylgalactosamine
CC (GalNAc), but not by raffinose, N-acetylglucosamine (GlcNAc), glucose,
CC mannose, ribose or sucrose (PubMed:9133626). Pore formation in
CC artificial lactosyl ceramide (LacCer) or globotetraosylceramide
CC (Gb4Cer) containing liposomes is strongly inhibited by lactose
CC (PubMed:10478454). {ECO:0000269|PubMed:10478454,
CC ECO:0000269|PubMed:11471734, ECO:0000269|PubMed:19420692,
CC ECO:0000269|PubMed:7798179, ECO:0000269|PubMed:7876091,
CC ECO:0000269|PubMed:9058193, ECO:0000269|PubMed:9133626}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH for hemolytic activity is 10. Hemolytic activity increases
CC with increasing pH from pH 7 to pH 10, but almost no hemolytic
CC activity is observed below pH 6.5 (PubMed:7876091, PubMed:8663224).
CC Binds to lactose between pH 4-10 (PubMed:9058193, PubMed:9805377).
CC Pore formation in artificial liposomes containing human erythrocyte
CC membrane lipids lactosyl ceramide (LacCer) or globotetraosylceramide
CC (Gb4Cer) increases with increasing pH (PubMed:10478454). Cytotoxic
CC effect on Madin-Darby canine kidney (MDCK) cell line increases with
CC increasing pH with maximal cytotoxicity at pH 10 at 4 degrees
CC Celsius, but no significant pH effect is observed at 37 degrees
CC Celsius (PubMed:9133626, PubMed:10101284).
CC {ECO:0000269|PubMed:10101284, ECO:0000269|PubMed:10478454,
CC ECO:0000269|PubMed:7876091, ECO:0000269|PubMed:8663224,
CC ECO:0000269|PubMed:9058193, ECO:0000269|PubMed:9133626,
CC ECO:0000269|PubMed:9805377};
CC Temperature dependence:
CC Optimum temperature for hemolytic activity is 10 degrees Celsius.
CC Hemolytic activity decreases markedly with increasing temperature
CC (PubMed:7876091). Binds to lactose between 5-40 degrees Celsius, with
CC maximal binding around 10 degrees Celsius (PubMed:9058193). Pore
CC formation in artificial liposomes containing human erythrocyte
CC membrane lipids lactosyl ceramide (LacCer) or globotetraosylceramide
CC (Gb4Cer) increases with increasing temperature (PubMed:9990124).
CC Cytotoxic effect on African green monkey kidney (Vero) and Madin-
CC Darby canine kidney (MDCK) cell lines increases with decreasing
CC temperature (PubMed:9133626). {ECO:0000269|PubMed:7876091,
CC ECO:0000269|PubMed:9058193, ECO:0000269|PubMed:9133626,
CC ECO:0000269|PubMed:9990124};
CC -!- SUBUNIT: Oligomerizes in the human and rabbit erythrocyte membranes
CC (PubMed:7876091, PubMed:8663224, PubMed:9305736, PubMed:9692203,
CC PubMed:10478454, PubMed:10101284, PubMed:10923802, PubMed:11471734,
CC PubMed:11983084, PubMed:14561725, PubMed:19356139, PubMed:23545649,
CC PubMed:23583369, PubMed:23470749, PubMed:24652284, PubMed:22313748).
CC Oligomerization is induced by binding of beta-1,4-linked disaccharide
CC ligands such as lactose, lactulose, N-acetyllactosamine and phenyl-
CC beta-D-galactoside, but only a little by N-acetylgalactosamine and
CC galactose, and not at all by melibiose in aqueous solution in the
CC presence of high salt concentration and pH 10 (PubMed:8663224,
CC PubMed:9305736, PubMed:11983084, PubMed:23545649, PubMed:23583369,
CC PubMed:23470749, PubMed:24652284). Forms heptamers that assemble into
CC larger 21mer oligomers, which may be inserted as a transmembrane pore
CC to the erythrocyte membrane (PubMed:9305736, PubMed:11983084,
CC PubMed:23545649, PubMed:23470749, PubMed:24652284).
CC {ECO:0000269|PubMed:10101284, ECO:0000269|PubMed:10478454,
CC ECO:0000269|PubMed:10923802, ECO:0000269|PubMed:11471734,
CC ECO:0000269|PubMed:11983084, ECO:0000269|PubMed:14561725,
CC ECO:0000269|PubMed:19356139, ECO:0000269|PubMed:22313748,
CC ECO:0000269|PubMed:23470749, ECO:0000269|PubMed:23545649,
CC ECO:0000269|PubMed:23583369, ECO:0000269|PubMed:24652284,
CC ECO:0000269|PubMed:7876091, ECO:0000269|PubMed:8663224,
CC ECO:0000269|PubMed:9305736, ECO:0000269|PubMed:9692203}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10101284,
CC ECO:0000269|PubMed:10478454, ECO:0000269|PubMed:11471734,
CC ECO:0000269|PubMed:14561725, ECO:0000269|PubMed:15194688,
CC ECO:0000269|PubMed:18159942, ECO:0000269|PubMed:22313748,
CC ECO:0000269|PubMed:24652284, ECO:0000269|PubMed:7876091,
CC ECO:0000269|PubMed:8663224, ECO:0000269|PubMed:9058193,
CC ECO:0000269|PubMed:9133626, ECO:0000269|PubMed:9305736}.
CC -!- TISSUE SPECIFICITY: Expressed in body fluid (at protein level).
CC {ECO:0000269|PubMed:10101284, ECO:0000269|PubMed:10478454,
CC ECO:0000269|PubMed:11471734, ECO:0000269|PubMed:14561725,
CC ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:18159942,
CC ECO:0000269|PubMed:24652284, ECO:0000269|PubMed:7876091,
CC ECO:0000269|PubMed:8663224, ECO:0000269|PubMed:9058193,
CC ECO:0000269|PubMed:9133626, ECO:0000269|PubMed:9305736}.
CC -!- DOMAIN: The N-terminal part (1-293) is a carbohydrate recognition
CC domain (CRD) having three ricin B-type lectin domains with two
CC carbohydrate-binding domains (PubMed:14561725). The CRD domain
CC comprises of residues 11-159 and 160-293 and each of them has a beta-
CC trefoil fold (PubMed:15194688, PubMed:17977832). Total of five
CC carbohydrate molecules are bound by the CRD domain (PubMed:17977832).
CC The CRD domain is sufficient for N-acetylgalactosamine (GalNAc)-binding
CC (PubMed:14561725, PubMed:17977832). The CRD domain has weak
CC hemagglutinating activity towards rabbit erythrocytes in the presence
CC or absence of Ca(2+), but it is abolished in the presence of 10 mM EDTA
CC or by lactose (PubMed:14561725). {ECO:0000269|PubMed:14561725,
CC ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832}.
CC -!- DOMAIN: The C-terminal part (291-442) is essential for oligomerization
CC (PubMed:11471734, PubMed:14561725, PubMed:17965430). Oligomerization of
CC the C-terminal part is induced upon binding of lactose. This C-terminal
CC part is able to cause hemagglutination of rabbit erythrocytes probably
CC due to hydrophobic interaction of the oligomer with the membrane
CC leading to formation of ion-permeable pores in the membrane.
CC Hemagglutinating activity of it is not inhibited by lactose, it is
CC enhanced by Ca(2+) and completetely abolished in the presence of 10 mM
CC EDTA (PubMed:14561725). {ECO:0000269|PubMed:11471734,
CC ECO:0000269|PubMed:14561725, ECO:0000269|PubMed:17965430}.
CC -!- DOMAIN: C-terminal part (342-361) has antibacterial activity especially
CC toward Gram-positive bacteria S.aureus IFO 12732, and to a lesser
CC extent toward Gram-positive bacteria B.subtilis IFO 3134
CC (PubMed:14999010, PubMed:17965430). Weak antibacterial activity toward
CC Gram-negative bacteria P.aeruginosa ATCC 27853, and even weaker toward
CC Gram-negative bacteria E.coli ATCC 43827. This C-terminal part disrupts
CC the bacterial membrane leading to enhanced permeabilization of the
CC bacterial membrane. It has membrane-permeabilizing activity also in
CC artificial lipid vesicles (PubMed:14999010).
CC {ECO:0000269|PubMed:14999010, ECO:0000269|PubMed:17965430}.
CC -!- MASS SPECTROMETRY: Mass=47490; Method=MALDI; Note=The measured mass is
CC that of the mature protein.; Evidence={ECO:0000269|PubMed:10561549,
CC ECO:0000269|PubMed:9305736};
CC -!- BIOTECHNOLOGY: May have potential as a tool for controlled
CC permeabilization of cell membranes (PubMed:9133626). The C-terminal
CC part (342-361) of this protein may be used to generate mutant peptides
CC having increased antibacterial effect (PubMed:14999010). This protein
CC may also be used for the generation of mosquitoes that are refractory
CC to all species of human Plasmodium (PubMed:18159942).
CC {ECO:0000305|PubMed:14999010, ECO:0000305|PubMed:18159942,
CC ECO:0000305|PubMed:9133626}.
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DR EMBL; AB109017; BAC75827.1; -; mRNA.
DR PDB; 1VCL; X-ray; 1.70 A; A/B=11-442.
DR PDB; 2Z48; X-ray; 1.70 A; A/B=11-442.
DR PDB; 2Z49; X-ray; 1.95 A; A/B=11-442.
DR PDB; 3W9T; X-ray; 2.90 A; A/B/C/D/E/F/G=11-442.
DR PDBsum; 1VCL; -.
DR PDBsum; 2Z48; -.
DR PDBsum; 2Z49; -.
DR PDBsum; 3W9T; -.
DR SMR; Q868M7; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR TCDB; 1.C.96.1.1; the haemolytic lectin, cel-iii (cel-iii) family.
DR UniLectin; Q868M7; -.
DR EvolutionaryTrace; Q868M7; -.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042806; F:fucose binding; IDA:UniProtKB.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0030395; F:lactose binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:1903777; F:melibiose binding; IDA:UniProtKB.
DR GO; GO:0046871; F:N-acetylgalactosamine binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IDA:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
DR GO; GO:0019730; P:antimicrobial humoral response; IC:UniProtKB.
DR GO; GO:0001906; P:cell killing; IDA:UniProtKB.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0044179; P:hemolysis in another organism; IDA:UniProtKB.
DR GO; GO:0051673; P:membrane disruption in another organism; IDA:UniProtKB.
DR GO; GO:0035915; P:pore formation in membrane of another organism; IDA:UniProtKB.
DR GO; GO:0034120; P:positive regulation of erythrocyte aggregation; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR CDD; cd00161; RICIN; 2.
DR Gene3D; 3.30.1750.10; -; 1.
DR InterPro; IPR028988; CEL-III_C_sf.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00652; Ricin_B_lectin; 2.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF111265; SSF111265; 1.
DR SUPFAM; SSF50370; SSF50370; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Calcium; Cytolysis;
KW Direct protein sequencing; Disulfide bond; Hemolysis; Lectin; Magnesium;
KW Metal-binding; Pyrrolidone carboxylic acid; Repeat; Secreted.
FT PROPEP 1..10
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:10561549"
FT /id="PRO_0000454468"
FT CHAIN 11..442
FT /note="Galactose/N-acetylgalactosamine-binding lectin CEL-
FT III"
FT /evidence="ECO:0000305|PubMed:10561549"
FT /id="PRO_0000454469"
FT DOMAIN 28..102
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 115..245
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DOMAIN 261..293
FT /note="Ricin B-type lectin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 11..304
FT /note="Has hemagglutinating activity towards rabbit
FT erythrocytes, but no hemolytic activity towards them"
FT /evidence="ECO:0000269|PubMed:19420692"
FT REGION 294..442
FT /note="Has a strong tendency to self-associate leading to
FT formation of oligomers"
FT /evidence="ECO:0000269|PubMed:17965430"
FT BINDING 19
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0007744|PDB:2Z48"
FT BINDING 33..36
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 42
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 43
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 49
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 53
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 82
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 117
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0007744|PDB:2Z48"
FT BINDING 131..134
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 141
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 144..147
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 178..181
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 187
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 188
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 191..194
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 198
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 219..222
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 219
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 232..235
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 266..269
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 267
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 279..282
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 286
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT BINDING 286
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT MOD_RES 11
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10561549,
FT ECO:0000269|PubMed:15194688"
FT DISULFID 14..59
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT DISULFID 31..48
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 129..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 176..193
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 217..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 249..254
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT DISULFID 264..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174,
FT ECO:0000269|PubMed:15194688, ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:24652284, ECO:0007744|PDB:1VCL,
FT ECO:0007744|PDB:2Z48, ECO:0007744|PDB:2Z49,
FT ECO:0007744|PDB:3W9T"
FT DISULFID 308..390
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT DISULFID 377..416
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT DISULFID 425..439
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT DISULFID 431..436
FT /evidence="ECO:0000269|PubMed:15194688,
FT ECO:0000269|PubMed:17977832, ECO:0000269|PubMed:24652284,
FT ECO:0007744|PDB:1VCL, ECO:0007744|PDB:2Z48,
FT ECO:0007744|PDB:2Z49, ECO:0007744|PDB:3W9T"
FT MUTAGEN 26
FT /note="Y->A: Weak N-acetylgalactosamine binding."
FT /evidence="ECO:0000269|PubMed:17977832"
FT MUTAGEN 33
FT /note="D->A: Loss of N-acetylgalactosamine binding."
FT /evidence="ECO:0000269|PubMed:17977832"
FT MUTAGEN 53
FT /note="D->A: Loss of N-acetylgalactosamine binding."
FT /evidence="ECO:0000269|PubMed:17977832"
FT MUTAGEN 54
FT /note="Q->A: Loss of N-acetylgalactosamine binding."
FT /evidence="ECO:0000269|PubMed:17977832"
FT MUTAGEN 55
FT /note="Q->A: Strongly decreased hemolytic activity compared
FT to the wild-type protein. No effect on N-
FT acetylgalactosamine binding."
FT /evidence="ECO:0000269|PubMed:17977832,
FT ECO:0000269|PubMed:23583369"
FT MUTAGEN 315
FT /note="S->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 325
FT /note="S->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 332
FT /note="V->A: Alterations in oligomer formation and in
FT hemolytic activity; when associated with A-334 and A-336.
FT Alterations in oligomer formation and hemolytic activity;
FT when associated with A-334; A-336; A-351; A-353 and A-355."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139"
FT MUTAGEN 334
FT /note="V->A: Alterations in oligomer formation and in
FT hemolytic activity; when associated with A-332 and A-336.
FT Alterations in oligomer formation and in hemolytic
FT activity; when associated with A-332; A-336; A-351; A-353
FT and A-355."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139"
FT MUTAGEN 336
FT /note="V->A: Alterations in oligomer formation and in
FT hemolytic activity; when associated with A-332 and A-334.
FT Alterations in oligomer formation and in hemolytic
FT activity; when associated with A-332; A-334; A-351; A-353
FT and A-355."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139"
FT MUTAGEN 340
FT /note="I->A: No effect on oligomerization. No effect on
FT lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 342
FT /note="K->A: No effect on lactose binding. Decreased
FT antibacterial activity toward Gram-positive bacteria
FT S.aureus IFO 12732."
FT /evidence="ECO:0000269|PubMed:14999010,
FT ECO:0000269|PubMed:23583369"
FT MUTAGEN 342
FT /note="K->R: Increased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732 and increased
FT permeability of the S.aureus cell membrane; when associated
FT with R-348; R-354 and R-361."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 344
FT /note="V->L: Increased antibacterial activity toward Gram-
FT negative bacteria E.coli ATCC 43827 and P.aeruginosa ATCC
FT 27853, and toward Gram-positive bacteria S.aureus IFO 12732
FT and B.subtilis IFO 3134 including increased permeability of
FT the S.aureus cell membrane; when associated with L-351; L-
FT 353 and L-355."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 345
FT /note="I->A: Partial oligomerization. No effect on lactose
FT binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 348
FT /note="K->A: Decreased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732. Markedly decreased
FT hemolytic activity compared to the wild-type protein. No
FT effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:14999010,
FT ECO:0000269|PubMed:23583369"
FT MUTAGEN 348
FT /note="K->R: Increased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732 and increased
FT permeability of the S.aureus cell membrane; when associated
FT with R-342; R-354 and R-361."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 350
FT /note="S->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 351
FT /note="V->A: Alterations in oligomer formation and in
FT hemolytic activity; when associated with A-332; A-334; A-
FT 336; A-353 and A-355. Alterations in oligomer formation and
FT in hemolytic activity; when associated with A-353 and A-
FT 355."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139"
FT MUTAGEN 351
FT /note="V->L: Increased antibacterial activity toward Gram-
FT negative bacteria E.coli ATCC 43827 and P.aeruginosa ATCC
FT 27853, and toward Gram-positive bacteria S.aureus IFO 12732
FT and B.subtilis IFO 3134 including increased permeability of
FT the S.aureus cell membrane; when associated with L-344; L-
FT 353 and L-355."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 353
FT /note="V->A: Alterations in oligomer formation and in
FT hemolytic activity; when associated with A-332; A-334; A-
FT 336; A-351 and A-355. Alterations in oligomer formation and
FT in hemolytic activity; when associated with A-351 and A-
FT 355."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139"
FT MUTAGEN 353
FT /note="V->L: Increased antibacterial activity toward Gram-
FT negative bacteria E.coli ATCC 43827 and P.aeruginosa ATCC
FT 27853, and toward Gram-positive bacteria S.aureus IFO 12732
FT and B.subtilis IFO 3134 including increased permeability of
FT the S.aureus cell membrane; when associated with L-344; L-
FT 351 and L-355."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 354
FT /note="K->A: Decreased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732. Markedly increased
FT hemolytic activity compared to the wild-type protein. No
FT effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:14999010,
FT ECO:0000269|PubMed:23583369"
FT MUTAGEN 354
FT /note="K->R: Increased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732 and increased
FT permeability of the S.aureus cell membrane; when associated
FT with R-342; R-348 and R-361."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 355
FT /note="V->A: No effect on lactose binding. Alterations in
FT oligomer formation and in hemolytic activity; when
FT associated with A-332; A-334; A-336; A-351 and A-353.
FT Alterations in oligomer formation and in hemolytic
FT activity; when associated with A-351 and A-353."
FT /evidence="ECO:0000269|PubMed:17965430,
FT ECO:0000269|PubMed:19356139, ECO:0000269|PubMed:23583369"
FT MUTAGEN 355
FT /note="V->L: Increased antibacterial activity toward Gram-
FT negative bacteria E.coli ATCC 43827 and P.aeruginosa ATCC
FT 27853, and toward Gram-positive bacteria S.aureus IFO 12732
FT and B.subtilis IFO 3134 including increased permeability of
FT the S.aureus cell membrane; when associated with L-344; L-
FT 351 and L-353."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 360
FT /note="S->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 361
FT /note="K->A: Decreased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732. Markedly increased
FT hemolytic activity compared to the wild-type protein. No
FT effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:14999010,
FT ECO:0000269|PubMed:23545649, ECO:0000269|PubMed:23583369"
FT MUTAGEN 361
FT /note="K->R: Increased antibacterial activity toward Gram-
FT positive bacteria S.aureus IFO 12732 and increased
FT permeability of the S.aureus cell membrane; when associated
FT with R-342; R-348 and R-354."
FT /evidence="ECO:0000269|PubMed:14999010"
FT MUTAGEN 365
FT /note="N->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 375
FT /note="Y->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 381
FT /note="D->A: Alterations in hemolytic activity compared to
FT the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369,
FT ECO:0000269|PubMed:27101707"
FT MUTAGEN 381
FT /note="D->K: Almost no hemolytic activity."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 381
FT /note="D->R: 20% of the hemolytic activity of that of the
FT wild-type protein."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 385
FT /note="E->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 388
FT /note="R->A: Strongly decreased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 405
FT /note="D->A: No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 407
FT /note="L->A: No effect on oligomerization. No effect on
FT lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 413
FT /note="I->A: No effect on oligomerization. No effect on
FT lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 415
FT /note="K->A: 3.6-fold higher hemolytic activity compared to
FT the wild-type protein. No effect on oligomerization. No
FT effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369,
FT ECO:0000269|PubMed:27101707"
FT MUTAGEN 415
FT /note="K->E: Markedly decreased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 415
FT /note="K->L: Autoaggregates and cannot be refolded to a
FT soluble form."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 415
FT /note="K->R: Markedly decreased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 415
FT /note="K->S: Markedly increased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:27101707"
FT MUTAGEN 418
FT /note="R->A: Markedly decreased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 430
FT /note="K->A: Markedly increased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT MUTAGEN 435
FT /note="D->A: Markedly increased hemolytic activity compared
FT to the wild-type protein. No effect on lactose binding."
FT /evidence="ECO:0000269|PubMed:23583369"
FT CONFLICT 107
FT /note="A -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="I -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 64..87
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 115..123
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 139..144
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 197..199
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 201..204
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 217..225
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 246..248
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 264..272
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 330..342
FT /evidence="ECO:0007829|PDB:1VCL"
FT HELIX 353..364
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 373..376
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 383..385
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 387..400
FT /evidence="ECO:0007829|PDB:1VCL"
FT TURN 401..404
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 405..410
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 429..433
FT /evidence="ECO:0007829|PDB:1VCL"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1VCL"
SQ SEQUENCE 442 AA; 48456 MW; 3E47C608446D40EC CRC64;
MVSLVPCGFA QVLCTNPLDI GELRNYKSKQ CVDIVGNQGS GNIATHDCDG LSDQQIIMCG
DGTIRNEARN YCFTPDGSGN ANVMSSPCTL YPEIPSSQRW RLGRKKAFTD NGGIEQVATE
IINLASGKCL DVEGSDGTGD IGVYDCQNLD DQYFYIRSRG PELFYGRLRN EKSDLCLDVE
GSEGKGNVLM YSCEDNLDQW FRYYENGEIV NAKQGMCLDV EGSDGSGNVG IYRCDDLRDQ
MWSRPNAYCN GDYCSFLNKE SNKCLDVSGD QGTGDVGTWQ CDGLPDQRFK WVFDDWEVPT
ATWNMVGCDQ NGKVSQQISN TISFSSTVTA GVAVEVSSTI EKGVIFAKAS VSVKVTASLS
KAWTNSQSGT TAITYTCDNY DSDEEFTRGC MWQLAIETTE VKSGDLLVWN PQIIKCTRSN
TAPGCAPFTK CANEDCTFCT DI
