LEC_CREGR
ID LEC_CREGR Reviewed; 150 AA.
AC H2FH31;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Galactose-binding lectin {ECO:0000303|PubMed:27010847, ECO:0000303|PubMed:28740170};
DE AltName: Full=CGL {ECO:0000303|PubMed:26527272, ECO:0000303|PubMed:27010847, ECO:0000303|PubMed:28636877, ECO:0000303|PubMed:28740170, ECO:0000303|PubMed:30486373, ECO:0000303|PubMed:31905927, ECO:0000303|Ref.3};
DE AltName: Full=GalNAc/Gal-specific lectin {ECO:0000303|PubMed:23886951, ECO:0000303|PubMed:25482060, ECO:0000303|PubMed:26439416, ECO:0000303|PubMed:28740170, ECO:0000303|PubMed:30486373, ECO:0000303|PubMed:31905927, ECO:0000303|PubMed:9568372};
OS Crenomytilus grayanus (Gray mussel) (Mytilus grayanus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Crenomytilus.
OX NCBI_TaxID=151218;
RN [1] {ECO:0000312|EMBL:AEY80387.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-20; 30-50; 68-84;
RP 88-102; 106-110 AND 129-140, FUNCTION, ACTIVITY REGULATION, CIRCULAR
RP DICHROISM ANALYSIS, AND PHYLOGENETIC ANALYSIS.
RX PubMed=23886951; DOI=10.1016/j.fsi.2013.07.011;
RA Kovalchuk S.N., Chikalovets I.V., Chernikov O.V., Molchanova V.I., Li W.,
RA Rasskazov V.A., Lukyanov P.A.;
RT "cDNA cloning and structural characterization of a lectin from the mussel
RT Crenomytilus grayanus with a unique amino acid sequence and antibacterial
RT activity.";
RL Fish Shellfish Immunol. 35:1320-1324(2013).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9568372; DOI=10.1016/s0742-8413(97)00180-1;
RA Belogortseva N.I., Molchanova V.I., Kurika A.V., Skobun A.S.,
RA Glazkova V.E.;
RT "Isolation and characterization of new GalNAc/Gal-specific lectin from the
RT sea mussel Crenomytilus grayanus.";
RL Comp. Biochem. Physiol. 119C:45-50(1998).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND DOMAIN.
RA Chikalovets I.V., Molchanova V.I., Chernikov O.V., Lukyanov P.A.;
RT "Domain organization of lectin from the mussel Crenomytilus grayanus.";
RL Chem. Nat. Comp. 50:706-709(2014).
RN [4]
RP FUNCTION, ACTIVITY REGULATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=25482060; DOI=10.1016/j.fsi.2014.11.036;
RA Chikalovets I.V., Chernikov O.V., Pivkin M.V., Molchanova V.I.,
RA Litovchenko A.P., Li W., Lukyanov P.A.;
RT "A lectin with antifungal activity from the mussel Crenomytilus grayanus.";
RL Fish Shellfish Immunol. 42:503-507(2015).
RN [5]
RP FUNCTION, ACTIVITY REGULATION, MUTAGENESIS OF HIS-16; PRO-17; GLY-19;
RP HIS-64; PRO-65; GLY-67; HIS-108; PRO-109 AND GLY-111, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=26439416; DOI=10.1016/j.fsi.2015.09.045;
RA Kovalchuk S.N., Golotin V.A., Balabanova L.A., Buinovskaya N.S.,
RA Likhatskaya G.N., Rasskazov V.A.;
RT "Carbohydrate-binding motifs in a novel type lectin from the sea mussel
RT Crenomytilus grayanus: Homology modeling study and site-specific
RT mutagenesis.";
RL Fish Shellfish Immunol. 47:565-571(2015).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, AND BIOTECHNOLOGY.
RX PubMed=28636877; DOI=10.1016/j.ijbiomac.2017.06.074;
RA Chernikov O., Kuzmich A., Chikalovets I., Molchanova V., Hua K.F.;
RT "Lectin CGL from the sea mussel Crenomytilus grayanus induces Burkitt's
RT lymphoma cells death via interaction with surface glycan.";
RL Int. J. Biol. Macromol. 104:508-514(2017).
RN [7]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=28740170; DOI=10.1038/s41598-017-06647-5;
RA Chernikov O.V., Wong W.T., Li L.H., Chikalovets I.V., Molchanova V.I.,
RA Wu S.H., Liao J.H., Hua K.F.;
RT "A GalNAc/Gal-specific lectin from the sea mussel Crenomytilus grayanus
RT modulates immune response in macrophages and in mice.";
RL Sci. Rep. 7:6315-6315(2017).
RN [8]
RP FUNCTION, BIOTECHNOLOGY, MUTAGENESIS OF ASN-27; HIS-37; GLU-75; HIS-85;
RP ASN-119; ASP-127 AND HIS-129, IN SILICO ANALYSIS OF BINDING TO GALACTOSE;
RP GLOBOTRIOSE GB3 AND PORCINE STOMACH MUCIN TRISACCHARIDE, AND 3D-STRUCTURE
RP MODELING OF THE LIGAND BINDING SITE IN COMPLEX WITH GLOBOTRIOSE GB3 AND
RP PORCINE STOMACH MUCIN TRISACCHARIDE.
RX PubMed=30486373; DOI=10.3390/md16120471;
RA Kovalchuk S.N., Buinovskaya N.S., Likhatskaya G.N., Rasskazov V.A.,
RA Son O.M., Tekutyeva L.A., Balabanova L.A.;
RT "Mutagenesis Studies and Structure-function Relationships for GalNAc/Gal-
RT Specific Lectin from the Sea Mussel Crenomytilus grayanus.";
RL Mar. Drugs 16:0-0(2018).
RN [9]
RP FUNCTION, BIOTECHNOLOGY, AND REVIEW.
RX PubMed=31905927; DOI=10.3390/molecules25010150;
RA Chikalovets I., Filshtein A., Molchanova V., Mizgina T., Lukyanov P.,
RA Nedashkovskaya O., Hua K.F., Chernikov O.;
RT "Activity Dependence of a Novel Lectin Family on Structure and
RT Carbohydrate-Binding Properties.";
RL Molecules 25:0-0(2019).
RN [10] {ECO:0007744|PDB:5DUY}
RP X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS), AND SUBUNIT.
RX PubMed=26527272; DOI=10.1107/s2053230x15019858;
RA Jakob M., Lubkowski J., O'Keefe B.R., Wlodawer A.;
RT "Structure of a lectin from the sea mussel Crenomytilus grayanus (CGL).";
RL Acta Crystallogr. F Struct. Biol. Commun. 71:1429-1436(2015).
RN [11] {ECO:0007744|PDB:5F8S, ECO:0007744|PDB:5F8W, ECO:0007744|PDB:5F8Y, ECO:0007744|PDB:5F90}
RP X-RAY CRYSTALLOGRAPHY (1.08 ANGSTROMS) AND IN COMPLEX WITH GALACTOSE;
RP GALACTOSAMINE AND GLOBOTRIOSE GB3, FUNCTION, SUBUNIT, BIOTECHNOLOGY, NMR
RP SPECTROSCOPY, AND PHYLOGENETIC ANALYSIS.
RX PubMed=27010847; DOI=10.1021/jacs.6b00111;
RA Liao J.H., Chien C.T., Wu H.Y., Huang K.F., Wang I., Ho M.R., Tu I.F.,
RA Lee I.M., Li W., Shih Y.L., Wu C.Y., Lukyanov P.A., Hsu S.T., Wu S.H.;
RT "A Multivalent Marine Lectin from Crenomytilus grayanus Possesses Anti-
RT cancer Activity through Recognizing Globotriose Gb3.";
RL J. Am. Chem. Soc. 138:4787-4795(2016).
CC -!- FUNCTION: Galactose-binding lectin (PubMed:23886951, PubMed:27010847,
CC PubMed:9568372, PubMed:28636877). Binds both alpha and beta anomer of
CC galactose (Gal), but has a stronger interaction with the glycans having
CC alpha Gal at the non-reducing end and binds beta Gal weakly only in
CC highly branched glycans. Has high affinity to Galalpha1-4Galbeta1-
CC 4GlcNAc (PubMed:28636877). Binds N-acetyl-2-deoxy-2-amino-galactose (2-
CC deoxy-GalNAc) (PubMed:23886951, PubMed:9568372). Binds N-
CC acetylgalactosamine (GalNAc) (PubMed:26439416). Binds porcine stomach
CC mucin (PSM) with high affinity (PubMed:26439416, PubMed:30486373).
CC Binds galactosamine (PubMed:27010847). Binds laminin, bovine
CC submaxillary mucin (BSM), fibronectin, type I collagen and gelatin with
CC a decreasing affinity, respectively (Ref.3). Has hemagglutinating
CC activity towards human type A erythrocytes (PubMed:9568372,
CC PubMed:26439416, Ref.3). Hemagglutinates also human type 0, B and AB
CC erythrocytes as well as rabbit and mouse erythrocytes (PubMed:9568372).
CC Agglutinates both Gram-positive and Gram-negative bacteria including
CC B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254,
CC respectively. No agglutination activity towards Gram-positive
CC S.amurskyense CMM 3673. Has bacteriostatic activity on S.amurskyense
CC CMM 3673, B.subtilis ATCC 6633, S.aureus ATCC 21027 and E.coli 3254.
CC However, has no agglutination nor bacteriostatic activity on Gram-
CC negative C.scophthalmum CIP 104199 or A.troitsensis KMM 3674
CC (PubMed:23886951). Inhibits growth of fungi from the genera
CC Aspergillus, Penicillium, Trichoderma and st. Mycelia. Inhibits
CC germination of spores and hyphal growth of them (PubMed:25482060). Has
CC dose-dependent cytotoxic effect on the human globotriaosylceramide
CC (Gb3)-expressing Burkitt's lymphoma (Raji) cell line. Binds to Gb3 in
CC these cells leading to activation of caspase-9/3 and PARP
CC (PubMed:28636877). Has dose-dependent cytotoxic effect on the Gb3-
CC expressing human MCF-7 breast cancer cell line (PubMed:27010847). No
CC cytotoxic effect on myelogenous leukemia K562 cell line, which does not
CC express Gb3 (PubMed:28636877). Activates immune responses in mice and
CC increases cytokine production of TNF-alpha, IL-6 and MCP-1 in the serum
CC and the peritoneal lavage of mice. Induces TNF-alpha and IL-6 secretion
CC in mouse RAW264.7 macrophages, mouse bone marrow-derived macrophages,
CC human THP-1 macrophages, human peripheral blood mononuclear cells
CC (PBMCs) and human blood monocyte-derived macrophages. TNF-alpha
CC production in macrophages could not be inhibited by GalNAc, GalN or
CC Gal, indicating that induced cytokine production is separate from its
CC sugar binding activity. Increases intracellular reactive oxygen species
CC levels, expression and phosphorylation of protein kinases PKC
CC alpha/delta, expression of COX-2 and NF-kappaB, and activates the MAPK
CC pathway by increasing the phosphorylation of ERK1/2, JNK1/2 and p38 in
CC mouse RAW264.7 macrophages. Induces endotoxin tolerance in
CC lipopolysaccharide(LPS)-activated macrophages by down-regulating IRAK2
CC expression, reducing JNK1/2 phosphorylation and NF-kappaB activation.
CC Can slightly increase the bactericidal activity of RAW264.7 macrophages
CC (PubMed:28740170). Has DNA-binding activity (PubMed:27010847).
CC Recognizes pathogen-associated molecular patterns (PAMPs) and binds to
CC LPS from E.coli, but has only little binding to beta-1,3-glucan from
CC E.gracilis and peptidoglycan from S.aureus. Activates secretion of TNF-
CC alpha and IFN-gamma by the human peripheral blood cells (HPBCs)
CC (PubMed:31905927). May be involved in innate immunity acting as an
CC antibacterial and antifungal agent involved in the recognition and
CC clearance of pathogens (PubMed:23886951, PubMed:25482060,
CC PubMed:31905927). {ECO:0000269|PubMed:23886951,
CC ECO:0000269|PubMed:25482060, ECO:0000269|PubMed:26439416,
CC ECO:0000269|PubMed:27010847, ECO:0000269|PubMed:28636877,
CC ECO:0000269|PubMed:28740170, ECO:0000269|PubMed:30486373,
CC ECO:0000269|PubMed:31905927, ECO:0000269|PubMed:9568372,
CC ECO:0000269|Ref.3}.
CC -!- ACTIVITY REGULATION: Bacterial binding activity is inhibited by D-
CC galactose (PubMed:23886951). Hemagglutinating activity is independent
CC of divalent cations Ca2(+) or Mg2(+). It is strongly inhibited by N-
CC acetyl-D-galactosamine (GalNAc), D-galactose and D-talose, and to a
CC lesser extent by melibiose and raffinose. Also inhibited by
CC glycoprotein asialo-bovine submaxillary mucin (BSM). Not inhibited by
CC D-glucose, D-fucose, D-galactitol, N-acetyl-D-glucosamine or lactose
CC (PubMed:9568372, PubMed:26439416). Fungal binding activity is inhibited
CC by D-galactose (PubMed:25482060). Cytotoxic activity against Raji cell
CC line is completely inhibited by galactose, melibiose and raffinose, but
CC not by glucose or lactose (PubMed:28636877). Galactose inhibits binding
CC to laminin and BSM, but not to collagen, gelatin or fibronectin
CC (Ref.3). {ECO:0000269|PubMed:23886951, ECO:0000269|PubMed:25482060,
CC ECO:0000269|PubMed:26439416, ECO:0000269|PubMed:28636877,
CC ECO:0000269|PubMed:9568372, ECO:0000269|Ref.3}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 8-10 for the hemagglutinating activity of the
CC human erythrocytes. {ECO:0000269|PubMed:9568372};
CC Temperature dependence:
CC Hemagglutinating activity of the human erythrocytes is fully
CC maintained after heating at 50 degrees Celsius for 3 hours. The
CC activity is partially lost after heating at 55 degrees Celsius and
CC completely lost after heating at 65 degrees Celsius for 30 minutes.
CC {ECO:0000269|PubMed:9568372};
CC -!- SUBUNIT: Monomer in solution (PubMed:26527272). Homodimer in solution
CC (PubMed:27010847). Exists as a monomer in solution when a low
CC concentration (0.001 mg/ml) of it is present. Homodimers start to
CC appear at a concentration of 0.01 mg/ml and tetramers at a
CC concentration of 0.1 mg/ml (Ref.3). {ECO:0000269|PubMed:26527272,
CC ECO:0000269|PubMed:27010847, ECO:0000269|Ref.3}.
CC -!- TISSUE SPECIFICITY: Highly expressed in mantle and to a lesser extent
CC in muscle, hepatopancreas, gill and hemocytes.
CC {ECO:0000269|PubMed:25482060}.
CC -!- INDUCTION: Up-regulated in mantle by challenge of yeast P.pastoris
CC reaching the maximum level at 12 hours post challenge and recovering to
CC the original level at 24 hours post challenge.
CC {ECO:0000269|PubMed:25482060}.
CC -!- DOMAIN: Contains a collagen like domain, which probably promotes
CC oligomerization. {ECO:0000269|Ref.3}.
CC -!- BIOTECHNOLOGY: This protein may have potential in cancer diagnosis and
CC treatment (PubMed:28636877, PubMed:27010847, PubMed:30486373,
CC PubMed:31905927). A synthetic analog of this protein with enhanced
CC carbohydrate-binding properties may be designed for the purpose of
CC constructing a biosensor for cancer diagnostics or anticancer therapy
CC (PubMed:30486373). May potentially be used as an immune modulator in
CC mammals, because of its effects on macrophages and its ability to
CC promote secretion of cytokines (PubMed:28740170).
CC {ECO:0000305|PubMed:27010847, ECO:0000305|PubMed:28636877,
CC ECO:0000305|PubMed:28740170, ECO:0000305|PubMed:30486373,
CC ECO:0000305|PubMed:31905927}.
CC -!- MISCELLANEOUS: Cleavage of the collagen like domain may decrease the
CC agglutinating ability and alter carbohydrate-binding properties. The
CC function of this protein could potentially be regulated by proteolysis
CC in vivo. {ECO:0000305|Ref.3}.
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; JQ314213; AEY80387.1; -; mRNA.
DR PDB; 5DUY; X-ray; 2.12 A; A/B/C/D/E/F=1-150.
DR PDB; 5F8S; X-ray; 1.08 A; A/B=1-150.
DR PDB; 5F8W; X-ray; 1.56 A; A/B=1-150.
DR PDB; 5F8Y; X-ray; 1.70 A; A/B=1-150.
DR PDB; 5F90; X-ray; 1.64 A; A/B=1-150.
DR PDBsum; 5DUY; -.
DR PDBsum; 5F8S; -.
DR PDBsum; 5F8W; -.
DR PDBsum; 5F8Y; -.
DR PDBsum; 5F90; -.
DR SMR; H2FH31; -.
DR UniLectin; H2FH31; -.
DR PRIDE; H2FH31; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycoprotein; Hemagglutinin;
KW Lectin.
FT CHAIN 1..150
FT /note="Galactose-binding lectin"
FT /id="PRO_0000453467"
FT BINDING 16
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 19
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 27
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F90"
FT BINDING 35..37
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 64
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 67
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 75
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 83..85
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 108
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT BINDING 111
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0007744|PDB:5F8W"
FT BINDING 119
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F90"
FT BINDING 127..129
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27010847,
FT ECO:0007744|PDB:5F8W"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 16
FT /note="H->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-17 and A-
FT 19."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 17
FT /note="P->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-16 and A-
FT 19."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 19
FT /note="G->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-16 and A-
FT 17."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 27
FT /note="N->A: 5.9-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 37
FT /note="H->A: 1.4-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 64
FT /note="H->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-65 and A-
FT 67."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 65
FT /note="P->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-64 and A-
FT 67."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 67
FT /note="G->A: Loss of hemagglutinating and porcine stomach
FT mucin-binding activities; when associated with A-64 and A-
FT 65."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 75
FT /note="E->A: 3.2-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 85
FT /note="H->A: 5.0-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 108
FT /note="H->A: Retains slight hemagglutinating activity and
FT has 6-fold decreased porcine stomach mucin-binding
FT activity; when associated with A-109 and A-111."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 109
FT /note="P->A: Retains slight hemagglutinating activity and
FT has 6-fold decreased porcine stomach mucin-binding
FT activity; when associated with A-108 and A-111."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 111
FT /note="G->A: Retains slight hemagglutinating activity and
FT has 6-fold decreased porcine stomach mucin-binding
FT activity; when associated with A-108 and A-109."
FT /evidence="ECO:0000269|PubMed:26439416"
FT MUTAGEN 119
FT /note="N->A: 11.1-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 127
FT /note="D->A: 4.5-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT MUTAGEN 129
FT /note="H->A: 2.3-fold decreased porcine stomach mucin-
FT binding activity compared to wild-type."
FT /evidence="ECO:0000269|PubMed:30486373"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:5F8S"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:5F8S"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:5F8S"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:5F8S"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:5F8S"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5F8S"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:5F8S"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5F8S"
SQ SEQUENCE 150 AA; 17023 MW; 9DA43920298898C9 CRC64;
MTTFLIKHKA SGKFLHPYGG SSNPANNTKL VLHSDIHERM YFQFDVVDER WGYIKHVASG
KIVHPYGGQA NPPNETNMVL HQDRHDRALF AMDFFNDNIM HKGGKYIHPK GGSPNPPNNT
ETVIHGDKHA AMEFIFVSPK NKDKRVLVYA
