LEC1_MYTGA
ID LEC1_MYTGA Reviewed; 187 AA.
AC B3EWR1; A0A140KFU1;
DT 31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 2.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Alpha-D-galactose-binding lectin {ECO:0000303|PubMed:23093409, ECO:0000303|PubMed:27187419};
DE AltName: Full=Galactose-binding lectin {ECO:0000303|PubMed:27321048};
DE AltName: Full=Lectin {ECO:0000303|PubMed:23093409};
DE AltName: Full=MytiLec {ECO:0000303|PubMed:23093409, ECO:0000303|PubMed:26694420, ECO:0000303|PubMed:27321048};
DE AltName: Full=MytiLec-1 {ECO:0000303|PubMed:27187419};
DE AltName: Full=R-type lectin {ECO:0000303|PubMed:26694420, ECO:0000303|PubMed:27187419};
DE Flags: Precursor;
OS Mytilus galloprovincialis (Mediterranean mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=29158;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=27187419; DOI=10.3390/md14050092;
RA Hasan I., Gerdol M., Fujii Y., Rajia S., Koide Y., Yamamoto D.,
RA Kawsar S.M., Ozeki Y.;
RT "cDNA and Gene Structure of MytiLec-1, A Bacteriostatic R-Type Lectin from
RT the Mediterranean Mussel (Mytilus galloprovincialis).";
RL Mar. Drugs 14:0-0(2016).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 39-187, FUNCTION, MASS SPECTROMETRY, AND ACETYLATION AT
RP THR-39.
RC TISSUE=Mantle {ECO:0000269|PubMed:23093409};
RX PubMed=23093409; DOI=10.1074/jbc.m112.418012;
RA Fujii Y., Dohmae N., Takio K., Kawsar S.M., Matsumoto R., Hasan I.,
RA Koide Y., Kanaly R.A., Yasumitsu H., Ogawa Y., Sugawara S., Hosono M.,
RA Nitta K., Hamako J., Matsui T., Ozeki Y.;
RT "A lectin from the mussel Mytilus galloprovincialis has a highly novel
RT primary structure and induces glycan-mediated cytotoxicity of
RT globotriaosylceramide-expressing lymphoma cells.";
RL J. Biol. Chem. 287:44772-44783(2012).
RN [3]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=26694420; DOI=10.3390/md13127071;
RA Hasan I., Sugawara S., Fujii Y., Koide Y., Terada D., Iimura N.,
RA Fujiwara T., Takahashi K.G., Kojima N., Rajia S., Kawsar S.M., Kanaly R.A.,
RA Uchiyama H., Hosono M., Ogawa Y., Fujita H., Hamako J., Matsui T.,
RA Ozeki Y.;
RT "MytiLec, a Mussel R-Type Lectin, Interacts with Surface Glycan Gb3 on
RT Burkitt's Lymphoma Cells to Trigger Apoptosis through Multiple Pathways.";
RL Mar. Drugs 13:7377-7389(2015).
RN [4] {ECO:0000312|PDB:3WMU, ECO:0000312|PDB:3WMV}
RP X-RAY CRYSTALLOGRAPHY (1.05 ANGSTROMS) OF 39-187 AND IN COMPLEX WITH
RP N-ACETYL-ALPHA-D-GALACTOSAMINE, FUNCTION, SUBUNIT, BIOTECHNOLOGY, AND
RP MUTAGENESIS OF PHE-131 AND PHE-132.
RX PubMed=27321048; DOI=10.1038/srep28344;
RA Terada D., Kawai F., Noguchi H., Unzai S., Hasan I., Fujii Y., Park S.Y.,
RA Ozeki Y., Tame J.R.;
RT "Crystal structure of MytiLec, a galactose-binding lectin from the mussel
RT Mytilus galloprovincialis with cytotoxicity against certain cancer cell
RT types.";
RL Sci. Rep. 6:28344-28344(2016).
CC -!- FUNCTION: Alpha-D-galactose-binding lectin (PubMed:27187419,
CC PubMed:23093409, PubMed:27321048). Binds D-GalNAc, but not glucose or
CC its derivatives (PubMed:27321048). Has hemagglutinating activity
CC towards rabbit erythrocytes (PubMed:23093409, PubMed:27321048).
CC Agglutinates bacteria. Has bacteriostatic activity on both Gram-
CC positive and Gram-negative bacteria including B.subtilis, S.aureus,
CC E.coli and V.parahaemolyticus, respectively (PubMed:27187419). Has a
CC dose-dependent cytotoxic effect on the human globotriaosylceramide
CC (Gb3)-expressing Epstein-Barr virus (EBV)-positive Burkitt's lymphoma
CC (Raji) cell line (PubMed:23093409, PubMed:27321048). Has dose-dependent
CC cytotoxic effect on another Burkitt's lymphoma (Ramos) cell line, which
CC does not possess the EBV genome, but also expresses Gb3. Binds to Gb3
CC in these cells leading to phosphorylation of MEK1/2, ERK1/2, JNK and
CC p38 kinase, activation of caspase-9/3 and to expression of p21 and
CC tumor necrosis factor (TNF)-alpha (PubMed:26694420). No cytotoxic
CC effect on the human chronic myelogenous leukemia (K-562) cell line,
CC which does not express Gb3 (PubMed:23093409, PubMed:26694420). May be
CC involved in innate immunity acting as an antibacterial or antifungal
CC agent (PubMed:26694420, PubMed:27321048). May be a pattern recognition
CC receptor (PRR) involved in recognition of glycans found on parasitic or
CC symbiotic microorganisms (PubMed:27187419).
CC {ECO:0000269|PubMed:23093409, ECO:0000269|PubMed:26694420,
CC ECO:0000269|PubMed:27187419, ECO:0000269|PubMed:27321048}.
CC -!- ACTIVITY REGULATION: Agglutination of E.coli is inhibited by alpha-
CC galactoside melibiose, but not by beta-galactoside lactose.
CC {ECO:0000269|PubMed:27187419}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:27321048}.
CC -!- TISSUE SPECIFICITY: Highest expression in the posterior part of the
CC mantle. Highly expressed in gills and to a lesser extent in mid mantle
CC and anterior muscle. Lowest expression in digestive gland and posterior
CC adductor muscle. Scarcely detectable in hemocytes.
CC {ECO:0000269|PubMed:27187419}.
CC -!- MASS SPECTROMETRY: Mass=16812.59; Mass_error=10.63;
CC Method=Electrospray; Note=The mass determined is that of range 39-187.;
CC Evidence={ECO:0000269|PubMed:23093409};
CC -!- BIOTECHNOLOGY: This protein may have potential for the development of
CC new diagnostic agents or treatments for cancer since Gb3 is a cell-
CC surface marker expressed by several different cancer cell lines.
CC {ECO:0000305|PubMed:26694420, ECO:0000305|PubMed:27321048}.
CC -!- CAUTION: Was originally thought to be a monomer in solution on the
CC basis of gel filtration. {ECO:0000269|PubMed:23093409}.
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DR EMBL; LC125182; BAU68218.1; -; mRNA.
DR EMBL; UYJE01006457; VDI46190.1; -; Genomic_DNA.
DR PDB; 3WMU; X-ray; 1.10 A; A/B=39-187.
DR PDB; 3WMV; X-ray; 1.05 A; A/B=39-187.
DR PDBsum; 3WMU; -.
DR PDBsum; 3WMV; -.
DR AlphaFoldDB; B3EWR1; -.
DR SMR; B3EWR1; -.
DR UniLectin; B3EWR1; -.
DR iPTMnet; B3EWR1; -.
DR Proteomes; UP000596742; Unassembled WGS sequence.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Hemagglutinin;
KW Lectin; Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000305|PubMed:27187419"
FT CHAIN 38..187
FT /note="Alpha-D-galactose-binding lectin"
FT /id="PRO_0000420129"
FT BINDING 53..56
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 64
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 72..76
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 101
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 104
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 112
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 120..122
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 145
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 148
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 156
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT BINDING 164..166
FT /ligand="N-acetyl-alpha-D-galactosamine"
FT /ligand_id="ChEBI:CHEBI:40356"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:27321048,
FT ECO:0007744|PDB:3WMV"
FT SITE 38
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:23093409"
FT MOD_RES 39
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000269|PubMed:23093409"
FT MUTAGEN 131..132
FT /note="FF->DS: Loss of homodimerization. Weak
FT hemagglutinating activity. Loss of cytotoxic effect on the
FT Burkitt's lymphoma (Raji) cell line."
FT /evidence="ECO:0000269|PubMed:27321048"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:3WMV"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:3WMV"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 88..93
FT /evidence="ECO:0007829|PDB:3WMV"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:3WMV"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3WMV"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:3WMV"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:3WMV"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:3WMV"
SQ SEQUENCE 187 AA; 21083 MW; 644D7D7F6930CDD9 CRC64;
MTFAKQSCFN SIILLSIATS YFKIGHKISE LGNRIEKMTT FLIKHKASGK FLHPKGGSSN
PANDTNLVLH SDIHERMYFQ FDVVDERWGY IKHAASGKIV HPLGGKADPP NETKLVLHQD
RHDRALFAMD FFNDNIIHKA GKYVHPKGGS TNPPNETLTV MHGDKHGAME FIFVSPKNKD
KRVLVYV
