LEC_MYTTR
ID LEC_MYTTR Reviewed; 150 AA.
AC A0A0G2UGT2;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=D-galactose-binding lectin {ECO:0000303|PubMed:26802895};
DE AltName: Full=GalNAc/Gal-specific lectin {ECO:0000303|PubMed:26802895, ECO:0000303|PubMed:31905927, ECO:0000303|Ref.2, ECO:0000312|EMBL:AKI29293.1};
DE AltName: Full=MTL {ECO:0000303|PubMed:26802895, ECO:0000303|PubMed:30292806, ECO:0000303|PubMed:31905927, ECO:0000303|Ref.2};
OS Mytilus trossulus (Blue mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6551 {ECO:0000312|EMBL:AKI29293.1};
RN [1] {ECO:0000312|EMBL:AKI29293.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, TISSUE
RP SPECIFICITY, INDUCTION, PTM, AND CIRCULAR DICHROISM ANALYSIS.
RC TISSUE=Mantle {ECO:0000303|PubMed:26802895};
RX PubMed=26802895; DOI=10.1016/j.fsi.2016.01.020;
RA Chikalovets I.V., Kovalchuk S.N., Litovchenko A.P., Molchanova V.I.,
RA Pivkin M.V., Chernikov O.V.;
RT "A new Gal/GalNAc-specific lectin from the mussel Mytilus trossulus:
RT Structure, tissue specificity, antimicrobial and antifungal activity.";
RL Fish Shellfish Immunol. 50:27-33(2016).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RA Chikalovets I.V., Kondrashina A.S., Chernikov O.V., Molchanova V.I.,
RA Lukyanov P.A.;
RT "Isolation and general characteristics of lectin from the mussel Mytilus
RT trossulus.";
RL Chem. Nat. Comp. 48:1058-1061(2013).
RN [3]
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 [4]
RP FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=30292806; DOI=10.1016/j.pep.2018.10.003;
RA Golotin V.A., Filshtein A.P., Chikalovets I.V., Yu K.N., Molchanova V.I.,
RA Chernikov O.V.;
RT "Expression and purification of a new lectin from mussel Mytilus
RT trossulus.";
RL Protein Expr. Purif. 154:62-65(2019).
CC -!- FUNCTION: D-galactose-binding lectin (PubMed:26802895, Ref.2). Binds
CC both alpha and beta anomer of galactose (Gal). Binds strongly to
CC branched beta-Gal-terminated glycans and weakly to unbranched glycans
CC with alpha-Gal on the end of chains (PubMed:31905927). Has strong
CC affinity for both Gal and GalNAc. Binds glycoproteins containing mucin-
CC type chains. Has hemagglutinating activity towards human group A
CC erythrocytes (Ref.2). Has hemagglutinating activity towards rabbit
CC erythrocytes (PubMed:30292806). Agglutinates V.proteolyticus bacteria.
CC Binds strongly to fungi including species from genera Aspergillus,
CC Alternaria, Fusarium and Haematonectria, and to a lesser extent to
CC fungi from genera Trichoderma. Decreases conidia germination and hyphal
CC growth of fungi (PubMed:26802895). At high concentration, stimulates
CC secretion of cytokines TNF-alpha and IFN-gamma from human peripheral
CC blood cells, and at low concentration reduces hyperexpression of
CC cytokine IL-10 in these cells, indicative of immunomodulatory
CC capability. However, has no effect on IL-4 production (Ref.2).
CC Recognizes pathogen-associated molecular patterns (PAMPs) and binds to
CC peptidoglycan from S.aureus, but has only little binding to beta-1,3-
CC glucan from E.gracilis and lipopolysaccharide (LPS) from E.coli
CC (PubMed:31905927). May be involved in innate immunity acting as an
CC antibacterial or antifungal agent recognizing carbohydrate ligands on
CC the surface of pathogens (PubMed:26802895, PubMed:31905927).
CC {ECO:0000269|PubMed:26802895, ECO:0000269|PubMed:30292806,
CC ECO:0000269|PubMed:31905927, ECO:0000269|Ref.2}.
CC -!- ACTIVITY REGULATION: Hemagglutinating activity does not require Ca(2+)
CC ions. Hemagglutinating activity is inhibited by porcine stomach mucin
CC (PSM), bovine submaxillary mucin (BSM) and fetuin (Ref.2).
CC Agglutination of V.proteolyticus bacteria is inhibited by D-galactose,
CC but not by D-glucose. Fungal binding is inhibited by D-galactose, but
CC not by pathogen-associated molecular patterns (PAMPs) including
CC lipopolysaccharide (LPS), peptidoglycan and beta-glucan
CC (PubMed:26802895). {ECO:0000269|PubMed:26802895, ECO:0000269|Ref.2}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 9-10 for hemagglutinating activity. The activity is
CC decreased by 25% at pH 6.0 and by 50% at pH 4.0. {ECO:0000269|Ref.2};
CC Temperature dependence:
CC Thermally labile. Complete loss of hemagglutinating activity after
CC incubation at 60 degrees Celsius for 30 min. {ECO:0000269|Ref.2};
CC -!- SUBUNIT: Oligomerizes in solution. {ECO:0000269|PubMed:30292806}.
CC -!- TISSUE SPECIFICITY: Expressed in mantle (PubMed:26802895, Ref.2,
CC PubMed:30292806). Expressed 51 and 1.6 fold in mantle and gonads,
CC respectively, relative to that in hemocytes. Expressed at a much lower
CC level in other tissues tested including gill, muscle and hepatopancreas
CC (PubMed:26802895). {ECO:0000269|PubMed:26802895,
CC ECO:0000269|PubMed:30292806, ECO:0000269|Ref.2}.
CC -!- INDUCTION: Up-regulated expression in the mantle following
CC V.proteolyticus bacterial challenge reaching the maximum expression at
CC 24 hours (about 1.5-fold) post-injection and then decreasing back to
CC the initial level at 48 hours post-injection.
CC {ECO:0000269|PubMed:26802895}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:26802895}.
CC -!- BIOTECHNOLOGY: This protein may have potential in cancer diagnosis and
CC treatment. {ECO:0000305|PubMed:31905927}.
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DR EMBL; KR019779; AKI29293.1; -; mRNA.
DR SMR; A0A0G2UGT2; -.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
DR GO; GO:0042834; F:peptidoglycan binding; IDA:UniProtKB.
DR GO; GO:0098630; P:aggregation of unicellular organisms; IDA:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0016045; P:detection of bacterium; IDA:UniProtKB.
DR GO; GO:0034117; P:erythrocyte aggregation; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IC:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
DR GO; GO:0140460; P:response to Gram-negative bacterium; IEP:UniProtKB.
PE 1: Evidence at protein level;
KW Glycoprotein; Hemagglutinin; Lectin.
FT CHAIN 1..150
FT /note="D-galactose-binding lectin"
FT /id="PRO_0000453718"
FT BINDING 16
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 19
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 35..37
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 64
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 67
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 83..85
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 108
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 111
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
FT BINDING 127..129
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:H2FH31"
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"
SQ SEQUENCE 150 AA; 17111 MW; 1EFCF4ACA24F3A08 CRC64;
MTTFLIKHKA SGKYFHPKGG TSNPPNGTNL VLHSDIHERM YFQFEVVNER WRYIKHVASE
KIVHPFGGKA DPLNGTNMVL HQDRHDRALF AMDFFNDNIR HKGGKYIHPK GGSKNPSNGN
LTVMHGDEHG AMEFIFVSPK NKDKRVLVYA
