LEC_MYTCA
ID LEC_MYTCA Reviewed; 150 AA.
AC A0A0P0E482;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Galactose-binding lectin {ECO:0000303|PubMed:28546025};
DE AltName: Full=MCL {ECO:0000303|PubMed:28546025};
OS Mytilus californianus (California mussel).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae; Mytilinae;
OC Mytilus.
OX NCBI_TaxID=6549 {ECO:0000312|EMBL:ALJ32152.1};
RN [1] {ECO:0007744|PDB:5VBK}
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (1.79 ANGSTROMS),
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MASS
RP SPECTROMETRY, GLYCOSYLATION, AND CIRCULAR DICHROISM ANALYSIS.
RX PubMed=28546025; DOI=10.1016/j.fsi.2017.05.057;
RA Garcia-Maldonado E., Cano-Sanchez P., Hernandez-Santoyo A.;
RT "Molecular and functional characterization of a glycosylated Galactose-
RT Binding lectin from Mytilus californianus.";
RL Fish Shellfish Immunol. 66:564-574(2017).
CC -!- FUNCTION: D-galactose-binding lectin. Binds also N-acetyl-D-
CC galactosamine. Has hemagglutination activity towards all types of human
CC erythrocytes (O, A and B) and rabbit erythrocytes. Agglutinates Gram-
CC negative and Gram-positive bacteria including E.coli DH5-alpha and
CC L.plantarum ATCC8014, respectively, and has bacteriostatic activity
CC against them. Agglutinates also M.lysodeikticus. May be involved in
CC innate immunity by recognizing and eliminating pathogens.
CC {ECO:0000269|PubMed:28546025}.
CC -!- ACTIVITY REGULATION: Hemagglutination activity is not dependent on
CC divalent cations. Hemagglutination activity is highly inhibited by D-
CC galactose and N-acetyl-D-galactosamine, and to a lesser extent by
CC raffinose. Also inhibited by melibiose and alpha-lactose, but not by
CC beta-lactose or D-glucose. {ECO:0000269|PubMed:28546025}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum hemagglutination activity at pH 7.4. Retains its
CC hemagglutination activity throughout pH range 3-10. This protein is
CC most stable at pH 7.4. {ECO:0000269|PubMed:28546025};
CC Temperature dependence:
CC Optimum hemagglutination activity between 37 and 40 degrees Celsius.
CC Retains its hemagglutination activity up to 60 degrees Celsius, but
CC loses the activity at higher temperatures. This protein is stable at
CC high temperatures over 80 degrees Celsius. The thermal stability is
CC increased by the presence of ligand D-galactose.
CC {ECO:0000269|PubMed:28546025};
CC -!- SUBUNIT: Homodimer. Likely to form large oligomers; oligomerization
CC enhances hemagglutination activity. {ECO:0000269|PubMed:28546025}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:28546025}.
CC -!- MASS SPECTROMETRY: Mass=18007; Method=MALDI; Note=Glycosylated form.;
CC Evidence={ECO:0000269|PubMed:28546025};
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DR EMBL; KT695159; ALJ32152.1; -; mRNA.
DR PDB; 5VBK; X-ray; 1.79 A; A/B=1-150.
DR PDB; 6BFM; X-ray; 1.49 A; A/B=1-150.
DR PDBsum; 5VBK; -.
DR PDBsum; 6BFM; -.
DR SMR; A0A0P0E482; -.
DR UniLectin; A0A0P0E482; -.
DR GO; GO:0005534; F:galactose binding; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Hemagglutinin; Lectin.
FT CHAIN 1..150
FT /note="Galactose-binding lectin"
FT /id="PRO_0000453468"
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 27
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="2"
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 75
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="3"
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 119
FT /ligand="D-galactose"
FT /ligand_id="ChEBI:CHEBI:4139"
FT /ligand_label="1"
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"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6BFM"
FT TURN 9..11
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:6BFM"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 51..56
FT /evidence="ECO:0007829|PDB:6BFM"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:6BFM"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5VBK"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:6BFM"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:6BFM"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:6BFM"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:6BFM"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:6BFM"
SQ SEQUENCE 150 AA; 16911 MW; 453E79EDF2E3342C CRC64;
MTTFLIKHKA SGKFLHPKGG SSNPANDTNL VLHSDIHERM YFQFDVVDER WGYIKHAASG
KIVHPLGGKA DPPNETKLVL HQDRHDRALF AMDFFNDNII HKAGKYVHPK GGSTNPPNET
LTVMHGDKHG AMEFIFVSPK NKDKRVLVYV
