LECS1_MYTVI
ID LECS1_MYTVI Reviewed; 129 AA.
AC A0A646QV53;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 22-APR-2020, sequence version 1.
DT 03-AUG-2022, entry version 9.
DE RecName: Full=GM1b/asialo-GM1 oligosaccharide-binding R-type lectin {ECO:0000303|PubMed:31769916, ECO:0000303|PubMed:33328520};
DE AltName: Full=R-type lectin 1 {ECO:0000312|EMBL:QBM06340.1};
DE AltName: Full=SeviL {ECO:0000303|PubMed:31769916, ECO:0000303|PubMed:33328520};
DE AltName: Full=SeviL-1 {ECO:0000303|PubMed:31769916};
OS Mytilisepta virgata (Purplish bifurcate mussel) (Tichogonia virgata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Mytilida; Mytiloidea; Mytilidae;
OC Brachidontinae; Mytilisepta.
OX NCBI_TaxID=2547956;
RN [1] {ECO:0000312|EMBL:QBM06340.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 104-115, FUNCTION, ACTIVITY
RP REGULATION, SUBUNIT, TISSUE SPECIFICITY, BIOTECHNOLOGY, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=31769916; DOI=10.1111/febs.15154;
RA Fujii Y., Gerdol M., Kawsar S.M.A., Hasan I., Spazzali F., Yoshida T.,
RA Ogawa Y., Rajia S., Kamata K., Koide Y., Sugawara S., Hosono M.,
RA Tame J.R.H., Fujita H., Pallavicini A., Ozeki Y.;
RT "A GM1b/asialo-GM1 oligosaccharide-binding R-type lectin from purplish
RT bifurcate mussels Mytilisepta virgata and its effect on MAP kinases.";
RL FEBS J. 287:2612-2630(2019).
RN [2] {ECO:0000312|PDB:6LF1, ECO:0000312|PDB:6LF2}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) AND IN COMPLEX WITH OLIGOSACCHARIDE
RP OF ASIALO-GM1, FUNCTION, ACTIVITY REGULATION, SUBUNIT, BIOTECHNOLOGY, AND
RP MUTAGENESIS OF GLN-12; ASP-39 AND PHE-126.
RX PubMed=33328520; DOI=10.1038/s41598-020-78926-7;
RA Kamata K., Mizutani K., Takahashi K., Marchetti R., Silipo A., Addy C.,
RA Park S.Y., Fujii Y., Fujita H., Konuma T., Ikegami T., Ozeki Y.,
RA Tame J.R.H.;
RT "The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the
RT mussel Mytilisepta virgata.";
RL Sci. Rep. 10:22102-22102(2020).
CC -!- FUNCTION: Galbeta1-3GalNAcbeta1-4Galbeta1-4Glc oligosaccharide-binding
CC lectin. Binds strongly to the oligosaccharides of ganglioside GM1b and
CC to a lesser extent its precursor asialo-GM1 (PubMed:31769916,
CC PubMed:33328520). Binds weakly to asialo-GM2 oligosaccharide and to the
CC glycan moiety of globo-series stage-specific embryonal antigen 4 (SSEA-
CC 4) hexaose (PubMed:31769916). Binds galactose, N-acetylgalactose and
CC lactose. Does not bind GM1 (PubMed:33328520). Does not bind to Gal-
CC beta1,3-GalNAc (Thomsen-Friedenreich antigen), the oligosaccharide of
CC GM1a ganglioside or SSEA-4 tetraose. Does not bind to N-glycans, O-
CC glycans or glycosaminoglycans of glycoproteins. Does not bind Lewis
CC glycans, derivatives of lactose or N-acetyllactosamine or blood group
CC (ABH-type) oligosaccharides (PubMed:31769916). Does not bind glucose
CC (PubMed:33328520). Has hemagglutination activity towards rabbit
CC erythrocytes (PubMed:31769916, PubMed:33328520). Displays cytotoxic
CC effects against various cultured cell lines including human breast
CC (MCF7), cervical (HeLa) and colon cancer (Caco2) cell lines, as well as
CC dog kidney (MDCK) cell line that express asialo-GM1 oligosaccharide at
CC their cell surface. Shows dose- and time-dependent activation of
CC MKK3/6, ERK1/2 and p38 MAPK, as well as caspase-3/9 in HeLa cervical
CC cancer cells. No cytotoxic effect on BT474 human breast cancer cell
CC line. May be involved in recognition of glycans found on parasitic or
CC symbiotic microorganisms (PubMed:31769916).
CC {ECO:0000269|PubMed:31769916, ECO:0000269|PubMed:33328520}.
CC -!- ACTIVITY REGULATION: Hemagglutination activity requires divalent
CC cations such as Ca(2+) (PubMed:31769916, PubMed:33328520).
CC Hemagglutination activity is weakly inhibited by monosaccharides such
CC as D-Gal (25 mM), D-GalNAc (25 mM) and D-Fuc (25 mM) and by
CC disaccharides such as melibiose (25 mM) and lactose (25 mM).
CC Hemagglutination activity is inhibited by bovine submaxillary mucin,
CC but not by porcine stomach mucin or fetuin (PubMed:31769916).
CC {ECO:0000269|PubMed:31769916, ECO:0000269|PubMed:33328520}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:31769916,
CC ECO:0000269|PubMed:33328520}.
CC -!- TISSUE SPECIFICITY: Highest expression in the outer part of the mantle
CC rim. Highly expressed in gills, with a much lower expression in the
CC digestive gland and posterior adductor muscle. Scarcely detectable in
CC foot. {ECO:0000269|PubMed:31769916}.
CC -!- BIOTECHNOLOGY: This protein has potential for the detection and control
CC of certain cancer cells and cells of the immune system, that display
CC asialo-GM1 (PubMed:33328520). Has potential clinical applications since
CC it recognizes glycans expressed specifically by the target antigen for
CC Guillain-Barre syndrome (GM1b), natural killer (NK) cells and basophils
CC (asialo-GM1) and glioblastoma multiforme (SSEA-4) in vertebrates
CC (PubMed:31769916). {ECO:0000305|PubMed:31769916,
CC ECO:0000305|PubMed:33328520}.
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DR EMBL; MK434191; QBM06340.1; -; mRNA.
DR PDB; 6LF1; X-ray; 1.70 A; A/B=1-129.
DR PDB; 6LF2; X-ray; 1.60 A; A/B=1-129.
DR PDBsum; 6LF1; -.
DR PDBsum; 6LF2; -.
DR SMR; A0A646QV53; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR SUPFAM; SSF50370; SSF50370; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hemagglutinin; Lectin.
FT CHAIN 1..129
FT /note="GM1b/asialo-GM1 oligosaccharide-binding R-type
FT lectin"
FT /id="PRO_0000453280"
FT BINDING 21..23
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:33328520,
FT ECO:0007744|PDB:6LF2"
FT BINDING 26..28
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:33328520,
FT ECO:0007744|PDB:6LF2"
FT BINDING 32
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:33328520,
FT ECO:0007744|PDB:6LF2"
FT BINDING 37..40
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:33328520,
FT ECO:0007744|PDB:6LF2"
FT MUTAGEN 12
FT /note="Q->R: Loss of hemagglutination. Loss of
FT homodimerization, but retains saccharide binding; when
FT associated with K-126."
FT /evidence="ECO:0000269|PubMed:33328520"
FT MUTAGEN 39
FT /note="D->H: Loss of hemagglutination."
FT /evidence="ECO:0000269|PubMed:33328520"
FT MUTAGEN 126
FT /note="F->K: Loss of hemagglutination. Loss of
FT homodimerization, but retains saccharide binding; when
FT associated with R-12."
FT /evidence="ECO:0000269|PubMed:33328520"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6LF2"
FT TURN 14..16
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 19..23
FT /evidence="ECO:0007829|PDB:6LF2"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:6LF2"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 42..46
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:6LF2"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:6LF2"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 110..116
FT /evidence="ECO:0007829|PDB:6LF2"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:6LF2"
FT STRAND 123..127
FT /evidence="ECO:0007829|PDB:6LF2"
SQ SEQUENCE 129 AA; 15047 MW; 149CC6B3A03C7562 CRC64;
MSSVTIGKCY IQNRENGGRA FYNLGRKDLG IFTGKMYDDQ IWSFQKSDTP GYYTIGRESK
FLQYNGEQVI MSDIEQDTTL WSLEEVPEDK GFYRLLNKVH KAYLDYNGGD LVANKHQTES
EKWILFKAY
