MALS_MAAAM
ID MALS_MAAAM Reviewed; 287 AA.
AC P0DKL3;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 18-JAN-2017, sequence version 1.
DT 03-AUG-2022, entry version 16.
DE RecName: Full=Seed leukoagglutinin {ECO:0000303|PubMed:9163528};
DE AltName: Full=Leukoagglutinating lectin MAL {ECO:0000303|PubMed:1985926};
DE AltName: Full=Seed leucoagglutinin {ECO:0000305};
DE Flags: Precursor;
GN Name=MAL {ECO:0000303|PubMed:1985926};
OS Maackia amurensis (Amur maackia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Sophoreae; Maackia.
OX NCBI_TaxID=37501;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-55; 74-176 AND 187-253,
RP SUBUNIT, AND GLYCOSYLATION AT ASN-90; ASN-142; ASN-208 AND ASN-220.
RC TISSUE=Seed;
RX PubMed=9163528; DOI=10.1093/oxfordjournals.jbchem.a021650;
RA Yamamoto K., Konami Y., Irimura T.;
RT "Sialic acid-binding motif of Maackia amurensis lectins.";
RL J. Biochem. 121:756-761(1997).
RN [2]
RP FUNCTION.
RC TISSUE=Seed;
RX PubMed=3350806; DOI=10.1016/s0021-9258(18)68821-0;
RA Wang W.C., Cummings R.D.;
RT "The immobilized leukoagglutinin from the seeds of Maackia amurensis binds
RT with high affinity to complex-type Asn-linked oligosaccharides containing
RT terminal sialic acid-linked alpha-2,3 to penultimate galactose residues.";
RL J. Biol. Chem. 263:4576-4585(1988).
RN [3]
RP FUNCTION.
RC TISSUE=Seed;
RX PubMed=1985926; DOI=10.1016/s0021-9258(18)52405-4;
RA Knibbs R.N., Goldstein I.J., Ratcliffe R.M., Shibuya N.;
RT "Characterization of the carbohydrate binding specificity of the
RT leukoagglutinating lectin from Maackia amurensis. Comparison with other
RT sialic acid-specific lectins.";
RL J. Biol. Chem. 266:83-88(1991).
RN [4]
RP FUNCTION, AND GLYCOSYLATION.
RC TISSUE=Seed;
RX PubMed=26003537; DOI=10.1016/j.bbagen.2015.05.011;
RA Kim B.S., Hwang H.S., Park H., Kim H.H.;
RT "Effects of selective cleavage of high-mannose-type glycans of Maackia
RT amurensis leukoagglutinin on sialic acid-binding activity.";
RL Biochim. Biophys. Acta 1850:1815-1821(2015).
RN [5]
RP GLYCOSYLATION AT ASN-90; ASN-142; ASN-208 AND ASN-220, PROTEOLYTIC
RP PROCESSING OF C-TERMINUS, SUBUNIT, DISULFIDE BOND, AND PARTIAL PROTEIN
RP SEQUENCE.
RX PubMed=27720757; DOI=10.1016/j.ijbiomac.2016.10.007;
RA Gnanesh Kumar B.S., Surolia A.;
RT "Comprehensive analysis of alpha 2-3-linked sialic acid specific Maackia
RT amurensis leukagglutinin reveals differentially occupied N-glycans and C-
RT terminal processing.";
RL Int. J. Biol. Macromol. 94:114-121(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 30-268 IN COMPLEX WITH CALCIUM;
RP SIALYLLACTOSE AND MANGANESE, GLYCOSYLATION AT ASN-90; ASN-142 AND ASN-208,
RP AND SUBUNIT.
RX PubMed=10747930; DOI=10.1074/jbc.m000560200;
RA Imberty A., Gautier C., Lescar J., Perez S., Wyns L., Loris R.;
RT "An unusual carbohydrate binding site revealed by the structures of two
RT Maackia amurensis lectins complexed with sialic acid-containing
RT oligosaccharides.";
RL J. Biol. Chem. 275:17541-17548(2000).
CC -!- FUNCTION: Sialic acid-binding lectin recognizing oligosaccharides
CC containing terminal sialic acid linked via alpha-2,3 bond to
CC penultimate galactose residues (PubMed:3350806). Binds the
CC trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,4-GlcNAc
CC (PubMed:1985926). Binds fetuin when fully glycosylated but not when the
CC high mannose-type glycans are removed, although the secondary structure
CC is virtually unaffected by deglycosylation of the high mannose-type
CC glycans (PubMed:26003537). The lectin activity may depend on the
CC presence of a single GlcNAc attached to N-90 (PubMed:26003537).
CC {ECO:0000269|PubMed:1985926, ECO:0000269|PubMed:26003537,
CC ECO:0000269|PubMed:3350806}.
CC -!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9163528, PubMed:27720757).
CC Dimer of homodimers (PubMed:10747930). {ECO:0000269|PubMed:10747930,
CC ECO:0000269|PubMed:27720757, ECO:0000305|PubMed:9163528}.
CC -!- PTM: The glycosylation on N-90 is determined to by of the high mannose
CC type in PubMed:26003537, while PubMed:27720757 found a paucimannose at
CC this position. {ECO:0000269|PubMed:26003537,
CC ECO:0000269|PubMed:27720757}.
CC -!- PTM: Processed at its C-terminus. {ECO:0000269|PubMed:27720757}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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 PIR; JC5444; JC5444.
DR PDB; 1DBN; X-ray; 2.75 A; A/B=30-268.
DR PDBsum; 1DBN; -.
DR AlphaFoldDB; P0DKL3; -.
DR SMR; P0DKL3; -.
DR IntAct; P0DKL3; 1.
DR UniLectin; P0DKL3; -.
DR iPTMnet; P0DKL3; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016363; L-lectin.
DR InterPro; IPR000985; Lectin_LegA_CS.
DR InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Lectin; Manganese; Metal-binding; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:9163528"
FT CHAIN 30..278
FT /note="Seed leukoagglutinin"
FT /id="PRO_0000438710"
FT PROPEP 279..287
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:27720757"
FT /id="PRO_0000438711"
FT BINDING 74
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 116
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 133
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 136
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 156
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 158
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 160
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 166
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT BINDING 253
FT /ligand="N-acetyl-alpha-neuraminyl-(2->3)-beta-D-
FT galactosyl-(1->4)-beta-D-glucose"
FT /ligand_id="ChEBI:CHEBI:59226"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0007744|PDB:1DBN"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0000269|PubMed:27720757, ECO:0000305|PubMed:9163528,
FT ECO:0007744|PDB:1DBN"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0000269|PubMed:27720757, ECO:0000305|PubMed:9163528,
FT ECO:0007744|PDB:1DBN"
FT CARBOHYD 208
FT /note="N-linked (GlcNAc...) (high mannose) asparagine;
FT partial"
FT /evidence="ECO:0000269|PubMed:27720757,
FT ECO:0000305|PubMed:9163528"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) (paucimannose) asparagine;
FT partial"
FT /evidence="ECO:0000269|PubMed:10747930,
FT ECO:0000269|PubMed:27720757, ECO:0000305|PubMed:9163528,
FT ECO:0007744|PDB:1DBN"
FT DISULFID 272
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:27720757,
FT ECO:0000305|PubMed:9163528"
SQ SEQUENCE 287 AA; 31286 MW; BE84411950B0BA7E CRC64;
MATSNSKPTQ VLLATFLTFF FLLLNNVNSS DELSFTINNF VPNEADLLFQ GEASVSSTGV
LQLTRVENGQ PQKYSVGRAL YAAPVRIWDN TTGSVASFST SFTFVVKAPN PDITSDGLAF
YLAPPDSQIP SGSVSKYLGL FNNSNSDSSN QIVAVELDTY FAHSYDPWDP NYRHIGIDVN
GIESIKTVQW DWINGGVAFA TITYLAPNKT LIASLVYPSN QTTFSVAASV DLKEILPEWV
RVGFSAATGY PTEVETHDVL SWSFTSTLEA NCDAATENNV HIARYTA
