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Seed leukoagglutinin (Leukoagglutinating lectin MAL) (Seed leucoagglutinin)

 MALS_MAAAM              Reviewed;         287 AA.
P0DKL3;
18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
18-JAN-2017, sequence version 1.
18-JUL-2018, entry version 8.
RecName: Full=Seed leukoagglutinin {ECO:0000303|PubMed:9163528};
AltName: Full=Leukoagglutinating lectin MAL {ECO:0000303|PubMed:1985926};
AltName: Full=Seed leucoagglutinin {ECO:0000305};
Flags: Precursor;
Name=MAL {ECO:0000303|PubMed:1985926};
Maackia amurensis (Amur maackia).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Sophoreae; Maackia.
NCBI_TaxID=37501;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-55; 74-176 AND
187-253, SUBUNIT, AND GLYCOSYLATION AT ASN-90; ASN-142; ASN-208 AND
ASN-220.
TISSUE=Seed;
PubMed=9163528; DOI=10.1093/oxfordjournals.jbchem.a021650;
Yamamoto K., Konami Y., Irimura T.;
"Sialic acid-binding motif of Maackia amurensis lectins.";
J. Biochem. 121:756-761(1997).
[2]
FUNCTION.
TISSUE=Seed;
PubMed=3350806;
Wang W.C., Cummings R.D.;
"The immobilized leukoagglutinin from the seeds of Maackia amurensis
binds with high affinity to complex-type Asn-linked oligosaccharides
containing terminal sialic acid-linked alpha-2,3 to penultimate
galactose residues.";
J. Biol. Chem. 263:4576-4585(1988).
[3]
FUNCTION.
TISSUE=Seed;
PubMed=1985926;
Knibbs R.N., Goldstein I.J., Ratcliffe R.M., Shibuya N.;
"Characterization of the carbohydrate binding specificity of the
leukoagglutinating lectin from Maackia amurensis. Comparison with
other sialic acid-specific lectins.";
J. Biol. Chem. 266:83-88(1991).
[4]
FUNCTION, AND GLYCOSYLATION.
TISSUE=Seed;
PubMed=26003537; DOI=10.1016/j.bbagen.2015.05.011;
Kim B.S., Hwang H.S., Park H., Kim H.H.;
"Effects of selective cleavage of high-mannose-type glycans of Maackia
amurensis leukoagglutinin on sialic acid-binding activity.";
Biochim. Biophys. Acta 1850:1815-1821(2015).
[5]
GLYCOSYLATION AT ASN-90; ASN-142; ASN-208 AND ASN-220, PROTEOLYTIC
PROCESSING OF C-TERMINUS, SUBUNIT, DISULFIDE BOND, AND PARTIAL PROTEIN
SEQUENCE.
PubMed=27720757; DOI=10.1016/j.ijbiomac.2016.10.007;
Gnanesh Kumar B.S., Surolia A.;
"Comprehensive analysis of alpha 2-3-linked sialic acid specific
Maackia amurensis leukagglutinin reveals differentially occupied N-
glycans and C-terminal processing.";
Int. J. Biol. Macromol. 94:114-121(2016).
[6]
X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 30-268 IN COMPLEX WITH
CALCIUM; SIALYLLACTOSE AND MANGANESE, GLYCOSYLATION AT ASN-90; ASN-142
AND ASN-208, AND SUBUNIT.
PubMed=10747930; DOI=10.1074/jbc.M000560200;
Imberty A., Gautier C., Lescar J., Perez S., Wyns L., Loris R.;
"An unusual carbohydrate binding site revealed by the structures of
two Maackia amurensis lectins complexed with sialic acid-containing
oligosaccharides.";
J. Biol. Chem. 275:17541-17548(2000).
-!- FUNCTION: Sialic acid-binding lectin recognizing oligosaccharides
containing terminal sialic acid linked via alpha-2,3 bond to
penultimate galactose residues (PubMed:3350806). Binds the
trisaccharide sequence Neu5Ac-alpha-2,3-Gal-beta-1,4-GlcNAc
(PubMed:1985926). Binds fetuin when fully glycosylated but not
when the high mannose-type glycans are removed, although the
secondary structure is virtually unaffected by deglycosylation of
the high mannose-type glycans (PubMed:26003537). The lectin
activity may depend on the presence of a single GlcNAc attached to
N-90 (PubMed:26003537). {ECO:0000269|PubMed:1985926,
ECO:0000269|PubMed:26003537, ECO:0000269|PubMed:3350806}.
-!- SUBUNIT: Homodimer; disulfide-linked (PubMed:9163528,
PubMed:27720757). Dimer of homodimers (PubMed:10747930).
{ECO:0000269|PubMed:10747930, ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
-!- PTM: The glycosylation on N-90 is determined to by of the high
mannose type in PubMed:26003537, while PubMed:27720757 found a
paucimannose at this position. {ECO:0000269|PubMed:26003537,
ECO:0000269|PubMed:27720757}.
-!- PTM: Processed at its C-terminus. {ECO:0000269|PubMed:27720757}.
-!- SIMILARITY: Belongs to the leguminous lectin family.
{ECO:0000305}.
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PIR; JC5444; JC5444.
PDB; 1DBN; X-ray; 2.75 A; A/B=30-268.
PDBsum; 1DBN; -.
SMR; P0DKL3; -.
UniLectin; P0DKL3; -.
iPTMnet; P0DKL3; -.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
CDD; cd06899; lectin_legume_LecRK_Arcelin_Co; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR016363; L-lectin.
InterPro; IPR000985; Lectin_LegA_CS.
InterPro; IPR019825; Lectin_legB_Mn/Ca_BS.
InterPro; IPR001220; Legume_lectin_dom.
Pfam; PF00139; Lectin_legB; 1.
PIRSF; PIRSF002690; L-type_lectin_plant; 1.
SUPFAM; SSF49899; SSF49899; 1.
1: Evidence at protein level;
3D-structure; Calcium; Direct protein sequencing; Disulfide bond;
Glycoprotein; Lectin; Manganese; Metal-binding; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:9163528}.
CHAIN 30 278 Seed leukoagglutinin.
/FTId=PRO_0000438710.
PROPEP 279 287 Removed in mature form.
{ECO:0000269|PubMed:27720757}.
/FTId=PRO_0000438711.
METAL 156 156 Manganese. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 158 158 Calcium. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 158 158 Manganese. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 160 160 Calcium; via carbonyl oxygen.
{ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 166 166 Calcium. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 169 169 Calcium. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 169 169 Manganese. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
METAL 174 174 Manganese; via tele nitrogen.
{ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 74 74 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 116 116 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 133 133 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 136 136 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 160 160 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 166 166 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
BINDING 253 253 Sialyllactose. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930}.
CARBOHYD 90 90 N-linked (GlcNAc...) (paucimannose)
asparagine. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930,
ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
/FTId=CAR_5005389752.
CARBOHYD 142 142 N-linked (GlcNAc...) (paucimannose)
asparagine. {ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930,
ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
/FTId=CAR_5005389753.
CARBOHYD 208 208 N-linked (GlcNAc...) (high mannose)
asparagine; partial.
{ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
/FTId=CAR_5005389751.
CARBOHYD 220 220 N-linked (GlcNAc...) (paucimannose)
asparagine; partial.
{ECO:0000244|PDB:1DBN,
ECO:0000269|PubMed:10747930,
ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
DISULFID 272 272 Interchain. {ECO:0000269|PubMed:27720757,
ECO:0000305|PubMed:9163528}.
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


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