MALB_MAAAM
ID MALB_MAAAM Reviewed; 286 AA.
AC P93248;
DT 18-JAN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Bark leucoagglutinin {ECO:0000303|PubMed:9249142};
DE AltName: Full=Bark leukoagglutinin {ECO:0000305};
DE Flags: Precursor; Fragment;
GN Name=MAL {ECO:0000303|PubMed:9249142};
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], AND FUNCTION.
RC TISSUE=Bark;
RX PubMed=9249142; DOI=10.1023/a:1018595300863;
RA Van Damme E.J., Van Leuven F., Peumans W.J.;
RT "Isolation, characterization and molecular cloning of the bark lectins from
RT Maackia amurensis.";
RL Glycoconj. J. 14:449-456(1997).
CC -!- FUNCTION: Sialic acid-binding lectin specifically recognizing the
CC trisaccharide sequence Neu5Ac/Gc-alpha-2,3-Gal-beta-1,4-GlcNAc/Glc.
CC {ECO:0000305|PubMed:9249142}.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; U65010; AAB39934.1; -; mRNA.
DR AlphaFoldDB; P93248; -.
DR SMR; P93248; -.
DR EvolutionaryTrace; P93248; -.
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.
DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
PE 2: Evidence at transcript level;
KW Calcium; Glycoprotein; Lectin; Manganese; Metal-binding; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT CHAIN 29..286
FT /note="Bark leucoagglutinin"
FT /id="PRO_5004161572"
FT PROPEP 278..286
FT /note="Removed in mature form"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT /id="PRO_0000438712"
FT BINDING 73
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:0000250|UniProtKB:P0DKL3"
FT BINDING 115
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:0000250|UniProtKB:P0DKL3"
FT BINDING 135
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:0000250|UniProtKB:P0DKL3"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 159
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:0000250|UniProtKB:P0DKL3"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 165
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:0000250|UniProtKB:P0DKL3"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 168
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:P0DKL3"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31209 MW; 0F2E27617A0F6D00 CRC64;
ATSNSKPTQV LLATFLTFFF LLLNNVNSSD ELSFTINNFV PNEADLLFQG EASVSSTGVL
QLTRVENGQP QQYSVGRALY AAPVRIWDNT TGSVASFSTS FTFVVKAPNP TITSDGLAFF
LAPPDSQIPS GRVSKYLGLF NNSNSDSSNQ IVAVEFDTYF GHSYDPWDPN YRHIGIDVNG
IESIKTVQWD WINGGVAFAT ITYLAPNKTL IASLVYPSNQ TSFIVAASVD LKEILPEWVR
VGFSAATGYP TQVETHDVLS WSFTSTLEAN SDAATENNVH IARYTA
