LECB_STYJP
ID LECB_STYJP Reviewed; 270 AA.
AC P93538;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Bark lectin;
DE AltName: Full=LECSJABG;
DE Flags: Precursor; Fragment;
OS Styphnolobium japonicum (Japanese pagoda tree) (Sophora japonica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; Cladrastis clade;
OC Styphnolobium.
OX NCBI_TaxID=3897;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bark;
RX PubMed=9049272; DOI=10.1023/a:1005781103418;
RA van Damme E.J., Barre A., Rouge P., Peumans W.J.;
RT "Molecular cloning of the bark and seed lectins from the Japanese pagoda
RT tree (Sophora japonica).";
RL Plant Mol. Biol. 33:523-536(1997).
CC -!- FUNCTION: GalNAc-specific lectin.
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 EMBL; U63014; AAB51458.1; -; mRNA.
DR AlphaFoldDB; P93538; -.
DR SMR; P93538; -.
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..15
FT /evidence="ECO:0000255"
FT CHAIN 16..270
FT /note="Bark lectin"
FT /id="PRO_0000017654"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 155
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT NON_TER 1
SQ SEQUENCE 270 AA; 29315 MW; 1FD655A2C4E550B3 CRC64;
ISITFFLLLL NKVNSAEILS FSFPKFVSNQ EDLLLQGDAL VSSEGELQLT TVENGVPVWN
STGRALYYAP VHIWDNSTGR VASFATSFSF VVKAPVASKS ADGIAFFLAP LNNQIHGAGG
GLYGLFNSSS YSSSYQIVAV EFDTHTNAWD PNTRHIGIDV NSVKSTKTVT WGWENGEVAN
VLITYQAATE MLTVSLTYPS NQTSYILSAA VDLKSILPEW VRVGFTATTG LTTQYVETND
VLSWSFTSTL ETSDCGAEDN NVHLASYAFI