LECS_STYJP
ID LECS_STYJP Reviewed; 292 AA.
AC P93535;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Seed lectin;
DE AltName: Full=LECSJASG;
DE Flags: Precursor;
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=Seed;
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: Mannose/glucose-specific lectin.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; U63011; AAB51441.1; -; mRNA.
DR AlphaFoldDB; P93535; -.
DR SMR; P93535; -.
DR GlyConnect; 552; 1 N-Linked glycan.
DR GO; GO:0005537; F:mannose 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; Mannose-binding; Metal-binding;
KW Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..292
FT /note="Seed lectin"
FT /id="PRO_0000017655"
FT BINDING 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 82
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 292 AA; 31657 MW; A7431C29117A503E CRC64;
MATSNSRPHL LQTHKPFSVV LAISITFFLL LLNKVNSAEI LSFSFPKFAS NQEDLLLQGD
ALVSSKGELQ LTTVENGVPI WNSTGRALYY APVHIWDKST GRVASFATSF SFVVKAPVAS
KSADGIAFFL APPNNQIQGP GGGHLGLFHS SGYNSSYQII AVDFDTHINA WDPNTRHIGI
DVNSINSTKT VTWGWQNGEV ANVLISYQAA TETLTVSLTY PSSQTSYILS AAVDLKSILP
EWVRVGFTAA TGLTTQYVET HDVLSWSFTS TLETGDCGAK DDNVHLVSYA FI