ID   LCS2_ROBPS              Reviewed;         285 AA.
AC   Q41161;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Seed agglutinin 2;
DE   AltName: Full=LECRPAS2;
DE   AltName: Full=RPSAII;
DE   AltName: Full=Seed agglutinin II;
DE   Flags: Precursor;
OS   Robinia pseudoacacia (Black locust).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; robinioid clade; Robinieae; Robinia.
OX   NCBI_TaxID=35938;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-50.
RC   TISSUE=Seed;
RX   PubMed=8616218; DOI=10.1007/bf00020462;
RA   van Damme E.J.M., Barre A., Rouge P., van Leuven F., Peumans W.J.;
RT   "The seed lectins of black locust (Robinia pseudoacacia) are encoded by two
RT   genes which differ from the bark lectin genes.";
RL   Plant Mol. Biol. 29:1197-1210(1995).
CC   -!- FUNCTION: Seed lectin.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- TISSUE SPECIFICITY: Expressed in seed.
CC   -!- PTM: Mostly found in non-glycosylated form.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; U24249; AAC49271.1; -; mRNA.
DR   PIR; S62691; S62691.
DR   AlphaFoldDB; Q41161; -.
DR   SMR; Q41161; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycoprotein; Lectin; Manganese;
KW   Metal-binding; Signal.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000269|PubMed:8616218"
FT   CHAIN           32..285
FT                   /note="Seed agglutinin 2"
FT                   /id="PRO_0000017643"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         158
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         166
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   285 AA;  31021 MW;  2C0B3249620294DE CRC64;
     MASYKFKTQN SFLLLLSISF FFLLLLNKVN STGSLSFSFP KFAPNQPYLI FQRDALVTST
     GVLQLTNVVN GVPSRKSLGR ALYAAPFQIW DSTTGNVASF VTSFSFIIQA PNPATTADGL
     AFFLAPVDTQ PLDLGGMLGI FKNGYFNKSN QIVAVEFDTF SNRHWDPTGR HMGINVNSIV
     SVKTVPWNWA NGEVANVFIS YEASTKSLTA SLVYPSLETS FIIHAIVDVK DVLPEWVRFG
     FSATTGIDTG YVQTNDVLSW SFESNLPGGN SVASVKNAGL STYAA