ID   LCB3_ROBPS              Reviewed;         272 AA.
AC   Q41160;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 2.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative bark agglutinin LECRPA3;
DE   Flags: Precursor; Fragment;
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].
RC   TISSUE=Bark;
RX   PubMed=7716244; DOI=10.1104/pp.107.3.833;
RA   van Damme E.J.M., Barre A., Smeets K., Torrekens S., van Leuven F.,
RA   Rouge P., Peumans W.J.;
RT   "The bark of Robinia pseudoacacia contains a complex mixture of lectins.
RT   Characterization of the proteins and the cDNA clones.";
RL   Plant Physiol. 107:833-843(1995).
CC   -!- FUNCTION: Bark lectins are storage proteins that probably maintain
CC       stocks of nitrogen during dormant period. Self-aggregatable molecules
CC       that can bind their own carbohydrate side chains. They could also play
CC       a role in the plant's defense against phytophagous invertebrates or
CC       herbivorous higher animals.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Weak expression in bark. The lectin accumulates in
CC       the inner bark in autumn.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA80183.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U12784; AAA80183.1; ALT_INIT; mRNA.
DR   AlphaFoldDB; Q41160; -.
DR   SMR; Q41160; -.
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..29
FT   CHAIN           30..272
FT                   /note="Putative bark agglutinin LECRPA3"
FT                   /id="PRO_0000017646"
FT   BINDING         150
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        65
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   272 AA;  29195 MW;  BE8B2834EA3100D4 CRC64;
     PFNPETVYAL LAMLISFFVL LASARKENSD EGISFNFTNF TRGDQGVTLL GQANIMANGI
     LALTNHTNPT WNTGRALYSK PVPIWDSATG NVASFVTSFS FVVQEIKGAI PADGIVFFLA
     PEARIPDNSA GGQLGIVNAN KAYNPFVGVE FDTYSNNWDP KSAHIGIDAS SLISLRTVKW
     NKVSGSLVKV SIIYDSLSKT LSVVVTHENG QISTIAQVVD LKAVLGEKVR VGFTAATTTG
     RELYDIHAWS FTSTLVTATS STSKNMNIAS YA