ID   LEC1_CLAKE              Reviewed;         293 AA.
AC   Q39528;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Agglutinin-1;
DE   AltName: Full=Agglutinin I;
DE   AltName: Full=ClAI;
DE   AltName: Full=LecClAI;
DE   Contains:
DE     RecName: Full=Agglutinin-1 subunit A;
DE   Contains:
DE     RecName: Full=Agglutinin-1 subunit B;
DE   Flags: Precursor;
OS   Cladrastis kentukea (Yellow wood) (Cladrastis lutea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; Cladrastis clade;
OC   Cladrastis.
OX   NCBI_TaxID=38412;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 36-55 AND 162-181.
RC   TISSUE=Bark;
RX   PubMed=8534854; DOI=10.1007/bf00020986;
RA   van Damme E.J.M., Barre A., Bemer V., Rouge P., van Leuven F.,
RA   Peumans W.J.;
RT   "A lectin and a lectin-related protein are the two most prominent proteins
RT   in the bark of yellow wood (Cladrastis lutea).";
RL   Plant Mol. Biol. 29:579-598(1995).
CC   -!- FUNCTION: Mannose/glucose binding bark lectin.
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 of four 32 kDa monomers which are post-
CC       translationally cleaved into a two subunits: A and B.
CC   -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion
CC       and one calcium ion. The metal ions are essential for the saccharide-
CC       binding and cell-agglutinating activities (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   EMBL; U21958; AAC49136.1; -; mRNA.
DR   PIR; S66356; S66356.
DR   AlphaFoldDB; Q39528; -.
DR   SMR; Q39528; -.
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   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Glycoprotein; Lectin; Manganese;
KW   Mannose-binding; Metal-binding; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:8534854"
FT   CHAIN           36..161
FT                   /note="Agglutinin-1 subunit A"
FT                   /id="PRO_0000017650"
FT   CHAIN           162..293
FT                   /note="Agglutinin-1 subunit B"
FT                   /id="PRO_0000017651"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         173
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         186
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        162
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        47
FT                   /note="P -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        162
FT                   /note="N -> D (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   293 AA;  32128 MW;  EDBED3FF5FA3C66C CRC64;
     MTISNTNFLE TKKPLSLPLL AFITIYLMLL HRVNSSDSLS FTFNNFPPNS EDLIFQKDAS
     ISSNETLELT RISSSGQPAT SSVGRALYYT PVRLWDKSTG RLASFKTTFS FAITSPTQDP
     GDGFAFFIAP PDTTPGYGGG LLGLFNGFNL RNSSNNGVAV NNQSAQIVAV EFDTYINGQC
     DPKYRHVGID VNSITSLAYT QWQWQNGVKA TAQISYNPAS QKLTAVTSYP NSTPLTVSLD
     IDLQTVLPEW VRVGFSASTG QNVERNSILA WSFSSSLTTL TAKKEDMYIA RYV