LCB1_ROBPS
ID LCB1_ROBPS Reviewed; 285 AA.
AC Q41159;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Bark agglutinin I polypeptide A;
DE AltName: Full=LECRPA1;
DE AltName: Full=RPbAI;
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=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: N-acetyl-D-galactosamine specific lectin. Bark lectins are
CC storage protein that probably maintains stocks of nitrogen during
CC dormant period. Self-aggregatable molecules that can bind their own
CC carbohydrate side chains. They could also play a role in the plant's
CC defense against phytophagous invertebrates or herbivorous higher
CC animals.
CC -!- SUBUNIT: RPbAI is composed of two polypeptides, A and B, that associate
CC into five different tetrameric isolectins. The A4 combination is the
CC only one devoid of agglutination activity. Isoform B4 displays maximal
CC agglutination activity.
CC -!- TISSUE SPECIFICITY: Strong expression in seed. Lower levels in the
CC flower, and the bark of the roots. No expression in leaf. The lectin
CC accumulates in the inner bark in autumn.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; U12782; AAA80181.1; -; mRNA.
DR PDB; 1FNY; X-ray; 1.81 A; A=32-268.
DR PDB; 1FNZ; X-ray; 2.05 A; A=32-268.
DR PDBsum; 1FNY; -.
DR PDBsum; 1FNZ; -.
DR AlphaFoldDB; Q41159; -.
DR SMR; Q41159; -.
DR UniLectin; Q41159; -.
DR EvolutionaryTrace; Q41159; -.
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 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin;
KW Manganese; Metal-binding; Signal.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:7716244"
FT CHAIN 32..285
FT /note="Bark agglutinin I polypeptide A"
FT /id="PRO_0000017644"
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 160
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
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"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1FNY"
FT TURN 92..94
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1FNY"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:1FNY"
FT TURN 138..140
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1FNY"
FT TURN 163..165
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 168..180
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 195..202
FT /evidence="ECO:0007829|PDB:1FNY"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 207..214
FT /evidence="ECO:0007829|PDB:1FNY"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 219..226
FT /evidence="ECO:0007829|PDB:1FNY"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:1FNY"
FT STRAND 256..266
FT /evidence="ECO:0007829|PDB:1FNY"
SQ SEQUENCE 285 AA; 30928 MW; 49382E50EEF27282 CRC64;
MTSYNFKTQT SFPLLLSISF FFLLLLNKVN STGSLSFSFP KFAPNQPYLI FQRDALVTST
GVLQLTNVVN GVPSGKSLGR ALYAAPFQIW DSTTGNVASF VTSFSFIIQA PNPTTTADGL
AFFLAPVDTQ PLDVGGMLGI FKDGYFNKSN QIVAVEFDTF SNIHFDPKGR HMGINVNSIV
SIKTVPWNWT NGEVANVFIS YEASTKSLTA SLVYPSLETS FIVHAIVDVK DVLPEWVRFG
FSATTGIDKG YVQTNDVLSW SFESNLPGGN SVASVKNAGL STYAA
