ID LCB2_ROBPS Reviewed; 286 AA.
AC Q42372;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 22-FEB-2023, entry version 87.
DE RecName: Full=Bark agglutinin I polypeptide B;
DE AltName: Full=LECRPA2;
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].
RC TISSUE=Bark;
RX PubMed=7915553; DOI=10.1007/bf00028879;
RA Yoshida K., Baba K., Yamamoto N., Tazaki K.;
RT "Cloning of a lectin cDNA and seasonal changes in levels of the lectin and
RT its mRNA in the inner bark of Robinia pseudoacacia.";
RL Plant Mol. Biol. 25:845-853(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 32-49.
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).
RN [3]
RP PROTEIN SEQUENCE OF 32-51.
RC TISSUE=Bark;
RA Tazaki K., Yoshida K.;
RT "The bark lectin of Robinia pseudoacacia: purification and partial
RT characterization.";
RL Plant Cell Physiol. 33:125-129(1992).
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: 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: Mostly in the axial and ray parenchymal cells of
CC the inner bark. Fewer in the axial and ray parenchymal cells of the
CC xylem. Strong expression in bark. The lectin accumulates in the inner
CC bark in autumn and winter and disappears in may.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; D17757; BAA04604.1; -; mRNA.
DR EMBL; U12783; AAA80182.1; -; mRNA.
DR PIR; S48033; S48033.
DR AlphaFoldDB; Q42372; -.
DR SMR; Q42372; -.
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 Gene3D; 2.60.120.200; -; 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 PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1.
DR PANTHER; PTHR32401:SF45; LECTIN; 1.
DR Pfam; PF00139; Lectin_legB; 1.
DR PIRSF; PIRSF002690; L-type_lectin_plant; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 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:7716244, ECO:0000269|Ref.3"
FT CHAIN 32..286
FT /note="Bark agglutinin I polypeptide B"
FT /id="PRO_0000017645"
FT BINDING 157
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
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 163
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 43..46
FT /note="KHSQ -> MPNE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="D -> W (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 286 AA; 31211 MW; 467E37661D1DC1E6 CRC64;
MASYKFKTQN SFLLLLSISF FFLLLLNKVN STGSLSFSFP KFKHSQPDLI FQSDALVTSK
GVLQLTTVND GRPVYDSIGR VLYAAPFQIW DSTTGNVASF VTSFSFIIKA PNEGKTADGL
VFFLAPVGST QPLKGGGLLG LFKDESYNKS NQIVAVEFDT FRNVAWDPNG IHMGIDVNSI
QSVRTVRWDW ANGEVANVFI SYEASTKSLT ASLVYPSLEK SFILSAIVDL KKVLPEWVRV
GFTATTGLSE DYVQTNDVLS WSFESNLPGG NSVASVKNAG LSTYAA
//
