LEC_BAUPU
ID LEC_BAUPU Reviewed; 290 AA.
AC P16030;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Lectin;
DE Flags: Precursor;
OS Bauhinia purpurea (Camel's foot tree) (Phanera purpurea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Cercidoideae; Cercideae; Bauhiniinae;
OC Bauhinia.
OX NCBI_TaxID=3806;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1657898; DOI=10.1093/oxfordjournals.jbchem.a123477;
RA Kusui K., Yamamoto K., Konami Y., Osawa T.;
RT "cDNA cloning and expression of Bauhinia purpurea lectin.";
RL J. Biochem. 109:899-903(1991).
RN [2]
RP PROTEIN SEQUENCE OF 29-62.
RA Young N.M., Watson D.C., Williams R.E.;
RT "Lectins and legume chemotaxonomy. Characterisation of the N-acetyl-D-
RT galactosamine specific lectin of Bauhinia purpurea.";
RL FEBS Lett. 182:403-405(1985).
CC -!- FUNCTION: N-acetyl-D-galactosamine specific lectin.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR EMBL; D12481; BAA02049.1; -; mRNA.
DR PIR; JX0175; JX0175.
DR AlphaFoldDB; P16030; -.
DR SMR; P16030; -.
DR IntAct; P16030; 1.
DR iPTMnet; P16030; -.
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..28
FT /evidence="ECO:0000269|Ref.2"
FT CHAIN 29..290
FT /note="Lectin"
FT /id="PRO_0000017584"
FT BINDING 161
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 163
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 165
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 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1657898"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1657898"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 35
FT /note="G -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 55
FT /note="Missing (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="P -> W (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 32238 MW; 9DBC144630D2C768 CRC64;
MLLYNSKSYV LQLIFITLLL TQLNKVKSTS STLTGFTFPN FWSNTQENGT EIIFLGNATY
TPGALRLTRI GEDGIPLKSN AGQASYSRPV FLWDSTGHVA SFYTSFSFIV RSIDVPHITA
DGFAFFLAPV DSSVKDYGGC LGLFRYKTAT DPSKNQVVAV EFDTWPNTEW SDLRYPHIGI
NVNSTVSVAT TRWDNDDAYV TKSTAHITYD ATSKIITVLL TYDNGRHYQL SHVVDLPKIL
PERVRIGFSG GTGFNETQYI LSWSFTSTLN STKISALTQK LRSSASYSSM