LEC1_LABAL
ID LEC1_LABAL Reviewed; 250 AA.
AC P23558;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Lectin 1;
DE AltName: Full=LAA-I;
DE AltName: Full=Lectin I;
DE AltName: Full=Seed lectin anti-H(O);
OS Laburnum alpinum (Scotch laburnum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Laburnum.
OX NCBI_TaxID=3852;
RN [1]
RP PROTEIN SEQUENCE, AND GLYCOSYLATION AT ASN-119.
RC TISSUE=Seed;
RX PubMed=1864376; DOI=10.1016/0014-5793(91)80934-u;
RA Konami Y., Yamamoto K., Toyoshima S., Osawa T.;
RT "The primary structure of the Laburnum alpinum seed lectin.";
RL FEBS Lett. 286:33-38(1991).
CC -!- FUNCTION: Di-N-acetylchitobiose specific lectin.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; S16964; S16964.
DR AlphaFoldDB; P23558; -.
DR SMR; P23558; -.
DR iPTMnet; P23558; -.
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.
FT CHAIN 1..250
FT /note="Lectin 1"
FT /id="PRO_0000105089"
FT BINDING 128
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 130
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; partial"
FT /evidence="ECO:0000269|PubMed:1864376"
SQ SEQUENCE 250 AA; 27151 MW; 05DC496E7DF60A0E CRC64;
LNELSFNFDK FVPNQNNILF QGVASVSTTG VLQVTKVTNT GIKRALYAAP IHAWDDDSET
GKVASFATSF SFVVKEPPIQ SRKADGVDGL AFFLAPANSQ IPSGSSAGMF GLFCSSDYNS
SNQIIAVEFD TYFGKAYNPW DPDFKHIGVD VNSIKSIKTV KWDWRNGDVA NVVITYRAPT
KSLTVSLSYP SDQTSNIVTA SVDLKAILPE WVSVGFSAGV GNAAKFNHDI LSWYFTSNLE
PNNPAVNQAQ
