LEC_LEUMI
ID LEC_LEUMI Reviewed; 240 AA.
AC P42088;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Lectin;
DE AltName: Full=Agglutinin;
DE AltName: Full=BMA;
DE Contains:
DE RecName: Full=Lectin beta chain;
DE Contains:
DE RecName: Full=Lectin alpha chain;
OS Leucomphalos mildbraedii (Bowringia mildbraedii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC Baphieae; Leucomphalos.
OX NCBI_TaxID=28956;
RN [1]
RP PROTEIN SEQUENCE, AND VARIANTS SER-143; ARG-158; ARG-177; VAL-187 AND
RP ALA-203.
RC TISSUE=Seed;
RX PubMed=8373823; DOI=10.1016/0167-4838(93)90060-5;
RA Chawla D., Animashaun T., Hughes R.C., Harris A., Aitken A.;
RT "Bowringia mildbraedii agglutinin: polypeptide composition, primary
RT structure and homologies with other legume lectins.";
RL Biochim. Biophys. Acta 1202:38-46(1993).
RN [2]
RP FUNCTION.
RX PubMed=2925660; DOI=10.1016/s0021-9258(18)83793-0;
RA Animashaun T., Hughes R.C.;
RT "Bowringia milbraedii agglutinin. Specificity of binding to early
RT processing intermediates of asparagine-linked oligosaccharide and use as a
RT marker of endoplasmic reticulum glycoproteins.";
RL J. Biol. Chem. 264:4657-4663(1989).
CC -!- FUNCTION: Binds preferentially to oligosaccharides bearing the sequence
CC Man-alpha-1->2 Man-alpha-1->6 Man-alpha-1->6Man found in early steps of
CC glycoprotein processing in the endoplasmic reticulum. It binds weakly
CC to highly processed oligosaccharide structures.
CC {ECO:0000269|PubMed:2925660}.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains; disulfide
CC bond linked.
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.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PDB; 2FMD; X-ray; 1.90 A; A=1-240.
DR PDBsum; 2FMD; -.
DR AlphaFoldDB; P42088; -.
DR SMR; P42088; -.
DR UniLectin; P42088; -.
DR EvolutionaryTrace; P42088; -.
DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
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; 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; PS00307; LECTIN_LEGUME_BETA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Disulfide bond; Lectin;
KW Manganese; Metal-binding.
FT CHAIN 1..116
FT /note="Lectin beta chain"
FT /id="PRO_0000017581"
FT CHAIN 117..240
FT /note="Lectin alpha chain"
FT /id="PRO_0000017582"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 133
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 138
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 143
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT DISULFID 5
FT /note="Interchain"
FT VARIANT 143
FT /note="H -> S"
FT /evidence="ECO:0000269|PubMed:8373823"
FT VARIANT 158
FT /note="K -> R"
FT /evidence="ECO:0000269|PubMed:8373823"
FT VARIANT 177
FT /note="S -> R"
FT /evidence="ECO:0000269|PubMed:8373823"
FT VARIANT 187
FT /note="P -> V"
FT /evidence="ECO:0000269|PubMed:8373823"
FT VARIANT 203
FT /note="V -> A"
FT /evidence="ECO:0000269|PubMed:8373823"
FT UNSURE 86..90
FT UNSURE 116
FT STRAND 3..10
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 65..76
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2FMD"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:2FMD"
FT TURN 108..110
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:2FMD"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 143..152
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:2FMD"
FT TURN 175..178
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:2FMD"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 206..215
FT /evidence="ECO:0007829|PDB:2FMD"
FT STRAND 224..235
FT /evidence="ECO:0007829|PDB:2FMD"
SQ SEQUENCE 240 AA; 25424 MW; 5A9F7FAF3A09B060 CRC64;
ANSVCFTFTD FESGQQDLIF QGDASVGSNK ALQLTKVDSK GNPQGGSVGR ALYTAPIRLW
QSSSLVASFE TTFTFSISQG SSTPAAALTF FIASPDTKIP SGSGGRLLGL FGSSNNAGSD
NGVVAVEFDT YPNTDIGDPN YRHIGIDVNS IRSKAASKWD WQNGKTATAH ISYNSASKRL
SVVSSYPNSS PVVVSFDVEL NNVGPPDVRV GFSATTGQYT QTNNILAWSF RSSLMGYQAN
