LECB_LATOC
ID LECB_LATOC Reviewed; 181 AA.
AC P04122;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1986, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lectin beta-1 and beta-2 chains;
OS Lathyrus ochrus (Cyprus-vetch) (Pisum ochrus).
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; IRL clade; Fabeae; Lathyrus.
OX NCBI_TaxID=3858;
RN [1]
RP PROTEIN SEQUENCE.
RA Yarwood A., Richardson M., Sousa-Cavada B., Rouge P.;
RT "The complete amino acid sequences of the beta-1- and beta-2-subunits of
RT the isolectins LoL1 and LoL11 from seeds of Lathyrus ochrus (L.) DC.";
RL FEBS Lett. 184:104-109(1985).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2380988; DOI=10.1016/0022-2836(90)90199-v;
RA Bourne Y., Abergel C., Cambillau C., Frey M., Rouge P.,
RA Fontecilla-Camps J.-C.;
RT "X-ray crystal structure determination and refinement at 1.9-A resolution
RT of isolectin I from the seeds of Lathyrus ochrus.";
RL J. Mol. Biol. 214:571-584(1990).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX PubMed=2091026; DOI=10.1002/prot.340080410;
RA Bourne Y., Roussel A., Frey M., Rouge P., Fontecilla-Camps J.-C.,
RA Cambillau C.;
RT "Three-dimensional structures of complexes of Lathyrus ochrus isolectin I
RT with glucose and mannose: fine specificity of the monosaccharide-binding
RT site.";
RL Proteins 8:365-376(1990).
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC -!- INTERACTION:
CC P04122; P12307; NbExp=2; IntAct=EBI-9019549, EBI-16210416;
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 -!- MISCELLANEOUS: The sequence shown is that of the beta-1.
CC -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR PIR; A05087; A05087.
DR PIR; A05088; A05088.
DR PDB; 1LGB; X-ray; 3.30 A; A=1-181.
DR PDB; 1LGC; X-ray; 2.80 A; A/C/E=1-181.
DR PDB; 1LOA; X-ray; 2.20 A; A/C/E/G=1-181.
DR PDB; 1LOB; X-ray; 2.00 A; A/C/E/G=1-181.
DR PDB; 1LOC; X-ray; 2.05 A; A/C/E/G=1-181.
DR PDB; 1LOD; X-ray; 2.05 A; A/C/E/G=1-181.
DR PDB; 1LOE; X-ray; 1.90 A; A/C=1-181.
DR PDB; 1LOF; X-ray; 2.30 A; A/C=1-181.
DR PDB; 1LOG; X-ray; 2.10 A; A/C=1-181.
DR PDBsum; 1LGB; -.
DR PDBsum; 1LGC; -.
DR PDBsum; 1LOA; -.
DR PDBsum; 1LOB; -.
DR PDBsum; 1LOC; -.
DR PDBsum; 1LOD; -.
DR PDBsum; 1LOE; -.
DR PDBsum; 1LOF; -.
DR PDBsum; 1LOG; -.
DR AlphaFoldDB; P04122; -.
DR SMR; P04122; -.
DR DIP; DIP-6190N; -.
DR IntAct; P04122; 1.
DR Allergome; 8817; Lat oc Agglutinin.
DR UniLectin; P04122; -.
DR EvolutionaryTrace; P04122; -.
DR GO; GO:0005537; F:mannose 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; IPR019825; Lectin_legB_Mn/Ca_BS.
DR InterPro; IPR001220; Legume_lectin_dom.
DR Pfam; PF00139; Lectin_legB; 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; Lectin; Manganese;
KW Mannose-binding; Metal-binding.
FT CHAIN 1..181
FT /note="Lectin beta-1 and beta-2 chains"
FT /id="PRO_0000105104"
FT BINDING 119
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 129
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT BINDING 136
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT VARIANT 16
FT /note="Q -> P (in beta-2)"
FT VARIANT 66
FT /note="S -> A (in beta-2)"
FT VARIANT 168
FT /note="A -> G (in beta-2)"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:1LOE"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 62..72
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 82..89
FT /evidence="ECO:0007829|PDB:1LOE"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1LOE"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1LOE"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:1LOE"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 147..151
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 159..167
FT /evidence="ECO:0007829|PDB:1LOE"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:1LOE"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:1LOE"
SQ SEQUENCE 181 AA; 19889 MW; C9AD28FC03A48215 CRC64;
TETTSFSITK FGPDQQNLIF QGDGYTTKER LTLTKAVRNT VGRALYSSPI HIWDSKTGNV
ANFVTSFTFV IDAPNSYNVA DGFTFFIAPV DTKPQTGGGY LGVFNSKDYD KTSQTVAVEF
DTFYNTAWDP SNGDRHIGID VNSIKSINTK SWKLQNGKEA NVVIAFNAAT NVLTVSLTYP
N
