ID   LEC1_LATOC              Reviewed;          53 AA.
AC   P12306;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Mannose/glucose-specific lectin alpha 1 chain;
DE            Short=Lol I;
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.
RX   PubMed=6383863; DOI=10.1016/0014-5793(84)80573-6;
RA   Richardson M., Rouge P., Sousa-Cavada B., Yarwood A.;
RT   "The amino acid sequences of the alpha 1 and alpha 2 subunits of the
RT   isolectins from seeds of Lathyrus ochrus (L) DC.";
RL   FEBS Lett. 175:76-81(1984).
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   -!- SIMILARITY: Belongs to the leguminous lectin family. {ECO:0000305}.
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DR   PIR; A25989; A25989.
DR   PDB; 1LOA; X-ray; 2.20 A; B/D/F/H=1-52.
DR   PDB; 1LOB; X-ray; 2.00 A; B/D/F/H=1-52.
DR   PDB; 1LOC; X-ray; 2.05 A; B/D/F/H=1-52.
DR   PDB; 1LOD; X-ray; 2.05 A; B/D/F/H=1-52.
DR   PDB; 1LOE; X-ray; 1.90 A; B/D=1-52.
DR   PDB; 1LOF; X-ray; 2.30 A; B=1-52, D=1-51.
DR   PDB; 1LOG; X-ray; 2.10 A; B/D=1-52.
DR   PDBsum; 1LOA; -.
DR   PDBsum; 1LOB; -.
DR   PDBsum; 1LOC; -.
DR   PDBsum; 1LOD; -.
DR   PDBsum; 1LOE; -.
DR   PDBsum; 1LOF; -.
DR   PDBsum; 1LOG; -.
DR   AlphaFoldDB; P12306; -.
DR   SMR; P12306; -.
DR   DIP; DIP-6192N; -.
DR   UniLectin; P12306; -.
DR   EvolutionaryTrace; P12306; -.
DR   GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000985; Lectin_LegA_CS.
DR   InterPro; IPR001220; Legume_lectin_dom.
DR   Pfam; PF00139; Lectin_legB; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Lectin; Mannose-binding.
FT   CHAIN           1..53
FT                   /note="Mannose/glucose-specific lectin alpha 1 chain"
FT                   /id="PRO_0000105102"
FT   STRAND          3..9
FT                   /evidence="ECO:0007829|PDB:1LOE"
FT   HELIX           12..14
FT                   /evidence="ECO:0007829|PDB:1LOE"
FT   STRAND          18..27
FT                   /evidence="ECO:0007829|PDB:1LOE"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1LOB"
FT   STRAND          34..46
FT                   /evidence="ECO:0007829|PDB:1LOE"
FT   STRAND          48..50
FT                   /evidence="ECO:0007829|PDB:1LOF"
SQ   SEQUENCE   53 AA;  5877 MW;  06E19D2C33444961 CRC64;
     ETSYTLNEVV PLKEFVPEWV RIGFSATTGA EFAAHEVLSW FFHSELAGTS SSN