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 02-JUN-2021, entry version 98. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 //