ID LEC_ERYCO Reviewed; 281 AA. AC P16404; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 04-NOV-2026, entry version 126. DE RecName: Full=Lectin; DE AltName: Full=ECorL; DE Flags: Precursor; OS Erythrina corallodendron (Coral tree). 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; indigoferoid/millettioid clade; Phaseoleae; Erythrina. OX NCBI_TaxID=3843; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1692539; DOI=10.1016/0014-5793(90)80777-g; RA Arango R., Rozenblatt S., Sharon N.; RT "Cloning and sequence analysis of the Erythrina corallodendron lectin RT cDNA."; RL FEBS Lett. 264:109-111(1990). RN [2] RP PROTEIN SEQUENCE OF 27-270. RX PubMed=2806566; DOI=10.1016/0014-5793(89)81791-0; RA Adar R., Richardson M., Lis H., Sharon N.; RT "The amino acid sequence of Erythrina corallodendron lectin and its RT homology with other legume lectins."; RL FEBS Lett. 257:81-85(1989). RN [3] RP PROTEIN SEQUENCE OF 27-55; 77-99; 126-166 AND 247-267, VARIANT GLN-160, RP PROTEOLYTIC PROCESSING, AND GLYCOSYLATION. RX PubMed=7852319; DOI=10.1074/jbc.270.6.2563; RA Young N.M., Watson D.C., Yaguchi M., Adar R., Arango R., RA Rodriguez-Arango E., Sharon N., Blay P.K., Thibault P.; RT "C-terminal post-translational proteolysis of plant lectins and their RT recombinant forms expressed in Escherichia coli. Characterization of RT 'ragged ends' by mass spectrometry."; RL J. Biol. Chem. 270:2563-2570(1995). RN [4] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=1948067; DOI=10.1126/science.1948067; RA Shaanan B., Lis H., Sharon N.; RT "Structure of a legume lectin with an ordered N-linked carbohydrate in RT complex with lactose."; RL Science 254:862-866(1991). RN [5] RP X-RAY CRYSTALLOGRAPHY. RX PubMed=9545381; DOI=10.1006/jmbi.1998.1664; RA Elgavish S., Shaanan B.; RT "Structures of the Erythrina corallodendron lectin and of its complexes RT with mono- and disaccharides."; RL J. Mol. Biol. 277:917-932(1998). CC -!- FUNCTION: Galactose and N-acetyllactosamine specific lectin. Binds to CC the H-2 blood type determinant fucosyl-N-acetyllactosamine. CC -!- SUBUNIT: Homodimer. CC -!- PTM: A minor C-terminal proteolytic processing site is observed at CC position 268. {ECO:0000269|PubMed:7852319}. CC -!- MISCELLANEOUS: Binds one manganese (or another transition metal) ion CC and one calcium ion. 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 EMBL; X52782; CAA36986.1; -; mRNA. DR PIR; S09697; S09697. DR PDB; 1AX0; X-ray; 1.90 A; A=27-265. DR PDB; 1AX1; X-ray; 1.95 A; A=27-265. DR PDB; 1AX2; X-ray; 1.95 A; A=27-265. DR PDB; 1AXY; X-ray; 1.95 A; A=27-265. DR PDB; 1AXZ; X-ray; 1.95 A; A=27-265. DR PDB; 1FYU; X-ray; 2.60 A; A/B=27-281. DR PDB; 1LTE; X-ray; 2.00 A; A=27-265. DR PDB; 1SFY; X-ray; 2.55 A; A/B/C/D/E/F=27-265. DR PDB; 3N35; X-ray; 2.00 A; A=27-268. DR PDB; 3N36; X-ray; 2.30 A; A=27-268. DR PDB; 3N3H; X-ray; 2.00 A; A=27-268. DR SMR; P16404; -. DR UniLectin; P16404; -. DR GlyCosmos; P16404; 2 sites, 1 glycan. DR iPTMnet; P16404; -. DR EvolutionaryTrace; P16404; -. DR CDD; cd06899; lectin_legume_LecRK_Arcelin_ConA; 1. DR Gene3D; 2.60.120.200; -; 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 InterPro; IPR050258; Leguminous_Lectin. DR PANTHER; PTHR32401; CONCANAVALIN A-LIKE LECTIN FAMILY PROTEIN; 1. DR PANTHER; PTHR32401:SF45; LECTIN; 1. DR Pfam; PF00139; Lectin_legB; 1. DR PIRSF; PIRSF002690; L-type_lectin_plant; 1. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1. DR PROSITE; PS00308; LECTIN_LEGUME_ALPHA; 1. DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR AlphaFoldDB; P16404; -. DR MDposit; P16404; -. DR MDRepo; P16404; -. PE 1: Evidence at protein level; KW 3D-structure; Calcium; Direct protein sequencing; Glycoprotein; Lectin; KW Signal. FT SIGNAL 1..26 FT /evidence="ECO:0000269|PubMed:2806566, FT ECO:0000269|PubMed:7852319" FT CHAIN 27..268 FT /note="Lectin" FT /id="PRO_0000017617" FT PROPEP 269..281 FT /id="PRO_0000017618" FT CARBOHYD 43 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:7852319" FT CARBOHYD 139 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:7852319" FT VARIANT 48 FT /note="G -> A" FT VARIANT 160 FT /note="P -> Q" FT /evidence="ECO:0000269|PubMed:7852319" FT VARIANT 225 FT /note="D -> V" FT CONFLICT 49..54 FT /note="AALITQ -> DSIPET (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="N -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 28..36 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 44..48 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 58..61 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 67..69 FT /evidence="ECO:0007829|PDB:3N35" FT STRAND 74..81 FT /evidence="ECO:0007829|PDB:1AX0" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 95..103 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 109..111 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 115..123 FT /evidence="ECO:0007829|PDB:1AX0" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:1AX0" FT TURN 135..137 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 138..142 FT /evidence="ECO:0007829|PDB:1AX0" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 150..155 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 166..177 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 179..183 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:1AX0" FT TURN 200..203 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 204..211 FT /evidence="ECO:0007829|PDB:1AX0" FT TURN 212..215 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 216..223 FT /evidence="ECO:0007829|PDB:1AX0" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 232..242 FT /evidence="ECO:0007829|PDB:1AX0" FT STRAND 253..263 FT /evidence="ECO:0007829|PDB:1AX0" SQ SEQUENCE 281 AA; 30752 MW; 311DE5A43AEF1E67 CRC64; MATYKLCSVL ALSLTLFLLI LNKVNSVETI SFSFSEFEPG NDNLTLQGAA LITQSGVLQL TKINQNGMPA WDSTGRTLYA KPVHIWDMTT GTVASFETRF SFSIEQPYTR PLPADGLVFF MGPTKSKPAQ GYGYLGIFNN SKQDNSYQTL GVEFDTFSNP WDPPQVPHIG IDVNSIRSIK TQPFQLDNGQ VANVVIKYDA SSKILHAVLV YPSSGAIYTI AEIVDVKQVL PEWVDVGLSG ATGAQRDAAE THDVYSWSFQ ASLPETNDAV IPTSNHNTFA I //