LEC_ERYCO
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 25-MAY-2022, entry version 120.
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 (2.0 ANGSTROMS).
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 (1.9 ANGSTROMS) OF 27-265.
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 PDBsum; 1AX0; -.
DR PDBsum; 1AX1; -.
DR PDBsum; 1AX2; -.
DR PDBsum; 1AXY; -.
DR PDBsum; 1AXZ; -.
DR PDBsum; 1FYU; -.
DR PDBsum; 1LTE; -.
DR PDBsum; 1SFY; -.
DR PDBsum; 3N35; -.
DR PDBsum; 3N36; -.
DR PDBsum; 3N3H; -.
DR AlphaFoldDB; P16404; -.
DR SMR; P16404; -.
DR UniLectin; P16404; -.
DR GlyConnect; 332; 1 N-Linked glycan.
DR iPTMnet; P16404; -.
DR EvolutionaryTrace; P16404; -.
DR GO; GO:0030246; F:carbohydrate 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; IPR000985; Lectin_LegA_CS.
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; PS00308; LECTIN_LEGUME_ALPHA; 1.
DR PROSITE; PS00307; LECTIN_LEGUME_BETA; 1.
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 42..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..210
FT /evidence="ECO:0007829|PDB:1AX0"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:1AX0"
FT STRAND 217..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
