LED2_PHYAM
ID LED2_PHYAM Reviewed; 82 AA.
AC P83790;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Lectin-D2;
DE AltName: Full=PL-D2;
OS Phytolacca americana (American pokeweed) (Phytolacca decandra).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Phytolaccaceae; Phytolacca.
OX NCBI_TaxID=3527;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE, AND FUNCTION.
RC TISSUE=Root {ECO:0000269|PubMed:8987560};
RX PubMed=8987560; DOI=10.1271/bbb.60.1380;
RA Yamaguchi K., Mori A., Funatsu G.;
RT "Amino acid sequence and some properties of lectin-D from the roots of
RT pokeweed (Phytolacca americana).";
RL Biosci. Biotechnol. Biochem. 60:1380-1382(1996).
RN [2] {ECO:0000305}
RP FUNCTION, AND SUBUNIT.
RX PubMed=15277769; DOI=10.1271/bbb.68.1591;
RA Yamaguchi K., Uechi M., Katakura Y., Oda T., Ishiguro M.;
RT "Mitogenic properties of pokeweed lectin-D isoforms on human peripheral
RT blood lymphocytes: non-mitogen PL-D1 and mitogen PL-D2.";
RL Biosci. Biotechnol. Biochem. 68:1591-1593(2004).
RN [3] {ECO:0000305, ECO:0000312|PDB:1ULM}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH
RP TRI-N-ACETYLCHITOTRIOSE.
RX PubMed=14623194; DOI=10.1016/j.jmb.2003.09.076;
RA Hayashida M., Fujii T., Hamasu M., Ishiguro M., Hata Y.;
RT "Similarity between protein-protein and protein-carbohydrate interactions,
RT revealed by two crystal structures of lectins from the roots of pokeweed.";
RL J. Mol. Biol. 334:551-565(2003).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX PubMed=15039554; DOI=10.1107/s090744490400232x;
RA Fujii T., Hayashida M., Hamasu M., Ishiguro M., Hata Y.;
RT "Structures of two lectins from the roots of pokeweed (Phytolacca
RT americana).";
RL Acta Crystallogr. D 60:665-673(2004).
CC -!- FUNCTION: N-acetyl-D-glucosamine binding lectin. Shows no
CC hemagglutinating activity towards rabbit erythrocytes and weak activity
CC towards trypsin-treated erythrocytes. Has mitogenic activity towards
CC human peripheral blood lymphocytes (HPBL).
CC {ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15277769,
CC ECO:0000269|PubMed:8987560}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:14623194,
CC ECO:0000269|PubMed:15277769}.
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DR PDB; 1UHA; X-ray; 1.50 A; A=1-82.
DR PDB; 1ULM; X-ray; 1.80 A; A/B=1-82.
DR PDB; 1ULN; X-ray; 1.65 A; A=1-82.
DR PDBsum; 1UHA; -.
DR PDBsum; 1ULM; -.
DR PDBsum; 1ULN; -.
DR AlphaFoldDB; P83790; -.
DR SMR; P83790; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR UniLectin; P83790; -.
DR EvolutionaryTrace; P83790; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IDA:UniProtKB.
DR Gene3D; 3.30.60.10; -; 2.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR Pfam; PF00187; Chitin_bind_1; 2.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 2.
DR SUPFAM; SSF57016; SSF57016; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Chitin-binding; Direct protein sequencing; Disulfide bond;
KW Lectin; Mitogen; Repeat.
FT CHAIN 1..82
FT /note="Lectin-D2"
FT /id="PRO_0000124812"
FT DOMAIN 1..42
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 43..82
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT BINDING 20
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 22
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 24
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 31
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 43
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 61
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 63
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 65
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT BINDING 72
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:14623194"
FT DISULFID 4..19
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 13..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 18..32
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 36..40
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 45..60
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 54..66
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 59..73
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT DISULFID 77..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:14623194, ECO:0000269|PubMed:15039554"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:1UHA"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:1UHA"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1UHA"
FT HELIX 29..32
FT /evidence="ECO:0007829|PDB:1UHA"
FT TURN 40..43
FT /evidence="ECO:0007829|PDB:1UHA"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1UHA"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:1UHA"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:1UHA"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1ULM"
SQ SEQUENCE 82 AA; 9103 MW; 1E65B08E58A80037 CRC64;
APECGERASG KRCPNGKCCS QWGYCGTTDN YCGQGCQSQC DYWRCGRDFG GRLCEEDMCC
SKYGWCGYSD DHCEDGCQSQ CD
