AGI3_WHEAT
ID AGI3_WHEAT Reviewed; 186 AA.
AC P10969;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Agglutinin isolectin 3;
DE AltName: Full=WGA3;
DE Flags: Precursor; Fragment;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16578818; DOI=10.1073/pnas.84.19.6745;
RA Raikhel N.V., Wilkins T.A.;
RT "Isolation and characterization of a cDNA clone encoding wheat germ
RT agglutinin.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6745-6749(1987).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), PYROGLUTAMATE FORMATION AT GLN-1,
RP AND SUBUNIT.
RX PubMed=15299769; DOI=10.1107/s0907444995004070;
RA Harata K., Nagahora H., Jigami Y.;
RT "X-ray structure of wheat germ agglutinin isolectin 3.";
RL Acta Crystallogr. D 51:1013-1019(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATES.
RX PubMed=11853952; DOI=10.1016/s0304-4165(01)00231-8;
RA Muraki M., Ishimura M., Harata K.;
RT "Interactions of wheat-germ agglutinin with GlcNAc beta 1,6Gal sequence.";
RL Biochim. Biophys. Acta 1569:10-20(2002).
CC -!- FUNCTION: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding
CC lectin.
CC -!- SUBUNIT: Homodimer, u-shaped. {ECO:0000269|PubMed:11853952,
CC ECO:0000269|PubMed:15299769}.
CC -!- MISCELLANEOUS: The 4 sites proposed for binding to carbohydrates (N-
CC acetyl-D-glucosamine) of receptor molecules are on the surface of the
CC agglutinin molecule.
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DR EMBL; J02961; AAA34257.1; -; mRNA.
DR PIR; A28401; A28401.
DR PDB; 1K7T; X-ray; 2.40 A; A/B=1-186.
DR PDB; 1K7U; X-ray; 2.20 A; A/B=1-186.
DR PDB; 1K7V; X-ray; 2.20 A; A/B=2-186.
DR PDB; 1WGT; X-ray; 1.90 A; A/B=2-186.
DR PDB; 2X52; X-ray; 1.70 A; A/B=2-171.
DR PDBsum; 1K7T; -.
DR PDBsum; 1K7U; -.
DR PDBsum; 1K7V; -.
DR PDBsum; 1WGT; -.
DR PDBsum; 2X52; -.
DR AlphaFoldDB; P10969; -.
DR SMR; P10969; -.
DR Allergome; 650; Tri a 18.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR UniLectin; P10969; -.
DR PRIDE; P10969; -.
DR EnsemblPlants; TraesCAD_scaffold_137513_01G000100.1; TraesCAD_scaffold_137513_01G000100.1; TraesCAD_scaffold_137513_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_122568_01G000100.1; TraesCLE_scaffold_122568_01G000100.1; TraesCLE_scaffold_122568_01G000100.
DR EnsemblPlants; TraesPAR_scaffold_127396_01G000100.1; TraesPAR_scaffold_127396_01G000100.1; TraesPAR_scaffold_127396_01G000100.
DR EnsemblPlants; TraesROB_scaffold_145157_01G000100.1; TraesROB_scaffold_145157_01G000100.1; TraesROB_scaffold_145157_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_016939_01G000300.1; TraesWEE_scaffold_016939_01G000300.1; TraesWEE_scaffold_016939_01G000300.
DR Gramene; TraesCAD_scaffold_137513_01G000100.1; TraesCAD_scaffold_137513_01G000100.1; TraesCAD_scaffold_137513_01G000100.
DR Gramene; TraesCLE_scaffold_122568_01G000100.1; TraesCLE_scaffold_122568_01G000100.1; TraesCLE_scaffold_122568_01G000100.
DR Gramene; TraesPAR_scaffold_127396_01G000100.1; TraesPAR_scaffold_127396_01G000100.1; TraesPAR_scaffold_127396_01G000100.
DR Gramene; TraesROB_scaffold_145157_01G000100.1; TraesROB_scaffold_145157_01G000100.1; TraesROB_scaffold_145157_01G000100.
DR Gramene; TraesWEE_scaffold_016939_01G000300.1; TraesWEE_scaffold_016939_01G000300.1; TraesWEE_scaffold_016939_01G000300.
DR EvolutionaryTrace; P10969; -.
DR PRO; PR:P10969; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P10969; differential.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.60.10; -; 4.
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; 4.
DR PRINTS; PR00451; CHITINBINDNG.
DR SMART; SM00270; ChtBD1; 4.
DR SUPFAM; SSF57016; SSF57016; 4.
DR PROSITE; PS00026; CHIT_BIND_I_1; 4.
DR PROSITE; PS50941; CHIT_BIND_I_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Chitin-binding; Disulfide bond; Glycoprotein; Lectin;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat.
FT CHAIN 1..171
FT /note="Agglutinin isolectin 3"
FT /id="PRO_0000005259"
FT PROPEP 172..186
FT /id="PRO_0000005260"
FT DOMAIN 1..42
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 43..85
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 86..128
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 129..171
FT /note="Chitin-binding type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT BINDING 10..12
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 62..73
FT /ligand="substrate"
FT BINDING 114..115
FT /ligand="substrate"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:15299769"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 3..18
FT DISULFID 12..24
FT DISULFID 17..31
FT DISULFID 35..40
FT DISULFID 46..61
FT DISULFID 55..67
FT DISULFID 60..74
FT DISULFID 78..83
FT DISULFID 89..104
FT DISULFID 98..110
FT DISULFID 103..117
FT DISULFID 121..126
FT DISULFID 132..147
FT DISULFID 141..153
FT DISULFID 146..160
FT DISULFID 164..169
FT NON_TER 1
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:2X52"
FT TURN 7..9
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 32..34
FT /evidence="ECO:0007829|PDB:1K7U"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 99..101
FT /evidence="ECO:0007829|PDB:1WGT"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 114..117
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2X52"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2X52"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:2X52"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2X52"
SQ SEQUENCE 186 AA; 18756 MW; 68461A20339378FD CRC64;
QRCGEQGSGM ECPNNLCCSQ YGYCGMGGDY CGKGCQNGAC WTSKRCGSQA GGKTCPNNHC
CSQYGHCGFG AEYCGAGCQG GPCRADIKCG SQAGGKLCPN NLCCSQWGYC GLGSEFCGEG
CQNGACSTDK PCGKDAGGRV CTNNYCCSKW GSCGIGPGYC GAGCQSGGCD GVFAEAIATN
STLLAE
