AGI1_WHEAT
ID AGI1_WHEAT Reviewed; 212 AA.
AC P10968;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Agglutinin isolectin 1;
DE AltName: Full=Isolectin A;
DE AltName: Full=WGA1;
DE Flags: Precursor;
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=2491677; DOI=10.1007/bf00027321;
RA Smith J.J., Raikhel N.V.;
RT "Nucleotide sequences of cDNA clones encoding wheat germ agglutinin
RT isolectins A and D.";
RL Plant Mol. Biol. 13:601-603(1989).
RN [2]
RP PROTEIN SEQUENCE OF 27-197.
RC TISSUE=Germ;
RX PubMed=2499688; DOI=10.1007/bf02103429;
RA Wright C.S., Raikhel N.V.;
RT "Sequence variability in three wheat germ agglutinin isolectins: products
RT of multiple genes in polyploid wheat.";
RL J. Mol. Evol. 28:327-336(1989).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-197, AND PYROGLUTAMATE
RP FORMATION AT GLN-27.
RX PubMed=2585496; DOI=10.1016/0022-2836(89)90011-9;
RA Wright C.S.;
RT "Comparison of the refined crystal structures of two wheat germ
RT isolectins.";
RL J. Mol. Biol. 209:475-487(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP N-ACETYLNEURAMINYL-LACTOSE.
RX PubMed=2231724; DOI=10.1016/s0022-2836(05)80174-3;
RA Wright C.S.;
RT "2.2-A resolution structure analysis of two refined N-acetylneuraminyl-
RT lactose-wheat germ agglutinin isolectin complexes.";
RL J. Mol. Biol. 215:635-651(1990).
CC -!- FUNCTION: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding
CC lectin.
CC -!- SUBUNIT: Homodimer, u-shaped. {ECO:0000269|PubMed:2231724}.
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; M25536; AAA34256.1; -; mRNA.
DR PIR; S09623; S09623.
DR PDB; 1WGC; X-ray; 2.20 A; A/B=28-197.
DR PDB; 2CWG; X-ray; 2.00 A; A/B=28-197.
DR PDB; 2UVO; X-ray; 1.40 A; A/B/E/F=28-197.
DR PDB; 2X3T; X-ray; 2.75 A; A/B/C/D=28-197.
DR PDB; 4AML; X-ray; 1.60 A; A/B=28-197.
DR PDB; 7WGA; X-ray; 2.00 A; A/B=28-197.
DR PDBsum; 1WGC; -.
DR PDBsum; 2CWG; -.
DR PDBsum; 2UVO; -.
DR PDBsum; 2X3T; -.
DR PDBsum; 4AML; -.
DR PDBsum; 7WGA; -.
DR AlphaFoldDB; P10968; -.
DR SMR; P10968; -.
DR STRING; 4565.Traes_1AL_B8B0A092C.1; -.
DR Allergome; 3501; Tri a 18.0101.
DR Allergome; 650; Tri a 18.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR UniLectin; P10968; -.
DR PRIDE; P10968; -.
DR EnsemblPlants; TraesCAD_scaffold_008297_01G000100.1; TraesCAD_scaffold_008297_01G000100.1; TraesCAD_scaffold_008297_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_063355_01G000600.1; TraesCLE_scaffold_063355_01G000600.1; TraesCLE_scaffold_063355_01G000600.
DR EnsemblPlants; TraesCS1A02G326800.1; TraesCS1A02G326800.1.cds1; TraesCS1A02G326800.
DR EnsemblPlants; TraesPAR_scaffold_047948_01G000700.1; TraesPAR_scaffold_047948_01G000700.1; TraesPAR_scaffold_047948_01G000700.
DR EnsemblPlants; TraesROB_scaffold_060582_01G000700.1; TraesROB_scaffold_060582_01G000700.1; TraesROB_scaffold_060582_01G000700.
DR EnsemblPlants; TraesWEE_scaffold_003839_01G001400.1; TraesWEE_scaffold_003839_01G001400.1; TraesWEE_scaffold_003839_01G001400.
DR Gramene; TraesCAD_scaffold_008297_01G000100.1; TraesCAD_scaffold_008297_01G000100.1; TraesCAD_scaffold_008297_01G000100.
DR Gramene; TraesCLE_scaffold_063355_01G000600.1; TraesCLE_scaffold_063355_01G000600.1; TraesCLE_scaffold_063355_01G000600.
DR Gramene; TraesCS1A02G326800.1; TraesCS1A02G326800.1.cds1; TraesCS1A02G326800.
DR Gramene; TraesPAR_scaffold_047948_01G000700.1; TraesPAR_scaffold_047948_01G000700.1; TraesPAR_scaffold_047948_01G000700.
DR Gramene; TraesROB_scaffold_060582_01G000700.1; TraesROB_scaffold_060582_01G000700.1; TraesROB_scaffold_060582_01G000700.
DR Gramene; TraesWEE_scaffold_003839_01G001400.1; TraesWEE_scaffold_003839_01G001400.1; TraesWEE_scaffold_003839_01G001400.
DR eggNOG; ENOG502S7G0; Eukaryota.
DR HOGENOM; CLU_112193_0_0_1; -.
DR OMA; AGNCGPQ; -.
DR EvolutionaryTrace; P10968; -.
DR PRO; PR:P10968; -.
DR Proteomes; UP000019116; Unplaced.
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; Direct protein sequencing; Disulfide bond;
KW Lectin; Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:2499688"
FT CHAIN 27..197
FT /note="Agglutinin isolectin 1"
FT /id="PRO_0000005255"
FT PROPEP 198..212
FT /id="PRO_0000005256"
FT DOMAIN 27..68
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 69..111
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 112..154
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 155..197
FT /note="Chitin-binding type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT BINDING 36..38
FT /ligand="substrate"
FT BINDING 88..99
FT /ligand="substrate"
FT BINDING 140..141
FT /ligand="substrate"
FT MOD_RES 27
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:2585496"
FT DISULFID 29..44
FT DISULFID 38..50
FT DISULFID 43..57
FT DISULFID 61..66
FT DISULFID 72..87
FT DISULFID 81..93
FT DISULFID 86..100
FT DISULFID 104..109
FT DISULFID 115..130
FT DISULFID 124..136
FT DISULFID 129..143
FT DISULFID 147..152
FT DISULFID 158..173
FT DISULFID 167..179
FT DISULFID 172..186
FT DISULFID 190..195
FT CONFLICT 63
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:2CWG"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 116..119
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:2X3T"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:2UVO"
FT TURN 160..164
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4AML"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2UVO"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:2UVO"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:2UVO"
SQ SEQUENCE 212 AA; 21239 MW; EC7B6F007DDC15EB CRC64;
MKMMSTRALA LGAAAVLAFA AATAQAQRCG EQGSNMECPN NLCCSQYGYC GMGGDYCGKG
CQNGACWTSK RCGSQAGGAT CTNNQCCSQY GYCGFGAEYC GAGCQGGPCR ADIKCGSQAG
GKLCPNNLCC SQWGFCGLGS EFCGGGCQSG ACSTDKPCGK DAGGRVCTNN YCCSKWGSCG
IGPGYCGAGC QSGGCDGVFA EAITANSTLL QE
