AGI2_WHEAT
ID AGI2_WHEAT Reviewed; 213 AA.
AC P02876;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 3.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Agglutinin isolectin 2;
DE AltName: Full=Isolectin D;
DE AltName: Full=WGA2;
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 28-198, AND PYROGLUTAMATE FORMATION AT GLN-28.
RC TISSUE=Germ;
RX PubMed=6546522; DOI=10.1021/bi00297a017;
RA Wright C.S., Gavilanes F., Peterson D.L.;
RT "Primary structure of wheat germ agglutinin isolectin 2. Peptide order
RT deduced from X-ray structure.";
RL Biochemistry 23:280-287(1984).
RN [3]
RP SEQUENCE REVISION TO 68; 136; 161 AND 177.
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 [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=871318; DOI=10.1016/s0022-2836(77)80063-6;
RA Wright C.S.;
RT "The crystal structure of wheat germ agglutinin at 2.2-A resolution.";
RL J. Mol. Biol. 111:439-457(1977).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=3625772; DOI=10.1016/0022-2836(87)90678-4;
RA Wright C.S.;
RT "Refinement of the crystal structure of wheat germ agglutinin isolectin 2
RT at 1.8-A resolution.";
RL J. Mol. Biol. 194:501-529(1987).
RN [6]
RP ERRATUM OF PUBMED:3625772.
RA Wright C.S.;
RL J. Mol. Biol. 199:239-239(1988).
CC -!- FUNCTION: N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding
CC lectin.
CC -!- SUBUNIT: Homodimer, u-shaped.
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; M25537; AAA34258.1; -; mRNA.
DR PIR; S09624; AEWT2.
DR PDB; 2WGC; X-ray; 2.20 A; A/B=29-198.
DR PDB; 9WGA; X-ray; 1.80 A; A/B=29-198.
DR PDBsum; 2WGC; -.
DR PDBsum; 9WGA; -.
DR AlphaFoldDB; P02876; -.
DR PCDDB; P02876; -.
DR SMR; P02876; -.
DR Allergome; 650; Tri a 18.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR UniLectin; P02876; -.
DR PRIDE; P02876; -.
DR EnsemblPlants; TraesCAD_scaffold_106355_01G000100.1; TraesCAD_scaffold_106355_01G000100.1; TraesCAD_scaffold_106355_01G000100.
DR EnsemblPlants; TraesCLE_scaffold_123220_01G000200.1; TraesCLE_scaffold_123220_01G000200.1; TraesCLE_scaffold_123220_01G000200.
DR EnsemblPlants; TraesPAR_scaffold_100131_01G000200.1; TraesPAR_scaffold_100131_01G000200.1; TraesPAR_scaffold_100131_01G000200.
DR EnsemblPlants; TraesROB_scaffold_105401_01G000100.1; TraesROB_scaffold_105401_01G000100.1; TraesROB_scaffold_105401_01G000100.
DR EnsemblPlants; TraesWEE_scaffold_107152_01G000200.1; TraesWEE_scaffold_107152_01G000200.1; TraesWEE_scaffold_107152_01G000200.
DR Gramene; TraesCAD_scaffold_106355_01G000100.1; TraesCAD_scaffold_106355_01G000100.1; TraesCAD_scaffold_106355_01G000100.
DR Gramene; TraesCLE_scaffold_123220_01G000200.1; TraesCLE_scaffold_123220_01G000200.1; TraesCLE_scaffold_123220_01G000200.
DR Gramene; TraesPAR_scaffold_100131_01G000200.1; TraesPAR_scaffold_100131_01G000200.1; TraesPAR_scaffold_100131_01G000200.
DR Gramene; TraesROB_scaffold_105401_01G000100.1; TraesROB_scaffold_105401_01G000100.1; TraesROB_scaffold_105401_01G000100.
DR Gramene; TraesWEE_scaffold_107152_01G000200.1; TraesWEE_scaffold_107152_01G000200.1; TraesWEE_scaffold_107152_01G000200.
DR EvolutionaryTrace; P02876; -.
DR PRO; PR:P02876; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; P02876; baseline and 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; Direct protein sequencing; Disulfide bond;
KW Lectin; Pyrrolidone carboxylic acid; Reference proteome; Repeat; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000269|PubMed:6546522"
FT CHAIN 28..198
FT /note="Agglutinin isolectin 2"
FT /id="PRO_0000005257"
FT PROPEP 199..213
FT /id="PRO_0000005258"
FT DOMAIN 28..69
FT /note="Chitin-binding type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 70..112
FT /note="Chitin-binding type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 113..155
FT /note="Chitin-binding type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT DOMAIN 156..198
FT /note="Chitin-binding type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT BINDING 37..39
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 89..100
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 141..142
FT /ligand="substrate"
FT MOD_RES 28
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:6546522"
FT DISULFID 30..45
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 39..51
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 44..58
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 62..67
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 73..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 82..94
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 87..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 105..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 116..131
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 125..137
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 130..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 148..153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 159..174
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 168..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 173..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT DISULFID 191..196
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261,
FT ECO:0000269|PubMed:6546522"
FT CONFLICT 64
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 83..85
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:9WGA"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:2WGC"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:2WGC"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2WGC"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:9WGA"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:9WGA"
SQ SEQUENCE 213 AA; 21356 MW; F656A5C9277148AF CRC64;
MRKMMSTMAL TLGAAVFLAF AAATAQAQRC GEQGSNMECP NNLCCSQYGY CGMGGDYCGK
GCQNGACWTS KRCGSQAGGA TCPNNHCCSQ YGHCGFGAEY CGAGCQGGPC RADIKCGSQS
GGKLCPNNLC CSQWGFCGLG SEFCGGGCQS GACSTDKPCG KDAGGRVCTN NYCCSKWGSC
GIGPGYCGAG CQSGGCDAVF AGAITANSTL LAE
