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 27-MAR-2024, entry version 152. 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. 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; 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 STRING; 4565.P02876; -. DR Allergome; 650; Tri a 18. DR CAZy; CBM18; Carbohydrate-Binding Module Family 18. DR UniLectin; 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; TraesKAR1D01G0303010.1; cds.TraesKAR1D01G0303010.1; TraesKAR1D01G0303010. 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; TraesKAR1D01G0303010.1; cds.TraesKAR1D01G0303010.1; TraesKAR1D01G0303010. 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 OrthoDB; 367498at2759; -. DR EvolutionaryTrace; P02876; -. DR PRO; PR:P02876; -. DR Proteomes; UP000019116; Unplaced. DR ExpressionAtlas; P02876; baseline. DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW. DR CDD; cd00035; ChtBD1; 4. DR Gene3D; 3.30.60.10; Endochitinase-like; 4. DR InterPro; IPR001002; Chitin-bd_1. DR InterPro; IPR018371; Chitin-binding_1_CS. DR InterPro; IPR036861; Endochitinase-like_sf. DR PANTHER; PTHR47849; CHITIN-BINDING LECTIN 1; 1. DR PANTHER; PTHR47849:SF8; LECTIN; 1. DR Pfam; PF00187; Chitin_bind_1; 4. DR PRINTS; PR00451; CHITINBINDNG. DR SMART; SM00270; ChtBD1; 4. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 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 //