AGI_URTDI
ID AGI_URTDI Reviewed; 372 AA.
AC P11218; Q9SYR1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Lectin/endochitinase 1;
DE EC=3.2.1.14;
DE AltName: Full=Agglutinin;
DE AltName: Full=UDA;
DE AltName: Full=chia5.1.1;
DE Contains:
DE RecName: Full=Lectin 1;
DE Flags: Precursor;
GN Name=UDA1;
OS Urtica dioica (Great nettle) (Stinging nettle).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Urticaceae; Urtica.
OX NCBI_TaxID=3501;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1375935; DOI=10.1016/s0021-9258(19)49878-5;
RA Lerner D.R., Raikhel N.V.;
RT "The gene for stinging nettle lectin (Urtica dioica agglutinin) encodes
RT both a lectin and a chitinase.";
RL J. Biol. Chem. 267:11085-11091(1992).
RN [2]
RP ERRATUM OF PUBMED:1375935.
RX PubMed=1429618; DOI=10.1016/s0021-9258(18)41729-2;
RA Lerner D.R., Raikhel N.V.;
RL J. Biol. Chem. 267:22694-22694(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MASS SPECTROMETRY.
RC STRAIN=cv. Weerselo;
RX PubMed=10080699; DOI=10.1023/a:1006134932290;
RA Does M.P., Ng D.K., Dekker H.L., Peumans W.J., Houterman P.M.,
RA Van Damme E.J., Cornelissen B.J.;
RT "Characterization of Urtica dioica agglutinin isolectins and the encoding
RT gene family.";
RL Plant Mol. Biol. 39:335-347(1999).
RN [4]
RP PROTEIN SEQUENCE OF 24-112, AND PYROGLUTAMATE FORMATION AT GLN-24.
RX PubMed=1544484; DOI=10.1016/0014-5793(92)80231-5;
RA Beintema J.J., Peumans W.J.;
RT "The primary structure of stinging nettle (Urtica dioica) agglutinin. A
RT two-domain member of the hevein family.";
RL FEBS Lett. 299:131-134(1992).
RN [5]
RP PRELIMINARY PROTEIN SEQUENCE OF 24-54.
RA Chapot M.-P., Peumans W.J., Strosberg A.D.;
RT "Extensive homologies between lectins from non-leguminous plants.";
RL FEBS Lett. 195:231-234(1986).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 24-112 IN COMPLEX WITH
RP TRI-ACETYLCHITOTRIOSE AND TETRA-ACETYLCHITOTETRAOSE, FUNCTION, INTERACTION
RP WITH HUMAN TCR AND MHC, AND DISULFIDE BONDS.
RX PubMed=10873861; DOI=10.1016/s0969-2126(00)00142-8;
RA Saul F.A., Rovira P., Boulot G., van Damme E.J.M., Peumans W.J.,
RA Truffa-Bachi P., Bentley G.A.;
RT "Crystal structure of Urtica dioica agglutinin, a superantigen presented by
RT MHC molecules of class I and class II.";
RL Structure 8:593-603(2000).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-112, SUBUNIT, ZINC BINDING, AND
RP DISULFIDE BONDS.
RX PubMed=11679714; DOI=10.1107/s090744490101232x;
RA Harata K., Schubert W.-D., Muraki M.;
RT "Structure of Urtica dioica agglutinin isolectin I: dimer formation
RT mediated by two zinc ions bound at the sugar-binding site.";
RL Acta Crystallogr. D 57:1513-1517(2001).
CC -!- FUNCTION: Functions both as a chitinase and as a N-acetyl-D-glucosamine
CC binding lectin. Inhibits the growth of several phytopathogenic chitin-
CC containing fungi. Possesses also insecticidal activity and
CC superantigenic properties. {ECO:0000269|PubMed:10873861}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC -!- SUBUNIT: Monomer and homodimer. Zinc favors dimerization. Active in the
CC monomeric form but probably inactive in the dimeric form. The
CC interaction with glycans on the mammalian TCR and MHC molecules of the
CC T-cell and antigen-presenting cell, respectively, is inhibited by
CC oligomers of GlcNAc. {ECO:0000269|PubMed:10873861,
CC ECO:0000269|PubMed:11679714}.
CC -!- INTERACTION:
CC P11218; Q75760: env; Xeno; NbExp=2; IntAct=EBI-8453649, EBI-8453491;
CC -!- TISSUE SPECIFICITY: Rhizomes and inflorescence with immature seeds.
CC -!- PTM: Proteolytically processed to yield a very small protein (8.5 kDa,
CC 86 AA) containing only the two chitin-binding domains.
CC -!- MASS SPECTROMETRY: [Lectin/endochitinase 1]: Mass=9380; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10080699};
CC -!- MASS SPECTROMETRY: [Lectin/endochitinase 1]: Mass=9380.7;
CC Mass_error=0.4; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:10080699};
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; M87302; AAA34219.1; -; mRNA.
DR EMBL; AF059535; AAD03614.1; -; Genomic_DNA.
DR PIR; A44298; A42778.
DR PDB; 1EN2; X-ray; 1.40 A; A=25-112.
DR PDB; 1ENM; X-ray; 1.90 A; A=25-112.
DR PDB; 1IQB; X-ray; 1.90 A; A/B=24-112.
DR PDBsum; 1EN2; -.
DR PDBsum; 1ENM; -.
DR PDBsum; 1IQB; -.
DR AlphaFoldDB; P11218; -.
DR SMR; P11218; -.
DR IntAct; P11218; 1.
DR MINT; P11218; -.
DR CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR CAZy; GH19; Glycoside Hydrolase Family 19.
DR UniLectin; P11218; -.
DR EvolutionaryTrace; P11218; -.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
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 InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SUPFAM; SSF53955; SSF53955; 1.
DR SUPFAM; SSF57016; SSF57016; 2.
DR PROSITE; PS00026; CHIT_BIND_I_1; 2.
DR PROSITE; PS50941; CHIT_BIND_I_2; 2.
DR PROSITE; PS00773; CHITINASE_19_1; 1.
DR PROSITE; PS00774; CHITINASE_19_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Carbohydrate metabolism; Chitin degradation;
KW Chitin-binding; Direct protein sequencing; Disulfide bond; Fungicide;
KW Glycoprotein; Glycosidase; Hydrolase; Lectin; Metal-binding; Plant defense;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Repeat; Signal;
KW Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1544484"
FT CHAIN 24..372
FT /note="Lectin/endochitinase 1"
FT /id="PRO_0000005266"
FT CHAIN 24..112
FT /note="Lectin 1"
FT /id="PRO_0000005267"
FT DOMAIN 24..64
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 REGION 113..128
FT /note="Spacer"
FT REGION 129..372
FT /note="Chitinase"
FT BINDING 24
FT /ligand="substrate"
FT BINDING 42..53
FT /ligand="substrate"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="ligand shared between dimeric partners"
FT MOD_RES 24
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1544484"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 26..41
FT DISULFID 35..47
FT DISULFID 40..54
FT DISULFID 58..62
FT DISULFID 72..87
FT DISULFID 81..93
FT DISULFID 86..100
FT DISULFID 105..109
FT CONFLICT 7
FT /note="S -> A (in Ref. 3; AAD03614)"
FT /evidence="ECO:0000305"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 51..54
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1IQB"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1IQB"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:1IQB"
SQ SEQUENCE 372 AA; 40542 MW; 28E9A2312BF08FD2 CRC64;
MMMRFLSAVV IMSSAMAVGL VSAQRCGSQG GGGTCPALWC CSIWGWCGDS EPYCGRTCEN
KCWSGERSDH RCGAAVGNPP CGQDRCCSVH GWCGGGNDYC SGSKCQYRCS SSVRGPRVAL
SGNSTANSIG NVVVTEPLFD QMFSHRKDCP SQGFYSYHSF LVAAESFPAF GTIGDVATRK
REVAAFLAHI SQATSGERSD VENPHAWGLC HINTTTVTEN DFCTSSDWPC AAGKKYSPRG
PIQLTHNFNY GLAGQAIGED LIQNPDLVEK DPIISFKTAL WFWMSQHDNK PSCHDIVLNA
NSAANRIPNK GVIGNIISRA FGHDDFAVRS SSIGFYKRYC DMLGVSYGHD LKYWFDNTPS
SEFQRIQMRV AA
