LEC_GALNI
ID LEC_GALNI Reviewed; 157 AA.
AC P30617;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Mannose-specific lectin {ECO:0000303|PubMed:1718752};
DE AltName: Full=Agglutinin {ECO:0000303|PubMed:1718752};
DE AltName: Full=LecGNA 2 {ECO:0000303|PubMed:1718752};
DE AltName: Full=Snowdrop lectin {ECO:0000303|PubMed:1718752, ECO:0000303|PubMed:34537212, ECO:0000303|PubMed:8939757};
DE Flags: Precursor;
OS Galanthus nivalis (Common snowdrop).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Amaryllidaceae;
OC Amaryllidoideae; Galanthus.
OX NCBI_TaxID=4670;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=1718752; DOI=10.1111/j.1432-1033.1991.tb16339.x;
RA van Damme E.J.M., Kaku H., Perini F., Goldstein I.J., Peeters B., Yagi F.,
RA Decock B., Peumans W.J.;
RT "Biosynthesis, primary structure and molecular cloning of snowdrop
RT (Galanthus nivalis L.) lectin.";
RL Eur. J. Biochem. 202:23-30(1991).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND DISULFIDE BOND.
RX PubMed=8939757; DOI=10.1016/s0969-2126(96)00141-4;
RA Wright C.S., Hester G.;
RT "The 2.0 A structure of a cross-linked complex between snowdrop lectin and
RT a branched mannopentaose: evidence for two unique binding modes.";
RL Structure 4:1339-1352(1996).
RN [3]
RP BIOTECHNOLOGY, AND RECOMBINANT EXPRESSION AS A CHIMERIC VARIANT.
RX PubMed=34537212; DOI=10.1016/j.toxicon.2021.09.001;
RA Khoshdel Nezamiha F., Imani S., Arabi Mianroodi R., Tirgari S.,
RA Shahbazzadeh D.;
RT "OdTx12/GNA, a chimeric variant of a beta excitatory toxin from
RT Odontobuthus doriae, reveals oral toxicity towards Locusta migratoria and
RT Tenebrio molitor.";
RL Toxicon 202:13-19(2021).
CC -!- FUNCTION: Mannose-specific lectin.
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- BIOTECHNOLOGY: Can be used as a chimeric variant with insecticidal
CC venom toxins to obtain biological insecticide candidates. This lectin
CC has receptors on insect midgut and this allows its internalization into
CC insects hemolymph. In an other hand, scorpion and spiders toxins are
CC naturally not toxic when administered orally to insect larvae, but a
CC fusion with this lectin makes them toxic for the larvae that would eat
CC them. {ECO:0000305|PubMed:34537212}.
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DR EMBL; M55556; AAA33346.1; -; mRNA.
DR PIR; S19735; S19735.
DR PDB; 1JPC; X-ray; 2.00 A; A=24-132.
DR PDB; 1MSA; X-ray; 2.29 A; A/B/C/D=24-132.
DR PDB; 1NIV; X-ray; 3.00 A; A/C=24-132.
DR PDBsum; 1JPC; -.
DR PDBsum; 1MSA; -.
DR PDBsum; 1NIV; -.
DR AlphaFoldDB; P30617; -.
DR SMR; P30617; -.
DR UniLectin; P30617; -.
DR EvolutionaryTrace; P30617; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005537; F:mannose binding; IEA:UniProtKB-KW.
DR CDD; cd00028; B_lectin; 1.
DR Gene3D; 2.90.10.10; -; 1.
DR InterPro; IPR001480; Bulb-type_lectin_dom.
DR InterPro; IPR036426; Bulb-type_lectin_dom_sf.
DR SMART; SM00108; B_lectin; 1.
DR SUPFAM; SSF51110; SSF51110; 1.
DR PROSITE; PS50927; BULB_LECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Lectin;
KW Mannose-binding; Secreted; Signal.
FT SIGNAL 1..19
FT /note="Or 23; in 70% of the molecules"
FT CHAIN 20..128
FT /note="Mannose-specific lectin"
FT /id="PRO_0000021586"
FT PROPEP 129..157
FT /note="Removed in mature form"
FT /id="PRO_0000021587"
FT DOMAIN 24..132
FT /note="Bulb-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00038"
FT DISULFID 52..75
FT /evidence="ECO:0000269|PubMed:8939757,
FT ECO:0007744|PDB:1JPC, ECO:0007744|PDB:1MSA,
FT ECO:0007744|PDB:1NIV"
FT VARIANT 21
FT /note="C -> Y"
FT VARIANT 74
FT /note="S -> H"
FT VARIANT 76
FT /note="F -> Y"
FT VARIANT 109
FT /note="C -> S"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 44..48
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 54..58
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1JPC"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:1JPC"
SQ SEQUENCE 157 AA; 16917 MW; B63AE3124DA2252B CRC64;
MAKASLLILA AIFLGVITPS CLSDNILYSG ETLSTGEFLN YGSFVFIMQE DCNLVLYDVD
KPIWATNTGG LSRSCFLSMQ TDGNLVVYNP SNKPIWASNT GGQNGNYVCI LQKDRNVVIY
GTDRWATGTH TGLVGIPASP PSEKYPTAGK IKLVTAK
