CGL3_COPCI
ID CGL3_COPCI Reviewed; 164 AA.
AC Q206Z5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Galectin-3;
DE AltName: Full=Cgl-III;
DE AltName: Full=Galectin III;
GN Name=Cgl3;
OS Coprinopsis cinerea (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=5346;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=AmutBmut;
RX PubMed=16607020; DOI=10.1128/ec.5.4.732-744.2006;
RA Waelti M.A., Villalba C., Buser R.M., Gruenler A., Aebi M., Kuenzler M.;
RT "Targeted gene silencing in the model mushroom Coprinopsis cinerea
RT (Coprinus cinereus) by expression of homologous hairpin RNAs.";
RL Eukaryot. Cell 5:732-744(2006).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CHITOTRIOSE,
RP FUNCTION, SUBUNIT, MUTAGENESIS OF ILE-43; ASN-45; ARG-81 AND ASN-138, AND
RP INDUCTION.
RX PubMed=18440554; DOI=10.1016/j.jmb.2008.03.062;
RA Waelti M.A., Walser P.J., Thore S., Gruenler A., Bednar M., Kuenzler M.,
RA Aebi M.;
RT "Structural basis for chitotetraose coordination by CGL3, a novel galectin-
RT related protein from Coprinopsis cinerea.";
RL J. Mol. Biol. 379:146-159(2008).
CC -!- FUNCTION: Binds complex carbohydrates, such as chitooligosaccharides.
CC Does not bind lactose. May play a role in fruiting body formation.
CC {ECO:0000269|PubMed:18440554}.
CC -!- SUBUNIT: Homotetramer. Oligomerization is required for carbohydrate
CC binding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC -!- INDUCTION: Induced during fruiting body formation.
CC {ECO:0000269|PubMed:16607020, ECO:0000269|PubMed:18440554}.
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DR EMBL; DQ408306; ABD64675.1; -; Genomic_DNA.
DR PDB; 2R0F; X-ray; 2.00 A; A/B=1-164.
DR PDB; 2R0H; X-ray; 1.90 A; A/B/C/D=1-164.
DR PDBsum; 2R0F; -.
DR PDBsum; 2R0H; -.
DR AlphaFoldDB; Q206Z5; -.
DR SMR; Q206Z5; -.
DR UniLectin; Q206Z5; -.
DR VEuPathDB; FungiDB:CC1G_00723; -.
DR VEuPathDB; FungiDB:CC2G_000186; -.
DR EvolutionaryTrace; Q206Z5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Extracellular matrix; Fruiting body; Lectin;
KW Secreted.
FT CHAIN 1..164
FT /note="Galectin-3"
FT /id="PRO_0000333263"
FT DOMAIN 9..154
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 45
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 64
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 73
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 81
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 84
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT BINDING 138
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT MUTAGEN 43
FT /note="I->A: Abolishes chitooligosaccharide binding; when
FT associated with A-45."
FT /evidence="ECO:0000269|PubMed:18440554"
FT MUTAGEN 45
FT /note="N->A: Abolishes chitooligosaccharide binding; when
FT associated with A-43."
FT /evidence="ECO:0000269|PubMed:18440554"
FT MUTAGEN 81
FT /note="R->A: Alters binding specificity, leading to lactose
FT binding and reduced affinity for chitooligosaccharide."
FT /evidence="ECO:0000269|PubMed:18440554"
FT MUTAGEN 81
FT /note="R->W: Alters binding specificity, leading to lactose
FT binding and loss of chitooligosaccharide binding."
FT /evidence="ECO:0000269|PubMed:18440554"
FT MUTAGEN 138
FT /note="N->A: Abolishes chitooligosaccharide binding."
FT /evidence="ECO:0000269|PubMed:18440554"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2R0H"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:2R0F"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2R0H"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:2R0H"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2R0F"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 107..114
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:2R0H"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:2R0H"
FT HELIX 156..159
FT /evidence="ECO:0007829|PDB:2R0H"
SQ SEQUENCE 164 AA; 18735 MW; 4AAF6E1507F88617 CRC64;
MFHILRLEST VDLSEPLKDN GIIVFQSDKL DLEPSPNLGP TGIDNTNVNL INAKGDVLLH
IGIRRRENAF VFNSIPYGES RGPEERIPLE GTFGDRRDPS ITIFDHPDRY QIMIDYKTVY
YYKKRLEGRC EKVSYKINEG QTPPFSDVLG VTVLYFANVM PRAN
