CGL2_COPCI
ID CGL2_COPCI Reviewed; 150 AA.
AC Q9P4R8; Q92214;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Galectin-2;
DE AltName: Full=Cgl-II;
DE AltName: Full=Galectin II;
GN Name=Cgl2;
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 [MRNA], PROTEIN SEQUENCE OF 1-20, FUNCTION, AND MASS
RP SPECTROMETRY.
RC STRAIN=JR52;
RX PubMed=8999822; DOI=10.1074/jbc.272.3.1514;
RA Cooper D.N.W., Boulianne R.P., Charlton S., Farrell E.M., Sucher A.,
RA Lu B.C.;
RT "Fungal galectins, sequence and specificity of two isolectins from Coprinus
RT cinereus.";
RL J. Biol. Chem. 272:1514-1521(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=AmutBmut;
RX PubMed=10931889; DOI=10.1099/00221287-146-8-1841;
RA Boulianne R.P., Liu Y., Aebi M., Lu B.C., Kuees U.;
RT "Fruiting body development in Coprinus cinereus: regulated expression of
RT two galectins secreted by a non-classical pathway.";
RL Microbiology 146:1841-1853(2000).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH LACTOSE AND SUBSTRATE
RP ANALOGS, FUNCTION, SUBUNIT, AND MUTAGENESIS OF ARG-55; TRP-72; PRO-146;
RP LEU-147 AND PRO-148.
RX PubMed=15062091; DOI=10.1016/j.str.2004.03.002;
RA Walser P.J., Haebel P.W., Kuenzler M., Sargent D., Kuees U., Aebi M.,
RA Ban N.;
RT "Structure and functional analysis of the fungal galectin CGL2.";
RL Structure 12:689-702(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP FUNCTION, AND MUTAGENESIS OF TRP-72.
RX PubMed=20062796; DOI=10.1371/journal.ppat.1000717;
RA Butschi A., Titz A., Waelti M.A., Olieric V., Paschinger K., Noebauer K.,
RA Guo X., Seeberger P.H., Wilson I.B., Aebi M., Hengartner M.O., Kuenzler M.;
RT "Caenorhabditis elegans N-glycan core beta-galactoside confers sensitivity
RT towards nematotoxic fungal galectin CGL2.";
RL PLoS Pathog. 6:E1000717-E1000717(2010).
CC -!- FUNCTION: Binds lactose (PubMed:8999822, PubMed:15062091). May play a
CC role in fruiting body formation (PubMed:8999822). Displays toxicity
CC towards the nematode C.elegans by binding to a specific Gal-beta-1,4-
CC Fuc-alpha-1,6 modification of N-glycan cores on C.elegans intestinal
CC cells (PubMed:20062796). {ECO:0000269|PubMed:15062091,
CC ECO:0000269|PubMed:20062796, ECO:0000269|PubMed:8999822}.
CC -!- SUBUNIT: Homotetramer. Oligomerization is required for carbohydrate
CC binding. {ECO:0000269|PubMed:15062091}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000269|PubMed:10931889}. Secreted, cell wall
CC {ECO:0000269|PubMed:10931889}. Endomembrane system
CC {ECO:0000269|PubMed:10931889}. Note=Detected in extracellular matrix,
CC cell wall and cytoplasmic membrane-bound bodies.
CC -!- MASS SPECTROMETRY: Mass=16672; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8999822};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=CGL2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_oth_Stlect_379";
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DR EMBL; U64676; AAB06178.1; -; mRNA.
DR EMBL; AF130360; AAF34732.1; -; Genomic_DNA.
DR PDB; 1UL9; X-ray; 2.22 A; A/B=1-150.
DR PDB; 1ULC; X-ray; 2.60 A; A/B=1-150.
DR PDB; 1ULD; X-ray; 2.10 A; A/B/C/D=1-150.
DR PDB; 1ULE; X-ray; 2.15 A; A/B=1-150.
DR PDB; 1ULF; X-ray; 2.36 A; A/B=1-150.
DR PDB; 1ULG; X-ray; 2.20 A; A/B/C/D=1-150.
DR PDB; 2WKK; X-ray; 1.50 A; A/B/C/D=1-150.
DR PDBsum; 1UL9; -.
DR PDBsum; 1ULC; -.
DR PDBsum; 1ULD; -.
DR PDBsum; 1ULE; -.
DR PDBsum; 1ULF; -.
DR PDBsum; 1ULG; -.
DR PDBsum; 2WKK; -.
DR AlphaFoldDB; Q9P4R8; -.
DR SMR; Q9P4R8; -.
DR UniLectin; Q9P4R8; -.
DR VEuPathDB; FungiDB:CC1G_05005; -.
DR VEuPathDB; FungiDB:CC2G_013120; -.
DR EvolutionaryTrace; Q9P4R8; -.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001079; Galectin_CRD.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Extracellular matrix;
KW Fruiting body; Lectin; Membrane; Secreted.
FT CHAIN 1..150
FT /note="Galectin-2"
FT /id="PRO_0000076968"
FT DOMAIN 9..141
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 51
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:15062091,
FT ECO:0000269|PubMed:20062796, ECO:0007744|PDB:1ULC,
FT ECO:0007744|PDB:1ULD, ECO:0007744|PDB:1ULE,
FT ECO:0007744|PDB:1ULF, ECO:0007744|PDB:1ULG,
FT ECO:0007744|PDB:2WKK"
FT BINDING 55
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:15062091,
FT ECO:0000269|PubMed:20062796, ECO:0007744|PDB:1ULC,
FT ECO:0007744|PDB:1ULD, ECO:0007744|PDB:1ULE,
FT ECO:0007744|PDB:1ULF, ECO:0007744|PDB:1ULG,
FT ECO:0007744|PDB:2WKK"
FT BINDING 64
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:15062091,
FT ECO:0000269|PubMed:20062796, ECO:0007744|PDB:1ULC,
FT ECO:0007744|PDB:1ULD, ECO:0007744|PDB:1ULE,
FT ECO:0007744|PDB:1ULF, ECO:0007744|PDB:1ULG,
FT ECO:0007744|PDB:2WKK"
FT BINDING 75
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:15062091,
FT ECO:0000269|PubMed:20062796, ECO:0007744|PDB:1ULG"
FT BINDING 77
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:20062796"
FT MUTAGEN 55
FT /note="R->A: Completely abolishes carbohydrate binding.
FT Loss of toxicity towards C.elegans."
FT /evidence="ECO:0000269|PubMed:15062091,
FT ECO:0000269|PubMed:20062796"
FT MUTAGEN 72
FT /note="W->G: Completely abolishes carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:15062091"
FT MUTAGEN 146
FT /note="P->G: Reduces the stability of the tetrameric
FT structure."
FT /evidence="ECO:0000269|PubMed:15062091"
FT MUTAGEN 147
FT /note="L->S: Reduces the stability of the tetrameric
FT structure."
FT /evidence="ECO:0000269|PubMed:15062091"
FT MUTAGEN 148
FT /note="P->G: Reduces the stability of the tetrameric
FT structure."
FT /evidence="ECO:0000269|PubMed:15062091"
FT CONFLICT 99
FT /note="R -> K (in Ref. 1; AAB06178)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="A -> T (in Ref. 1; AAB06178)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="N -> S (in Ref. 1; AAB06178)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="L -> S (in Ref. 1; AAB06178)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="P -> A (in Ref. 1; AAB06178)"
FT /evidence="ECO:0000305"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:2WKK"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1ULG"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 97..103
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 120..129
FT /evidence="ECO:0007829|PDB:2WKK"
FT STRAND 134..143
FT /evidence="ECO:0007829|PDB:2WKK"
SQ SEQUENCE 150 AA; 16748 MW; EA6914570761AD7B CRC64;
MLYHLFVNNQ VKLQNDFKPE SVAAIRSSAF NSKGGTTVFN FLSAGENILL HISIRPGENV
IVFNSRLKNG AWGPEERIPY AEKFRPPNPS ITVIDHGDRF QIRFDYGTSI YYNKRIKENA
AAIAYNAENS LFSSPVTVDV HGLLPPLPPA
