CGL2_COPC7
ID CGL2_COPC7 Reviewed; 150 AA.
AC A8NSH3;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Galectin-2;
DE AltName: Full=Cgl-II;
DE AltName: Full=Galectin II;
GN Name=Cgl2; ORFNames=CC1G_05005;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
CC -!- FUNCTION: Binds lactose. May play a role in fruiting body formation.
CC Displays toxicity towards the nematode C.elegans by binding to a
CC specific Gal-beta-1,4-Fuc-alpha-1,6 modification of N-glycan cores on
CC C.elegans intestinal cells. {ECO:0000250|UniProtKB:Q9P4R8}.
CC -!- SUBUNIT: Homotetramer. Oligomerization is required for carbohydrate
CC binding. {ECO:0000250|UniProtKB:Q9P4R8}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:Q9P4R8}. Secreted, cell wall
CC {ECO:0000250|UniProtKB:Q9P4R8}. Endomembrane system
CC {ECO:0000250|UniProtKB:Q9P4R8}. Note=Detected in extracellular matrix,
CC cell wall and cytoplasmic membrane-bound bodies.
CC {ECO:0000250|UniProtKB:Q9P4R8}.
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DR EMBL; AACS02000008; EAU85788.2; -; Genomic_DNA.
DR RefSeq; XP_001836012.2; XM_001835960.2.
DR AlphaFoldDB; A8NSH3; -.
DR SMR; A8NSH3; -.
DR EnsemblFungi; EAU85788; EAU85788; CC1G_05005.
DR GeneID; 6012552; -.
DR KEGG; cci:CC1G_05005; -.
DR VEuPathDB; FungiDB:CC1G_05005; -.
DR eggNOG; ENOG502SYUU; Eukaryota.
DR HOGENOM; CLU_117277_0_0_1; -.
DR InParanoid; A8NSH3; -.
DR OrthoDB; 829777at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Cell wall; Extracellular matrix; Fruiting body; Lectin; Membrane;
KW Reference proteome; Secreted.
FT CHAIN 1..150
FT /note="Galectin-2"
FT /id="PRO_0000333262"
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:0000250|UniProtKB:Q9P4R8"
FT BINDING 55
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R8"
FT BINDING 64
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R8"
FT BINDING 75
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R8"
FT BINDING 77
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000250|UniProtKB:Q9P4R8"
SQ SEQUENCE 150 AA; 16748 MW; EA6914570761AD7B CRC64;
MLYHLFVNNQ VKLQNDFKPE SVAAIRSSAF NSKGGTTVFN FLSAGENILL HISIRPGENV
IVFNSRLKNG AWGPEERIPY AEKFRPPNPS ITVIDHGDRF QIRFDYGTSI YYNKRIKENA
AAIAYNAENS LFSSPVTVDV HGLLPPLPPA
