ID   CGL1_COPC7              Reviewed;         150 AA.
AC   A8NSH0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Galectin-1;
GN   Name=Cgl1; ORFNames=CC1G_05003;
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homotetramer. Oligomerization is required for carbohydrate
CC       binding. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix {ECO:0000250}. Secreted, cell wall {ECO:0000250}. Endomembrane
CC       system {ECO:0000250}. Note=Detected in extracellular matrix, cell wall
CC       and cytoplasmic membrane-bound bodies. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Most abundant in fruiting bodies. Very low levels
CC       of expression in asexual vegetative mycelia.
CC   -!- DEVELOPMENTAL STAGE: Most abundant prior to premeiotic S-phase, remains
CC       high from karyogamy to early pachytene, declines drastically by late
CC       pachytene and diplotene, and is undetectable by sterigma stage.
CC   -!- INDUCTION: Repressed by continuous light. {ECO:0000250}.
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DR   EMBL; AACS02000008; EAU85786.2; -; Genomic_DNA.
DR   RefSeq; XP_001836010.2; XM_001835958.2.
DR   AlphaFoldDB; A8NSH0; -.
DR   SMR; A8NSH0; -.
DR   EnsemblFungi; EAU85786; EAU85786; CC1G_05003.
DR   GeneID; 6012550; -.
DR   KEGG; cci:CC1G_05003; -.
DR   VEuPathDB; FungiDB:CC1G_05003; -.
DR   eggNOG; ENOG502SYUU; Eukaryota.
DR   HOGENOM; CLU_117277_0_0_1; -.
DR   InParanoid; A8NSH0; -.
DR   OMA; VRVWINI; -.
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   2: Evidence at transcript level;
KW   Cell wall; Extracellular matrix; Fruiting body; Lectin; Membrane;
KW   Reference proteome; Secreted.
FT   CHAIN           1..150
FT                   /note="Galectin-1"
FT                   /id="PRO_0000333261"
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"
FT   BINDING         55
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
FT   BINDING         75
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   150 AA;  16408 MW;  9DAF46E0AC860AF0 CRC64;
     MLYHLFVNNQ IKLQDDFKAE AVATIRSSVF NSKGGTTVFN FLSAGENILL HISIRPGENA
     IVFNSRTKGG AWGPEERVPY AGKFKGPNPS ITVLDHGDRF QILFDNATAI YYTKRIKENA
     AAIAYSAENS LFSSPVTVDI HGLLPPLPPA