CGL1_COPCI
ID CGL1_COPCI Reviewed; 150 AA.
AC Q06100; Q00358;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Galectin-1;
DE AltName: Full=Cgl-I;
DE AltName: Full=Galectin I;
GN Name=Cgl1 {ECO:0000312|EMBL:AAF34731.1};
GN Synonyms=CglI {ECO:0000312|EMBL:AAB04141.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAB04141.1}
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] {ECO:0000305, ECO:0000312|EMBL:AAF34731.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND REPRESSION.
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] {ECO:0000305, ECO:0000312|EMBL:AAB04141.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-129, PROTEIN SEQUENCE OF 1-20, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Fruiting body {ECO:0000269|PubMed:1452023};
RX PubMed=1452023; DOI=10.1016/0378-1119(92)90044-p;
RA Charlton S., Boulianne R.P., Chow Y.-C., Lu B.C.;
RT "Cloning and differential expression during the sexual cycle of a meiotic
RT endonuclease-encoding gene from the basidiomycete Coprinus cinereus.";
RL Gene 122:163-169(1992).
CC -!- FUNCTION: Binds lactose. May play a role in fruiting body formation.
CC {ECO:0000269|PubMed:8999822, ECO:0000303|PubMed:10931889}.
CC -!- SUBUNIT: Homotetramer. Oligomerization is required for carbohydrate
CC binding. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Most abundant in fruiting bodies. Very low levels
CC of expression in asexual vegetative mycelia.
CC {ECO:0000269|PubMed:10931889, ECO:0000269|PubMed:1452023}.
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 {ECO:0000269|PubMed:1452023}.
CC -!- INDUCTION: Repressed by continuous light.
CC {ECO:0000269|PubMed:10931889}.
CC -!- MASS SPECTROMETRY: Mass=16408; Mass_error=1.2; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:8999822};
CC -!- CAUTION: Was originally thought to be an endonuclease subunit.
CC {ECO:0000305|PubMed:1452023}.
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DR EMBL; L03301; AAB04141.1; -; mRNA.
DR EMBL; AF130360; AAF34731.1; -; Genomic_DNA.
DR PIR; PC1254; PC1254.
DR AlphaFoldDB; Q06100; -.
DR SMR; Q06100; -.
DR VEuPathDB; FungiDB:CC1G_05003; -.
DR VEuPathDB; FungiDB:CC2G_013119; -.
DR OMA; VRVWINI; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030395; F:lactose binding; IDA:UniProtKB.
DR GO; GO:0030584; P:sporocarp development; NAS:UniProtKB.
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 Cell wall; Direct protein sequencing; Extracellular matrix; Fruiting body;
KW Lectin; Membrane; Secreted.
FT CHAIN 1..150
FT /note="Galectin-1"
FT /id="PRO_0000076967"
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"
FT CONFLICT 4
FT /note="H -> R (in Ref. 1 and 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 150 AA; 16408 MW; 9DAF46E0AC860AF0 CRC64;
MLYHLFVNNQ IKLQDDFKAE AVATIRSSVF NSKGGTTVFN FLSAGENILL HISIRPGENA
IVFNSRTKGG AWGPEERVPY AGKFKGPNPS ITVLDHGDRF QILFDNATAI YYTKRIKENA
AAIAYSAENS LFSSPVTVDI HGLLPPLPPA
