LEG1_BUBBU
ID LEG1_BUBBU Reviewed; 135 AA.
AC C0HJQ1;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Galectin-1 {ECO:0000303|PubMed:20354738};
DE Short=Gal-1 {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=14 kDa lectin {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=Beta-galactoside-binding lectin L-14-I {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=Galaptin {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=Heart galectin-1 {ECO:0000303|PubMed:20354738};
DE Short=BfHG-1 {ECO:0000303|PubMed:20354738};
DE AltName: Full=Lactose-binding lectin 1 {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=Lectin galactoside-binding soluble 1 {ECO:0000250|UniProtKB:P11116};
DE AltName: Full=S-Lac lectin 1 {ECO:0000250|UniProtKB:P11116};
GN Name=LGALS1 {ECO:0000250|UniProtKB:P09382};
OS Bubalus bubalis (Domestic water buffalo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bubalus.
OX NCBI_TaxID=89462 {ECO:0000303|PubMed:20354738};
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-135, FUNCTION, SUBUNIT, AND BLOCKAGE OF N-TERMINUS.
RC TISSUE=Heart {ECO:0000303|PubMed:20354738};
RX PubMed=20354738; DOI=10.1007/s00726-010-0574-7;
RA Ashraf G.M., Rizvi S., Naqvi S., Suhail N., Bilal N., Hasan S., Tabish M.,
RA Banu N.;
RT "Purification, characterization, structural analysis and protein chemistry
RT of a buffalo heart galectin-1.";
RL Amino Acids 39:1321-1332(2010).
CC -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC complex carbohydrates. Plays a role in regulating apoptosis, cell
CC proliferation and cell differentiation. Inhibits CD45 protein
CC phosphatase activity and therefore the dephosphorylation of Lyn kinase.
CC Strong inducer of T-cell apoptosis. {ECO:0000250|UniProtKB:P09382,
CC ECO:0000269|PubMed:20354738}.
CC -!- SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6,
CC CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-
CC acetyllactosamine). Interacts with SUSD2. Interacts with cargo receptor
CC TMED10; the interaction mediates the translocation from the cytoplasm
CC into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment)
CC and thereby secretion (By similarity). {ECO:0000250|UniProtKB:P09382,
CC ECO:0000269|PubMed:20354738}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm
CC {ECO:0000250|UniProtKB:P09382}. Secreted
CC {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is
CC dependent on protein unfolding and facilitated by the cargo receptor
CC TMED10; it results in protein translocation from the cytoplasm into the
CC ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed
CC by vesicle entry and secretion. {ECO:0000250|UniProtKB:P09382}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:20354738}.
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DR AlphaFoldDB; C0HJQ1; -.
DR SMR; C0HJQ1; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00908; 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 Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing;
KW Extracellular matrix; Lectin; Phosphoprotein; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT CHAIN 2..135
FT /note="Galectin-1"
FT /evidence="ECO:0000269|PubMed:20354738"
FT /id="PRO_0000431835"
FT DOMAIN 4..135
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 45..49
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT BINDING 53
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT BINDING 62
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT BINDING 69..72
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT MOD_RES 30
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09382"
FT MOD_RES 108
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 108
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P16045"
FT MOD_RES 128
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P16045"
SQ SEQUENCE 135 AA; 14716 MW; F0B6E13DB77ACC94 CRC64;
MACGLVASNL NLKPGECLRV RGEVAPDAKS FLLNLGKDDN NLCLHFNPRF NAHGDINTIV
CNSKDGGAWG AEQREVAFPF QPGSVVEVCI SFNQADLTVK LPDGHEFKFP NRLNLEAINY
MSAGGDFKIK CVAFD
