LEG1_CAPHI
ID LEG1_CAPHI Reviewed; 135 AA.
AC C0HJR3;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Galectin-1 {ECO:0000303|PubMed:21210196};
DE Short=Gal-1 {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=14 kDa lectin {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=Beta-galactoside-binding lectin L-14-I {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=Galaptin {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=Lactose-binding lectin 1 {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=Lectin galactoside-binding soluble 1 {ECO:0000250|UniProtKB:P09382};
DE AltName: Full=S-Lac lectin 1 {ECO:0000250|UniProtKB:P09382};
GN Name=LGALS1 {ECO:0000250|UniProtKB:P09382};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1] {ECO:0000305}
RP PROTEIN SEQUENCE OF 2-135, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RC TISSUE=Heart {ECO:0000303|PubMed:21210196};
RX PubMed=21210196; DOI=10.1007/s10930-010-9300-2;
RA Ashraf G.M., Banu N., Ahmad A., Singh L.P., Kumar R.;
RT "Purification, characterization, sequencing and biological chemistry of
RT galectin-1 purified from Capra hircus (goat) heart.";
RL Protein J. 30:39-51(2011).
CC -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC complex carbohydrates (PubMed:21210196). Plays a role in regulating
CC apoptosis, cell proliferation and cell differentiation. Inhibits CD45
CC protein phosphatase activity and therefore the dephosphorylation of Lyn
CC kinase. Strong inducer of T-cell apoptosis. Has hemaglutinating
CC activity towards human erythrocytes (PubMed:21210196).
CC {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:21210196}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH for hemagglutinating activity is 7.4.
CC {ECO:0000269|PubMed:21210196};
CC Temperature dependence:
CC Retains hemagglutinating activity up to 42 degrees Celsius. The
CC activity then drops and is completely lost at 65 degrees Celsius.
CC {ECO:0000269|PubMed:21210196};
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. {ECO:0000250|UniProtKB:P09382}.
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}.
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DR AlphaFoldDB; C0HJR3; -.
DR SMR; C0HJR3; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
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; Hemagglutinin; Lectin; Phosphoprotein;
KW Reference proteome; 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:21210196"
FT /id="PRO_0000432997"
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; 14798 MW; 25C092F9D9BF130A CRC64;
MACGLVASNL NLKPGECLRV RGELAADAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNSKDDGTWG AEQREVAFPF QPGSVVEVCI SFNQADLTVK LPDGHEFKFP NRLNMEAINY
MSADGDFKIK CVAFE
