LEG1_SHEEP
ID LEG1_SHEEP Reviewed; 135 AA.
AC P81184;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Galectin-1;
DE Short=Gal-1;
DE AltName: Full=14 kDa lectin;
DE AltName: Full=Beta-galactoside-binding lectin L-14-I;
DE AltName: Full=Galaptin;
DE AltName: Full=Lactose-binding lectin 1;
DE AltName: Full=Lectin galactoside-binding soluble 1;
DE AltName: Full=OPG-1;
DE AltName: Full=S-Lac lectin 1;
GN Name=LGALS1;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP PROTEIN SEQUENCE OF 2-135, AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=9546655; DOI=10.1046/j.1432-1327.1998.2520400.x;
RA Iglesias M.M., Rabinovich G.A., Ivanovic V., Sotomayor C.,
RA Wolfenstein-Todel C.;
RT "Galectin-1 from ovine placenta -- amino-acid sequence, physicochemical
RT properties and implications in T-cell death.";
RL Eur. J. Biochem. 252:400-407(1998).
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 (PubMed:9546655). Inhibits CD45
CC protein phosphatase activity and therefore the dephosphorylation of Lyn
CC kinase (By similarity). Strong inducer of T-cell apoptosis
CC (PubMed:9546655). {ECO:0000250|UniProtKB:P09382,
CC ECO:0000269|PubMed:9546655}.
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; P81184; -.
DR SMR; P81184; -.
DR STRING; 9940.ENSOARP00000014976; -.
DR eggNOG; KOG3587; Eukaryota.
DR Proteomes; UP000002356; Unplaced.
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; Reference proteome; Secreted.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P09382,
FT ECO:0000269|PubMed:9546655"
FT CHAIN 2..135
FT /note="Galectin-1"
FT /id="PRO_0000076921"
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"
FT BINDING 53
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT BINDING 69..72
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
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; 14704 MW; 6B4842FC35C72610 CRC64;
MACGLVASNL NLKPGECLRV RGEVAADAKS FSLNLGKDDN NLCLHFNPRF NAHGDINTIV
CNSKDGGAWG AEQRETAFPF QPGSVAEVCI SFNQTDLTIK LPDGYEFKFP NRLNLEAINY
LSAGGDFKIK CVAFE
