LEG1_BOVIN
ID LEG1_BOVIN Reviewed; 135 AA.
AC P11116; P11945; Q54A27;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 169.
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=S-Lac lectin 1;
GN Name=LGALS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trachea;
RX PubMed=2470348; DOI=10.1042/bj2590283;
RA Abbott W.M., Mellor A., Edwards Y., Feizi T.;
RT "Soluble bovine galactose-binding lectin. cDNA cloning reveals the complete
RT amino acid sequence and an antigenic relationship with the major
RT encephalitogenic domain of myelin basic protein.";
RL Biochem. J. 259:283-290(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Heart ventricle;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PRELIMINARY PROTEIN SEQUENCE OF 11-134.
RC TISSUE=Heart;
RX PubMed=3569527; DOI=10.1016/0014-5793(87)80074-1;
RA Southan C., Aitken A., Childs R.A., Abbott W.M., Feizi T.;
RT "Amino acid sequence of beta-galactoside-binding bovine heart lectin.
RT Member of a novel class of vertebrate proteins.";
RL FEBS Lett. 214:301-304(1987).
RN [5]
RP MUTAGENESIS, AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=1900835; DOI=10.1016/s0021-9258(19)67630-1;
RA Abbott W.M., Feizi T.;
RT "Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from
RT mutagenesis and proteolysis that almost the complete polypeptide chain is
RT necessary for integrity of the carbohydrate recognition domain.";
RL J. Biol. Chem. 266:5552-5557(1991).
RN [6]
RP CHARACTERIZATION, AND MASS SPECTROMETRY.
RC TISSUE=Heart;
RX PubMed=1587821; DOI=10.1016/s0021-9258(19)50024-2;
RA Tracey B.M., Feizi T., Abbott W.M., Carruthers R.A., Green B.N.,
RA Lawson A.M.;
RT "Subunit molecular mass assignment of 14,654 Da to the soluble beta-
RT galactoside-binding lectin from bovine heart muscle and demonstration of
RT intramolecular disulfide bonding associated with oxidative inactivation.";
RL J. Biol. Chem. 267:10342-10347(1992).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, AND
RP FUNCTION.
RC TISSUE=Spleen;
RX PubMed=8108426; DOI=10.1073/pnas.91.4.1428;
RA Liao D.-I., Kapadia G., Ahmed H., Vasta G.R., Herzberg O.;
RT "Structure of S-lectin, a developmentally regulated vertebrate beta-
RT galactoside-binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1428-1432(1994).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, AND
RP FUNCTION.
RX PubMed=7773775; DOI=10.1038/nsb1294-863;
RA Bourne Y., Bolgiano B., Liao D.-I., Strecker G., Cantau P., Herzberg O.,
RA Feizi T., Cambillau C.;
RT "Crosslinking of mammalian lectin (galectin-1) by complex biantennary
RT saccharides.";
RL Nat. Struct. Biol. 1:863-870(1994).
CC -!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
CC complex carbohydrates (PubMed:1900835, PubMed:8108426, PubMed:7773775).
CC Plays a role in regulating apoptosis, cell proliferation and cell
CC differentiation. Inhibits CD45 protein phosphatase activity and
CC therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell
CC apoptosis. {ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:1900835,
CC ECO:0000269|PubMed:7773775, ECO:0000269|PubMed:8108426}.
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}.
CC -!- MASS SPECTROMETRY: Mass=14654.6; Mass_error=0.9; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:1587821};
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DR EMBL; X14330; CAA32508.1; -; mRNA.
DR EMBL; AB099039; BAC56529.1; -; mRNA.
DR EMBL; BC103156; AAI03157.1; -; mRNA.
DR PIR; S03865; LNBOGB.
DR RefSeq; NP_786976.1; NM_175782.1.
DR PDB; 1SLA; X-ray; 2.45 A; A/B=2-135.
DR PDB; 1SLB; X-ray; 2.30 A; A/B/C/D=2-135.
DR PDB; 1SLC; X-ray; 2.15 A; A/B/C/D=2-135.
DR PDB; 1SLT; X-ray; 1.90 A; A/B=2-135.
DR PDBsum; 1SLA; -.
DR PDBsum; 1SLB; -.
DR PDBsum; 1SLC; -.
DR PDBsum; 1SLT; -.
DR AlphaFoldDB; P11116; -.
DR SMR; P11116; -.
DR STRING; 9913.ENSBTAP00000020080; -.
DR UniLectin; P11116; -.
DR PaxDb; P11116; -.
DR PeptideAtlas; P11116; -.
DR PRIDE; P11116; -.
DR Ensembl; ENSBTAT00000020080; ENSBTAP00000020080; ENSBTAG00000015089.
DR GeneID; 326598; -.
DR KEGG; bta:326598; -.
DR CTD; 3956; -.
DR VEuPathDB; HostDB:ENSBTAG00000015089; -.
DR VGNC; VGNC:30850; LGALS1.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155534; -.
DR HOGENOM; CLU_037794_5_0_1; -.
DR InParanoid; P11116; -.
DR OMA; KIKCMAF; -.
DR OrthoDB; 1429018at2759; -.
DR TreeFam; TF315551; -.
DR Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
DR EvolutionaryTrace; P11116; -.
DR Proteomes; UP000009136; Chromosome 5.
DR Bgee; ENSBTAG00000015089; Expressed in pons and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:1990724; C:galectin complex; IEA:Ensembl.
DR GO; GO:0030246; F:carbohydrate binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
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 3D-structure; 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 CHAIN 2..135
FT /note="Galectin-1"
FT /id="PRO_0000076915"
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"
FT MUTAGEN 69
FT /note="W->F: Reduced carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:1900835"
FT MUTAGEN 69
FT /note="W->L: No carbohydrate binding."
FT /evidence="ECO:0000269|PubMed:1900835"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 17..24
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 41..52
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 55..65
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1SLT"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1SLC"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:1SLT"
FT STRAND 120..135
FT /evidence="ECO:0007829|PDB:1SLT"
SQ SEQUENCE 135 AA; 14744 MW; 77FE0F95C67317BC CRC64;
MACGLVASNL NLKPGECLRV RGEVAADAKS FLLNLGKDDN NLCLHFNPRF NAHGDVNTIV
CNSKDAGAWG AEQRESAFPF QPGSVVEVCI SFNQTDLTIK LPDGYEFKFP NRLNLEAINY
LSAGGDFKIK CVAFE
