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Galectin-1 (Gal-1) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (S-Lac lectin 1)

 LEG1_BOVIN              Reviewed;         135 AA.
P11116; P11945; Q54A27;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
28-MAR-2018, entry version 148.
RecName: Full=Galectin-1;
Short=Gal-1;
AltName: Full=14 kDa lectin;
AltName: Full=Beta-galactoside-binding lectin L-14-I;
AltName: Full=Galaptin;
AltName: Full=Lactose-binding lectin 1;
AltName: Full=Lectin galactoside-binding soluble 1;
AltName: Full=S-Lac lectin 1;
Name=LGALS1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Trachea;
PubMed=2470348; DOI=10.1042/bj2590283;
Abbott W.M., Mellor A., Edwards Y., Feizi T.;
"Soluble bovine galactose-binding lectin. cDNA cloning reveals the
complete amino acid sequence and an antigenic relationship with the
major encephalitogenic domain of myelin basic protein.";
Biochem. J. 259:283-290(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12658628; DOI=10.1002/mrd.10292;
Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H.,
Takahashi T., Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y.,
Tsujimoto G., Izaike Y., Todoroki J., Hashizume K.;
"Characterization of gene expression profiles in early bovine
pregnancy using a custom cDNA microarray.";
Mol. Reprod. Dev. 65:9-18(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Heart ventricle;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PRELIMINARY PROTEIN SEQUENCE OF 11-134.
TISSUE=Heart;
PubMed=3569527; DOI=10.1016/0014-5793(87)80074-1;
Southan C., Aitken A., Childs R.A., Abbott W.M., Feizi T.;
"Amino acid sequence of beta-galactoside-binding bovine heart lectin.
Member of a novel class of vertebrate proteins.";
FEBS Lett. 214:301-304(1987).
[5]
MUTAGENESIS, AND FUNCTION.
TISSUE=Heart;
PubMed=1900835;
Abbott W.M., Feizi T.;
"Soluble 14-kDa beta-galactoside-specific bovine lectin. Evidence from
mutagenesis and proteolysis that almost the complete polypeptide chain
is necessary for integrity of the carbohydrate recognition domain.";
J. Biol. Chem. 266:5552-5557(1991).
[6]
CHARACTERIZATION, AND MASS SPECTROMETRY.
TISSUE=Heart;
PubMed=1587821;
Tracey B.M., Feizi T., Abbott W.M., Carruthers R.A., Green B.N.,
Lawson A.M.;
"Subunit molecular mass assignment of 14,654 Da to the soluble beta-
galactoside-binding lectin from bovine heart muscle and demonstration
of intramolecular disulfide bonding associated with oxidative
inactivation.";
J. Biol. Chem. 267:10342-10347(1992).
[7]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE,
AND FUNCTION.
TISSUE=Spleen;
PubMed=8108426; DOI=10.1073/pnas.91.4.1428;
Liao D.-I., Kapadia G., Ahmed H., Vasta G.R., Herzberg O.;
"Structure of S-lectin, a developmentally regulated vertebrate beta-
galactoside-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 91:1428-1432(1994).
[8]
X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE,
AND FUNCTION.
PubMed=7773775; DOI=10.1038/nsb1294-863;
Bourne Y., Bolgiano B., Liao D.-I., Strecker G., Cantau P.,
Herzberg O., Feizi T., Cambillau C.;
"Crosslinking of mammalian lectin (galectin-1) by complex biantennary
saccharides.";
Nat. Struct. Biol. 1:863-870(1994).
-!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
complex carbohydrates (PubMed:1900835, PubMed:8108426,
PubMed:7773775). Plays a role in regulating apoptosis, cell
proliferation and cell differentiation. Inhibits CD45 protein
phosphatase activity and therefore the dephosphorylation of Lyn
kinase. Strong inducer of T-cell apoptosis.
{ECO:0000250|UniProtKB:P09382, ECO:0000269|PubMed:1900835,
ECO:0000269|PubMed:7773775, ECO:0000269|PubMed:8108426}.
-!- SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4,
CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-
N-acetyllactosamine). Interacts with SUSD2.
{ECO:0000250|UniProtKB:P09382}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250|UniProtKB:P09382}.
-!- MASS SPECTROMETRY: Mass=14654.6; Mass_error=0.9;
Method=Electrospray; Range=2-135;
Evidence={ECO:0000269|PubMed:1587821};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14330; CAA32508.1; -; mRNA.
EMBL; AB099039; BAC56529.1; -; mRNA.
EMBL; BC103156; AAI03157.1; -; mRNA.
PIR; S03865; LNBOGB.
RefSeq; NP_786976.1; NM_175782.1.
UniGene; Bt.5472; -.
PDB; 1SLA; X-ray; 2.45 A; A/B=2-135.
PDB; 1SLB; X-ray; 2.30 A; A/B/C/D=2-135.
PDB; 1SLC; X-ray; 2.15 A; A/B/C/D=2-135.
PDB; 1SLT; X-ray; 1.90 A; A/B=2-135.
PDBsum; 1SLA; -.
PDBsum; 1SLB; -.
PDBsum; 1SLC; -.
PDBsum; 1SLT; -.
ProteinModelPortal; P11116; -.
SMR; P11116; -.
STRING; 9913.ENSBTAP00000020080; -.
PaxDb; P11116; -.
PeptideAtlas; P11116; -.
PRIDE; P11116; -.
Ensembl; ENSBTAT00000020080; ENSBTAP00000020080; ENSBTAG00000015089.
GeneID; 326598; -.
KEGG; bta:326598; -.
CTD; 3956; -.
VGNC; VGNC:30850; LGALS1.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00440000034263; -.
HOGENOM; HOG000059539; -.
HOVERGEN; HBG006255; -.
InParanoid; P11116; -.
KO; K06830; -.
OMA; CNSKEDG; -.
OrthoDB; EOG091G0S7H; -.
TreeFam; TF315551; -.
Reactome; R-BTA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-BTA-8957275; Post-translational protein phosphorylation.
EvolutionaryTrace; P11116; -.
Proteomes; UP000009136; Chromosome 5.
Bgee; ENSBTAG00000015089; -.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005622; C:intracellular; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
CDD; cd00070; GLECT; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001079; Galectin_CRD.
Pfam; PF00337; Gal-bind_lectin; 1.
SMART; SM00908; Gal-bind_lectin; 1.
SMART; SM00276; GLECT; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51304; GALECTIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome;
Direct protein sequencing; Extracellular matrix; Lectin;
Phosphoprotein; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P09382}.
CHAIN 2 135 Galectin-1.
/FTId=PRO_0000076915.
DOMAIN 4 135 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 45 49 Beta-galactoside binding. {ECO:0000250}.
REGION 69 72 Beta-galactoside binding. {ECO:0000250}.
BINDING 53 53 Beta-galactoside. {ECO:0000250}.
BINDING 62 62 Beta-galactoside. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P09382}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09382}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:P09382}.
MOD_RES 108 108 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 108 108 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P16045}.
MUTAGEN 69 69 W->F: Reduced carbohydrate binding.
{ECO:0000269|PubMed:1900835}.
MUTAGEN 69 69 W->L: No carbohydrate binding.
{ECO:0000269|PubMed:1900835}.
STRAND 6 9 {ECO:0000244|PDB:1SLT}.
STRAND 17 24 {ECO:0000244|PDB:1SLT}.
STRAND 30 38 {ECO:0000244|PDB:1SLT}.
STRAND 41 52 {ECO:0000244|PDB:1SLT}.
STRAND 55 65 {ECO:0000244|PDB:1SLT}.
STRAND 73 75 {ECO:0000244|PDB:1SLT}.
STRAND 85 92 {ECO:0000244|PDB:1SLT}.
STRAND 94 100 {ECO:0000244|PDB:1SLT}.
HELIX 102 104 {ECO:0000244|PDB:1SLC}.
STRAND 106 110 {ECO:0000244|PDB:1SLT}.
STRAND 120 135 {ECO:0000244|PDB:1SLT}.
SEQUENCE 135 AA; 14744 MW; 77FE0F95C67317BC CRC64;
MACGLVASNL NLKPGECLRV RGEVAADAKS FLLNLGKDDN NLCLHFNPRF NAHGDVNTIV
CNSKDAGAWG AEQRESAFPF QPGSVVEVCI SFNQTDLTIK LPDGYEFKFP NRLNLEAINY
LSAGGDFKIK CVAFE


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