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Protein

Galectin-1

Gene

LGALS1

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei53 – 531Beta-galactosideBy similarity
Binding sitei62 – 621Beta-galactosideBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

Lectin

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-1
Short name:
Gal-1
Alternative name(s):
14 kDa lectin
Beta-galactoside-binding lectin L-14-I
Galaptin
Lactose-binding lectin 1
Lectin galactoside-binding soluble 1
S-Lac lectin 1
Gene namesi
Name:LGALS1
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi69 – 691W → F: Reduced carbohydrate binding. 1 Publication
Mutagenesisi69 – 691W → L: No carbohydrate binding. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Galectin-1PRO_0000076915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei29 – 291N6-acetyllysineBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei108 – 1081N6-acetyllysine; alternateBy similarity
Modified residuei108 – 1081N6-succinyllysine; alternateBy similarity
Modified residuei128 – 1281N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP11116.
PeptideAtlasiP11116.
PRIDEiP11116.

Interactioni

Subunit structurei

Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4, CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-N-acetyllactosamine). Interacts with SUSD2.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020080.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Beta strandi17 – 248Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi73 – 753Combined sources
Beta strandi85 – 928Combined sources
Beta strandi94 – 1007Combined sources
Helixi102 – 1043Combined sources
Beta strandi106 – 1105Combined sources
Beta strandi120 – 13516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SLAX-ray2.45A/B2-135[»]
1SLBX-ray2.30A/B/C/D2-135[»]
1SLCX-ray2.15A/B/C/D2-135[»]
1SLTX-ray1.90A/B2-135[»]
ProteinModelPortaliP11116.
SMRiP11116. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11116.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 135132GalectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 495Beta-galactoside bindingBy similarity
Regioni69 – 724Beta-galactoside bindingBy similarity

Sequence similaritiesi

Contains 1 galectin domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOGENOMiHOG000059539.
HOVERGENiHBG006255.
InParanoidiP11116.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
TreeFamiTF315551.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11116-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACGLVASNL NLKPGECLRV RGEVAADAKS FLLNLGKDDN NLCLHFNPRF
60 70 80 90 100
NAHGDVNTIV CNSKDAGAWG AEQRESAFPF QPGSVVEVCI SFNQTDLTIK
110 120 130
LPDGYEFKFP NRLNLEAINY LSAGGDFKIK CVAFE
Length:135
Mass (Da):14,744
Last modified:January 23, 2007 - v2
Checksum:i77FE0F95C67317BC
GO

Mass spectrometryi

Molecular mass is 14654.6±0.9 Da from positions 2 - 135. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14330 mRNA. Translation: CAA32508.1.
AB099039 mRNA. Translation: BAC56529.1.
BC103156 mRNA. Translation: AAI03157.1.
PIRiS03865. LNBOGB.
RefSeqiNP_786976.1. NM_175782.1.
UniGeneiBt.5472.

Genome annotation databases

EnsembliENSBTAT00000020080; ENSBTAP00000020080; ENSBTAG00000015089.
GeneIDi326598.
KEGGibta:326598.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X14330 mRNA. Translation: CAA32508.1.
AB099039 mRNA. Translation: BAC56529.1.
BC103156 mRNA. Translation: AAI03157.1.
PIRiS03865. LNBOGB.
RefSeqiNP_786976.1. NM_175782.1.
UniGeneiBt.5472.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SLAX-ray2.45A/B2-135[»]
1SLBX-ray2.30A/B/C/D2-135[»]
1SLCX-ray2.15A/B/C/D2-135[»]
1SLTX-ray1.90A/B2-135[»]
ProteinModelPortaliP11116.
SMRiP11116. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000020080.

Proteomic databases

PaxDbiP11116.
PeptideAtlasiP11116.
PRIDEiP11116.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000020080; ENSBTAP00000020080; ENSBTAG00000015089.
GeneIDi326598.
KEGGibta:326598.

Organism-specific databases

CTDi3956.

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOGENOMiHOG000059539.
HOVERGENiHBG006255.
InParanoidiP11116.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
TreeFamiTF315551.

Miscellaneous databases

EvolutionaryTraceiP11116.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 1 hit.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS51304. GALECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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."
    Abbott W.M., Mellor A., Edwards Y., Feizi T.
    Biochem. J. 259:283-290(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Trachea.
  2. "Characterization of gene expression profiles in early bovine pregnancy using a custom cDNA microarray."
    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.
    Mol. Reprod. Dev. 65:9-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Heart ventricle.
  4. "Amino acid sequence of beta-galactoside-binding bovine heart lectin. Member of a novel class of vertebrate proteins."
    Southan C., Aitken A., Childs R.A., Abbott W.M., Feizi T.
    FEBS Lett. 214:301-304(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PRELIMINARY PROTEIN SEQUENCE OF 11-134.
    Tissue: Heart.
  5. "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."
    Abbott W.M., Feizi T.
    J. Biol. Chem. 266:5552-5557(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, FUNCTION.
    Tissue: Heart.
  6. "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."
    Tracey B.M., Feizi T., Abbott W.M., Carruthers R.A., Green B.N., Lawson A.M.
    J. Biol. Chem. 267:10342-10347(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MASS SPECTROMETRY.
    Tissue: Heart.
  7. "Structure of S-lectin, a developmentally regulated vertebrate beta-galactoside-binding protein."
    Liao D.-I., Kapadia G., Ahmed H., Vasta G.R., Herzberg O.
    Proc. Natl. Acad. Sci. U.S.A. 91:1428-1432(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, FUNCTION.
    Tissue: Spleen.
  8. "Crosslinking of mammalian lectin (galectin-1) by complex biantennary saccharides."
    Bourne Y., Bolgiano B., Liao D.-I., Strecker G., Cantau P., Herzberg O., Feizi T., Cambillau C.
    Nat. Struct. Biol. 1:863-870(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE, FUNCTION.

Entry informationi

Entry nameiLEG1_BOVIN
AccessioniPrimary (citable) accession number: P11116
Secondary accession number(s): P11945, Q54A27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.