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Protein

Galectin-1

Gene

Lgals1

Organism
Rattus norvegicus (Rat)
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. 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 similarity

Sites

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

GO - Molecular functioni

  • glycoprotein binding Source: RGD
  • lactose binding Source: RGD
  • laminin binding Source: RGD
  • poly(A) RNA binding Source: Ensembl
  • protein homodimerization activity Source: RGD
  • signal transducer activity Source: Ensembl

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cellular response to glucose stimulus Source: RGD
  • cellular response to organic cyclic compound Source: RGD
  • multicellular organismal response to stress Source: RGD
  • myoblast differentiation Source: Ensembl
  • negative regulation of cell-substrate adhesion Source: RGD
  • negative regulation of neuron projection development Source: RGD
  • plasma cell differentiation Source: Ensembl
  • positive regulation of erythrocyte aggregation Source: RGD
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of viral entry into host cell Source: Ensembl
  • response to axon injury Source: RGD
  • response to drug Source: RGD
  • T cell costimulation Source: Ensembl
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
RL 14.5
S-Lac lectin 1
Gene namesi
Name:Lgals1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi69355. Lgals1.

Subcellular locationi

GO - Cellular componenti

  • cell surface Source: RGD
  • cytoplasm Source: RGD
  • extracellular exosome Source: Ensembl
  • extracellular space Source: Ensembl
  • nucleus Source: RGD
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 135134Galectin-1PRO_0000076920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei19 – 191N6-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

PaxDbiP11762.
PRIDEiP11762.

PTM databases

iPTMnetiP11762.

Expressioni

Gene expression databases

GenevisibleiP11762. RN.

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

GO - Molecular functioni

  • glycoprotein binding Source: RGD
  • laminin binding Source: RGD
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

BioGridi248567. 1 interaction.
DIPiDIP-37188N.
IntActiP11762. 1 interaction.
STRINGi10116.ENSRNOP00000013538.

Structurei

Secondary structure

1
135
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 74Combined sources
Beta strandi17 – 248Combined sources
Beta strandi30 – 389Combined sources
Beta strandi41 – 5212Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi73 – 753Combined sources
Beta strandi84 – 929Combined sources
Beta strandi94 – 1007Combined 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
3M2MX-ray2.95A/B/C/D/E/F/G/H2-135[»]
4GA9X-ray1.88A/B2-135[»]
4NO4X-ray1.40A/B/C/D/E/F2-135[»]
ProteinModelPortaliP11762.
SMRiP11762. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11762.

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.
InParanoidiP11762.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
PhylomeDBiP11762.

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.

P11762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACGLVASNL NLKPGECLKV RGELAPDAKS FVLNLGKDSN NLCLHFNPRF
60 70 80 90 100
NAHGDANTIV CNSKDDGTWG TEQRETAFPF QPGSITEVCI TFDQADLTIK
110 120 130
LPDGHEFKFP NRLNMEAINY MAADGDFKIK CVAFE
Length:135
Mass (Da):14,857
Last modified:January 23, 2007 - v2
Checksum:iA2C2DFB464FE81CF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19036 mRNA. Translation: AAA40822.1.
BC058476 mRNA. Translation: AAH58476.1.
PIRiA28703. LNRTGB.
RefSeqiNP_063969.1. NM_019904.1.
UniGeneiRn.57.

Genome annotation databases

EnsembliENSRNOT00000013538; ENSRNOP00000013538; ENSRNOG00000009884.
GeneIDi56646.
KEGGirno:56646.
UCSCiRGD:69355. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M19036 mRNA. Translation: AAA40822.1.
BC058476 mRNA. Translation: AAH58476.1.
PIRiA28703. LNRTGB.
RefSeqiNP_063969.1. NM_019904.1.
UniGeneiRn.57.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3M2MX-ray2.95A/B/C/D/E/F/G/H2-135[»]
4GA9X-ray1.88A/B2-135[»]
4NO4X-ray1.40A/B/C/D/E/F2-135[»]
ProteinModelPortaliP11762.
SMRiP11762. Positions 2-135.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248567. 1 interaction.
DIPiDIP-37188N.
IntActiP11762. 1 interaction.
STRINGi10116.ENSRNOP00000013538.

PTM databases

iPTMnetiP11762.

Proteomic databases

PaxDbiP11762.
PRIDEiP11762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000013538; ENSRNOP00000013538; ENSRNOG00000009884.
GeneIDi56646.
KEGGirno:56646.
UCSCiRGD:69355. rat.

Organism-specific databases

CTDi3956.
RGDi69355. Lgals1.

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00440000034263.
HOGENOMiHOG000059539.
HOVERGENiHBG006255.
InParanoidiP11762.
KOiK06830.
OMAiCNSKEDG.
OrthoDBiEOG7NKKN0.
PhylomeDBiP11762.

Miscellaneous databases

EvolutionaryTraceiP11762.
PROiP11762.

Gene expression databases

GenevisibleiP11762. RN.

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. "Sequence of a full-length cDNA for rat lung beta-galactoside-binding protein: primary and secondary structure of the lectin."
    Clerch L.B., Whitney P., Hass M., Brew K., Miller T., Werner R., Massaro D.
    Biochemistry 27:692-699(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Selective expression of an endogenous lactose-binding lectin gene in subsets of central and peripheral neurons."
    Hynes M.A., Gitt M., Barondes S.H., Jessell T.M., Buck L.B.
    J. Neurosci. 10:1004-1013(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Pituitary.
  4. Lubec G., Afjehi-Sadat L.
    Submitted (NOV-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 38-49, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Spinal cord.

Entry informationi

Entry nameiLEG1_RAT
AccessioniPrimary (citable) accession number: P11762
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 128 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.