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Protein

Galectin-9

Gene

Lgals9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds galactosides (By similarity). Has high affinity for the Forssman pentasaccharide (By similarity). Ligand for HAVCR2/TIM3 (By similarity). Binding to HAVCR2 induces T-helper type 1 lymphocyte (Th1) death (By similarity). Also stimulates bactericidal activity in infected macrophages by causing macrophage activation and IL1B secretion which restricts intracellular bacterial growth (PubMed:20937702). Ligand for P4HB; the interaction retains P4HB at the cell surface of Th2 T-helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration (PubMed:21670307). Ligand for CD44; the interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and increased induced regulatory T (iTreg) cell stability and suppressive function (PubMed:25065622). Promotes ability of mesenchymal stromal cells to suppress T-cell proliferation (By similarity). Expands regulatory T-cells and induces cytotoxic T-cell apoptosis following virus infection (By similarity). Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in mast and dendritic cells (By similarity). Inhibits degranulation and induces apoptosis of mast cells (By similarity). Induces maturation and migration of dendritic cells (By similarity). Inhibits natural killer (NK) cell function (PubMed:23408620). Can transform NK cell phenotype from peripheral to decidual during pregnancy (By similarity). Astrocyte derived galectin-9 enhances microglial TNF production (PubMed:25158758). May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. May provide the molecular basis for urate flux across cell membranes, allowing urate that is formed during purine metabolism to efflux from cells and serving as an electrogenic transporter that plays an important role in renal and gastrointestinal urate excretion (By similarity). Highly selective to the anion urate (By similarity).By similarity5 Publications
Isoform 2: Acts as an eosinophil chemoattractant (By similarity). It also inhibits angiogenesis (By similarity). Suppresses IFNG production by natural killer cells.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei47 – 471Beta-galactoside 1
Binding sitei60 – 601Beta-galactoside 1
Binding sitei64 – 641Beta-galactoside 1
Binding sitei74 – 741Beta-galactoside 1
Binding sitei265 – 2651Beta-galactoside 2By similarity
Binding sitei269 – 2691Beta-galactoside 2By similarity
Binding sitei279 – 2791Beta-galactoside 2By similarity

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • galactoside binding Source: UniProtKB
  • protein serine/threonine kinase activator activity Source: UniProtKB
  • receptor binding Source: UniProtKB

GO - Biological processi

  • cellular response to virus Source: UniProtKB
  • chemotaxis Source: UniProtKB-KW
  • female pregnancy Source: UniProtKB
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: MGI
  • immune system process Source: UniProtKB-KW
  • maintenance of protein location Source: UniProtKB
  • negative regulation of CD4-positive, alpha-beta T cell proliferation Source: UniProtKB
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of inflammatory response Source: UniProtKB
  • negative regulation of interferon-gamma production Source: UniProtKB
  • negative regulation of interferon-gamma secretion Source: UniProtKB
  • negative regulation of natural killer cell activation Source: UniProtKB
  • negative regulation of natural killer cell degranulation Source: UniProtKB
  • positive regulation of chemokine production Source: UniProtKB
  • positive regulation of cytokine production Source: UniProtKB
  • positive regulation of defense response to bacterium Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of innate immune response Source: UniProtKB
  • positive regulation of interleukin-10 secretion Source: UniProtKB
  • positive regulation of interleukin-1 production Source: UniProtKB
  • positive regulation of interleukin-6 secretion Source: UniProtKB
  • positive regulation of macrophage activation Source: UniProtKB
  • positive regulation of oxidoreductase activity Source: UniProtKB
  • positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
  • positive regulation of protein serine/threonine kinase activity Source: GOC
  • positive regulation of regulatory T cell differentiation Source: UniProtKB
  • positive regulation of T cell migration Source: UniProtKB
  • positive regulation of transcription regulatory region DNA binding Source: UniProtKB
  • positive regulation of tumor necrosis factor production Source: UniProtKB
  • regulation of natural killer cell differentiation Source: UniProtKB
  • response to lipopolysaccharide Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Chemotaxis, Immunity

Keywords - Ligandi

Lectin

Enzyme and pathway databases

ReactomeiR-MMU-451927. Interleukin-2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Galectin-9
Short name:
Gal-9
Gene namesi
Name:Lgals9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:109496. Lgals9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular region Source: Reactome
  • intracellular Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Secreted

Pathology & Biotechi

Disruption phenotypei

Increased natural killer (NK) cell activity with enhanced degranulation, higher expression of NK cell activating receptors, increased frequency of intermediate and mature NK cells, and greater production of interferon-gamma following murine cytomegalovirus infection (PubMed:23408620). Defective iTreg cell differentiation with impaired Foxp3 expression, reduced stability and suppressor function of iTreg cells and reduced frequency of iTreg cells but not natural regulatory T (nTreg) cells in lamina propria (PubMed:25065622).2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Galectin-9PRO_0000076947Add
BLAST

Proteomic databases

EPDiO08573.
MaxQBiO08573.
PaxDbiO08573.
PRIDEiO08573.

PTM databases

iPTMnetiO08573.
PhosphoSiteiO08573.
SwissPalmiO08573.

Expressioni

Tissue specificityi

Accentuated expression in liver and thymus of embryo, detected in embryonic heart, brain, lung, liver, and kidney. Highly expressed in adult thymus, small intestine, and liver, and to a lesser extent in lung, kidney, spleen, cardiac, and skeletal muscle. Barely detectable in brain and reticulocyte. Expressed in placenta, uterus and decidua during pregnancy (PubMed:23242525). Expressed in CD4+ T-cells with higher levels in iTreg cells than other T-cell types and sustained high levels throughout iTreg cell differentiation (at protein level) (PubMed:25065622). Expressed in myeloid cells in lung (PubMed:20937702). Constitutively expressed in microglia (PubMed:25158758). Isoform 1 is expressed exclusively in the small intestine. Isoform 2 expression in decidua increases in pathological pregnancy from gestation day 7.5 to 13.5 and it is higher than in normal pregnancy (PubMed:23242525). Isoform 3 expression in decidua is higher in normal pregnancy than in pathological pregnancy (PubMed:23242525).4 Publications

Developmental stagei

The expression increases with successive stages of embryonic development.

Inductioni

By viral mimic polyinosinic:polycytidylic acid (poly I:C) and lipopolysaccharides (LPS) in microglia (PubMed:25158758). Up-regulated in macrophages following infection with Mycobacterium tuberculosis (PubMed:20937702).2 Publications

Gene expression databases

BgeeiO08573.
CleanExiMM_LGALS9.
ExpressionAtlasiO08573. baseline and differential.
GenevisibleiO08573. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Cd44P153792EBI-8377586,EBI-7565891
Havcr2Q8VIM04EBI-11316797,EBI-6665112

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

IntActiO08573. 5 interactions.
MINTiMINT-1864855.
STRINGi10090.ENSMUSP00000103904.

Structurei

Secondary structure

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Beta strandi15 – 206Combined sources
Beta strandi30 – 378Combined sources
Beta strandi43 – 519Combined sources
Beta strandi57 – 648Combined sources
Beta strandi70 – 778Combined sources
Beta strandi85 – 873Combined sources
Beta strandi97 – 1048Combined sources
Beta strandi106 – 1138Combined sources
Beta strandi116 – 1227Combined sources
Helixi127 – 1293Combined sources
Beta strandi132 – 14716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D6KX-ray2.50A/B1-188[»]
2D6LX-ray2.50X1-188[»]
2D6MX-ray1.60A/B1-188[»]
2D6NX-ray2.00A/B1-188[»]
2D6OX-ray1.78X1-188[»]
2D6PX-ray2.70A/B1-188[»]
ProteinModelPortaliO08573.
SMRiO08573. Positions 1-353.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08573.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini17 – 147131Galectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini225 – 353129Galectin 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 877Beta-galactoside binding 1
Regioni285 – 2917Beta-galactoside binding 2By similarity

Domaini

Contains two homologous but distinct carbohydrate-binding domains.

Sequence similaritiesi

Contains 2 galectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00760000119105.
HOGENOMiHOG000290194.
HOVERGENiHBG002412.
InParanoidiO08573.
KOiK10093.
OrthoDBiEOG73Z2TM.
PhylomeDBiO08573.
TreeFamiTF315551.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 2 hits.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS51304. GALECTIN. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O08573-1) [UniParc]FASTAAdd to basket

Also known as: Long, FL1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALFSAQSPY INPIIPFTGP IQGGLQEGLQ VTLQGTTKSF AQRFVVNFQN
60 70 80 90 100
SFNGNDIAFH FNPRFEEGGY VVCNTKQNGQ WGPEERKMQM PFQKGMPFEL
110 120 130 140 150
CFLVQRSEFK VMVNKKFFVQ YQHRVPYHLV DTIAVSGCLK LSFITFQNSA
160 170 180 190 200
APVQHVFSTL QFSQPVQFPR TPKGRKQKTQ NFRPAHQAPM AQTTIHMVHS
210 220 230 240 250
TPGQMFSTPG IPPVVYPTPA YTIPFYTPIP NGLYPSKSIM ISGNVLPDAT
260 270 280 290 300
RFHINLRCGG DIAFHLNPRF NENAVVRNTQ INNSWGQEER SLLGRMPFSR
310 320 330 340 350
GQSFSVWIIC EGHCFKVAVN GQHMCEYYHR LKNLQDINTL EVAGDIQLTH

VQT
Length:353
Mass (Da):40,036
Last modified:July 1, 1997 - v1
Checksum:iB54036F6E280C531
GO
Isoform 2 (identifier: O08573-2) [UniParc]FASTAAdd to basket

Also known as: Short, D51 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     148-178: Missing.

Show »
Length:322
Mass (Da):36,544
Checksum:iB4961AFB6F1FF13F
GO
Isoform 3 (identifier: O08573-3) [UniParc]FASTAAdd to basket

Also known as: D5/61 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     148-178: Missing.
     179-190: Missing.

Show »
Length:310
Mass (Da):35,164
Checksum:i0269E1592EB9B535
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti181 – 1811N → D in AAH03754 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei148 – 17831Missing in isoform 2 and isoform 3. 1 Publication1 PublicationVSP_003097Add
BLAST
Alternative sequencei179 – 19012Missing in isoform 3. 1 PublicationVSP_057844Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55061 mRNA. Translation: AAB51190.1.
U55060 mRNA. Translation: AAB51189.1.
AK146044 mRNA. Translation: BAE26856.1.
AL592551, AL592185 Genomic DNA. Translation: CAI24050.1.
AL592185, AL592551 Genomic DNA. Translation: CAI25276.1.
CH466556 Genomic DNA. Translation: EDL15600.1.
BC003754 mRNA. Translation: AAH03754.1.
CCDSiCCDS25116.1. [O08573-1]
CCDS48858.1. [O08573-2]
RefSeqiNP_001152773.1. NM_001159301.1. [O08573-2]
NP_034838.2. NM_010708.2.
UniGeneiMm.341434.

Genome annotation databases

EnsembliENSMUST00000108268; ENSMUSP00000103903; ENSMUSG00000001123. [O08573-2]
GeneIDi16859.
KEGGimmu:16859.
UCSCiuc007kke.2. mouse. [O08573-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55061 mRNA. Translation: AAB51190.1.
U55060 mRNA. Translation: AAB51189.1.
AK146044 mRNA. Translation: BAE26856.1.
AL592551, AL592185 Genomic DNA. Translation: CAI24050.1.
AL592185, AL592551 Genomic DNA. Translation: CAI25276.1.
CH466556 Genomic DNA. Translation: EDL15600.1.
BC003754 mRNA. Translation: AAH03754.1.
CCDSiCCDS25116.1. [O08573-1]
CCDS48858.1. [O08573-2]
RefSeqiNP_001152773.1. NM_001159301.1. [O08573-2]
NP_034838.2. NM_010708.2.
UniGeneiMm.341434.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D6KX-ray2.50A/B1-188[»]
2D6LX-ray2.50X1-188[»]
2D6MX-ray1.60A/B1-188[»]
2D6NX-ray2.00A/B1-188[»]
2D6OX-ray1.78X1-188[»]
2D6PX-ray2.70A/B1-188[»]
ProteinModelPortaliO08573.
SMRiO08573. Positions 1-353.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08573. 5 interactions.
MINTiMINT-1864855.
STRINGi10090.ENSMUSP00000103904.

PTM databases

iPTMnetiO08573.
PhosphoSiteiO08573.
SwissPalmiO08573.

Proteomic databases

EPDiO08573.
MaxQBiO08573.
PaxDbiO08573.
PRIDEiO08573.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108268; ENSMUSP00000103903; ENSMUSG00000001123. [O08573-2]
GeneIDi16859.
KEGGimmu:16859.
UCSCiuc007kke.2. mouse. [O08573-2]

Organism-specific databases

CTDi3965.
MGIiMGI:109496. Lgals9.

Phylogenomic databases

eggNOGiKOG3587. Eukaryota.
ENOG4111EA0. LUCA.
GeneTreeiENSGT00760000119105.
HOGENOMiHOG000290194.
HOVERGENiHBG002412.
InParanoidiO08573.
KOiK10093.
OrthoDBiEOG73Z2TM.
PhylomeDBiO08573.
TreeFamiTF315551.

Enzyme and pathway databases

ReactomeiR-MMU-451927. Interleukin-2 signaling.

Miscellaneous databases

EvolutionaryTraceiO08573.
PROiO08573.
SOURCEiSearch...

Gene expression databases

BgeeiO08573.
CleanExiMM_LGALS9.
ExpressionAtlasiO08573. baseline and differential.
GenevisibleiO08573. MM.

Family and domain databases

Gene3Di2.60.120.200. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR001079. Galectin_CRD.
[Graphical view]
PfamiPF00337. Gal-bind_lectin. 2 hits.
[Graphical view]
SMARTiSM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 2 hits.
PROSITEiPS51304. GALECTIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of galectin-9, a novel beta-galactoside-binding mammalian lectin."
    Wada J., Kanwar Y.S.
    J. Biol. Chem. 272:6078-6086(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
    Strain: CD-1.
    Tissue: Kidney and Small intestine.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Strain: FVB/NImported.
    Tissue: Mammary tumorImported.
  6. "Developmental regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside binding lectin."
    Wada J., Ota K., Kumar A., Wallner E.I., Kanwar Y.S.
    J. Clin. Invest. 99:2452-2461(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  9. "Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry."
    Bi S., Hong P.W., Lee B., Baum L.G.
    Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS LIGAND FOR P4HB.
  10. "Profiling Lgals9 splice variant expression at the fetal-maternal interface: implications in normal and pathological human pregnancy."
    Heusschen R., Freitag N., Tirado-Gonzalez I., Barrientos G., Moschansky P., Munoz-Fernandez R., Leno-Duran E., Klapp B.F., Thijssen V.L., Blois S.M.
    Biol. Reprod. 88:22-22(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
  11. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  12. "Galectin-9-CD44 interaction enhances stability and function of adaptive regulatory T cells."
    Wu C., Thalhamer T., Franca R.F., Xiao S., Wang C., Hotta C., Zhu C., Hirashima M., Anderson A.C., Kuchroo V.K.
    Immunity 41:270-282(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS LIGAND FOR CD44, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  13. "Astrocyte galectin-9 potentiates microglial TNF secretion."
    Steelman A.J., Li J.
    J. Neuroinflamm. 11:144-144(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
  14. "Crystal structure of the galectin-9 N-terminal carbohydrate recognition domain from Mus musculus reveals the basic mechanism of carbohydrate recognition."
    Nagae M., Nishi N., Murata T., Usui T., Nakamura T., Wakatsuki S., Kato R.
    J. Biol. Chem. 281:35884-35893(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 1-188 OF APOPROTEIN AND OF COMPLEX WITH CARBOHYDRATE, SUBUNIT.

Entry informationi

Entry nameiLEG9_MOUSE
AccessioniPrimary (citable) accession number: O08573
Secondary accession number(s): O08572, Q3UKE5, Q99L83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: June 8, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.