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O00182 (LEG9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Galectin-9

Short name=Gal-9
Alternative name(s):
Ecalectin
Tumor antigen HOM-HD-21
Gene names
Name:LGALS9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length355 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds galactosides. Has high affinity for the Forssman pentasaccharide. May play a role in thymocyte-epithelial interactions relevant to the biology of the thymus. Inhibits cell proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil chemoattractant. Ref.10 Ref.11 Ref.13

Subunit structure

Monomer Probable. Ref.11

Subcellular location

Cytoplasm By similarity. Secreted By similarity. Note: May also be secreted by a non-classical secretory pathway By similarity.

Tissue specificity

Peripheral blood leukocytes and lymphatic tissues. Overexpressed in Hodgkin disease tissue.

Domain

Contains two homologous but distinct carbohydrate-binding domains.

Sequence similarities

Contains 2 galectin domains.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform Long (identifier: O00182-1)

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.
Isoform Short (identifier: O00182-2)

The sequence of this isoform differs from the canonical sequence as follows:
     149-180: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 355355Galectin-9
PRO_0000076946

Regions

Domain17 – 148132Galectin 1
Domain227 – 355129Galectin 2
Region82 – 887Beta-galactoside binding 1
Region287 – 2937Beta-galactoside binding 2 By similarity

Sites

Binding site481Beta-galactoside 1
Binding site611Beta-galactoside 1
Binding site651Beta-galactoside 1
Binding site751Beta-galactoside 1
Binding site2671Beta-galactoside 2
Binding site2711Beta-galactoside 2
Binding site2811Beta-galactoside 2 By similarity

Natural variations

Alternative sequence149 – 18032Missing in isoform Short.
VSP_003096
Natural variant51G → S. Ref.3 Ref.7
Corresponds to variant rs3751093 [ dbSNP | Ensembl ].
VAR_020453

Experimental info

Sequence conflict481N → D in CAB93851. Ref.6
Sequence conflict79 – 813NGS → KGR in CAB93851. Ref.6
Sequence conflict881K → R in CAA88922. Ref.1
Sequence conflict891T → M in CAB93851. Ref.6
Sequence conflict931F → S in BAD96952. Ref.7
Sequence conflict1351S → F in CAA88922. Ref.1
Sequence conflict2701P → L in CAA88922. Ref.1
Sequence conflict3131E → G in CAA88922. Ref.1
Sequence conflict3261L → V in CAB93851. Ref.6
Sequence conflict3411R → K in CAB93851. Ref.6

Secondary structure

................................................... 355
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified July 15, 1998. Version 2.
Checksum: 4748C22FCAFA536A

FASTA35539,518
        10         20         30         40         50         60 
MAFSGSQAPY LSPAVPFSGT IQGGLQDGLQ ITVNGTVLSS SGTRFAVNFQ TGFSGNDIAF 

        70         80         90        100        110        120 
HFNPRFEDGG YVVCNTRQNG SWGPEERKTH MPFQKGMPFD LCFLVQSSDF KVMVNGILFV 

       130        140        150        160        170        180 
QYFHRVPFHR VDTISVNGSV QLSYISFQNP RTVPVQPAFS TVPFSQPVCF PPRPRGRRQK 

       190        200        210        220        230        240 
PPGVWPANPA PITQTVIHTV QSAPGQMFST PAIPPMMYPH PAYPMPFITT ILGGLYPSKS 

       250        260        270        280        290        300 
ILLSGTVLPS AQRFHINLCS GNHIAFHLNP RFDENAVVRN TQIDNSWGSE ERSLPRKMPF 

       310        320        330        340        350 
VRGQSFSVWI LCEAHCLKVA VDGQHLFEYY HRLRNLPTIN RLEVGGDIQL THVQT 

« Hide

Isoform Short [UniParc].

Checksum: 1A3EB2941FC7F377
Show »

FASTA32335,888

References

« Hide 'large scale' references
[1]"Molecular definition of a novel human galectin which is immunogenic in patients with Hodgkin's disease."
Tuereci O., Schmitt H., Fadle N., Pfreundschuh M., Sahin U.
J. Biol. Chem. 272:6416-6422(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
Tissue: Spleen.
[2]"Human galectin-9 isoform full-length cDNA from gastric adenocarcinoma."
Kato S.
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Gastric carcinoma.
[3]"Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes."
Matsumoto R., Matsumoto H., Seki M., Hata M., Asano Y., Kanegasaki S., Stevens R.L., Hirashima M.
J. Biol. Chem. 273:16976-16984(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), VARIANT SER-5.
[4]"Cloning and expression of human urate transporter mRNA."
Nakajima H., Shichiri M., Hamaguchi T.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
Tissue: Kidney and Stomach.
[5]"Homo sapiens galectin-9 (LGALS9) / ecalectin gene, exon 2 through 11."
Akiyama S.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Genomic organization of the human galectin-9 gene."
Graessler J., Spitzenberger F., Schroeder H.E.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT), VARIANT SER-5.
Tissue: Gastric mucosa.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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 SHORT).
Tissue: Colon.
[10]"The Tim-3 ligand galectin-9 negatively regulates T helper type 1 immunity."
Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J., Zheng X.X., Strom T.B., Kuchroo V.K.
Nat. Immunol. 6:1245-1252(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS LIGAND FOR HAVCR2/TIM3.
[11]"Structural analysis of the human galectin-9 N-terminal carbohydrate recognition domain reveals unexpected properties that differ from the mouse orthologue."
Nagae M., Nishi N., Nakamura-Tsuruta S., Hirabayashi J., Wakatsuki S., Kato R.
J. Mol. Biol. 375:119-135(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH LACTOSE AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE SPECIFICITY, FUNCTION.
[12]"Crystal structure of N-terminal domain of human galectin-9 containing L-acetyllactosamine."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-150 IN COMPLEX WITH L-ACETYLLACTOSAMINE.
[13]"Structural analysis of the recognition mechanism of poly-N-acetyllactosamine by the human galectin-9 N-terminal carbohydrate recognition domain."
Nagae M., Nishi N., Murata T., Usui T., Nakamura T., Wakatsuki S., Kato R.
Glycobiology 19:112-117(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1-148 IN COMPLEXES WITH N-ACETYLLACTOSAMINE OLIGOMERS, FUNCTION.
[14]"X-ray structures of human galectin-9 C-terminal domain in complexes with a biantennary oligosaccharide and sialyllactose."
Yoshida H., Teraoka M., Nishi N., Nakakita S., Nakamura T., Hirashima M., Kamitori S.
J. Biol. Chem. 285:36969-36976(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-323 IN COMPLEXES WITH OLIGOSACCHARIDES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z49107 mRNA. Translation: CAA88922.1.
AB006782 mRNA. Translation: BAA22166.1.
AB005894 mRNA. Translation: BAA31542.1.
AB003517 mRNA. Translation: BAF76327.1.
AB008492 mRNA. Translation: BAF76328.1.
AB040130 Genomic DNA. Translation: BAB83625.1.
AB040130 Genomic DNA. Translation: BAB83624.1.
AJ288083 expand/collapse EMBL AC list , AJ288084, AJ288085, AJ288086, AJ288087, AJ288088, AJ288089, AJ288090 Genomic DNA. Translation: CAB93851.1.
AK223232 mRNA. Translation: BAD96952.1.
CH471159 Genomic DNA. Translation: EAW51037.1.
CH471159 Genomic DNA. Translation: EAW51044.1.
BC105942 mRNA. Translation: AAI05943.1.
BC105944 mRNA. Translation: AAI05945.1.
BC110340 mRNA. Translation: AAI10341.1.
RefSeqNP_002299.2. NM_002308.3.
NP_033665.1. NM_009587.2.
UniGeneHs.81337.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EAKX-ray1.97A/B/C1-148[»]
2EALX-ray1.85A/B1-148[»]
2YY1X-ray2.17A1-147[»]
2ZHKX-ray1.80A/B1-148[»]
2ZHLX-ray1.75A/B/C/D1-148[»]
2ZHMX-ray1.84A/B/C/D1-148[»]
2ZHNX-ray1.30A1-148[»]
3LSDX-ray2.03A6-148[»]
3LSEX-ray2.69A6-148[»]
3NV1X-ray1.50A218-355[»]
3NV2X-ray2.34A218-355[»]
3NV3X-ray1.57A218-355[»]
3NV4X-ray1.99A218-355[»]
ProteinModelPortalO00182.
SMRO00182. Positions 1-355.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110156. 3 interactions.
IntActO00182. 12 interactions.
STRING9606.ENSP00000378856.

Chemistry

BindingDBO00182.
ChEMBLCHEMBL5474.

PTM databases

PhosphoSiteO00182.

Proteomic databases

PRIDEO00182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302228; ENSP00000306228; ENSG00000168961. [O00182-2]
ENST00000395473; ENSP00000378856; ENSG00000168961. [O00182-1]
GeneID3965.
KEGGhsa:3965.
UCSCuc002gzp.3. human. [O00182-1]
uc002gzq.3. human. [O00182-2]

Organism-specific databases

CTD3965.
GeneCardsGC17P025956.
HGNCHGNC:6570. LGALS9.
HPAHPA046876.
HPA047218.
MIM601879. gene.
neXtProtNX_O00182.
PharmGKBPA30347.
GenAtlasSearch...

Phylogenomic databases

HOGENOMHOG000290194.
HOVERGENHBG002412.
InParanoidO00182.
KOK10093.
OMAVCNTRQN.
OrthoDBEOG73Z2TM.
PhylomeDBO00182.
TreeFamTF315551.

Gene expression databases

ArrayExpressO00182.
BgeeO00182.
CleanExHS_LGALS9.
GenevestigatorO00182.

Family and domain databases

Gene3D2.60.120.200. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR001079. Galectin_CRD.
[Graphical view]
PfamPF00337. Gal-bind_lectin. 2 hits.
[Graphical view]
SMARTSM00908. Gal-bind_lectin. 2 hits.
SM00276. GLECT. 2 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 2 hits.
PROSITEPS51304. GALECTIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSlgals9. human.
EvolutionaryTraceO00182.
GeneWikiLGALS9.
GenomeRNAi3965.
NextBio15562.
PROO00182.
SOURCESearch...

Entry information

Entry nameLEG9_HUMAN
AccessionPrimary (citable) accession number: O00182
Secondary accession number(s): A7VJG6 expand/collapse secondary AC list , O14532, O75028, Q3B8N1, Q53FQ0, Q9NQ58
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM