Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Galectin-9 (Gal-9) (Ecalectin) (Tumor antigen HOM-HD-21)

 LEG9_HUMAN              Reviewed;         355 AA.
O00182; A7VJG6; F8W9W4; O14532; O75028; Q3B8N1; Q53FQ0; Q8WYQ7;
Q9NQ58;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
27-SEP-2017, entry version 170.
RecName: Full=Galectin-9;
Short=Gal-9;
AltName: Full=Ecalectin;
AltName: Full=Tumor antigen HOM-HD-21;
Name=LGALS9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Spleen;
PubMed=9045665; DOI=10.1074/jbc.272.10.6416;
Tuereci O., Schmitt H., Fadle N., Pfreundschuh M., Sahin U.;
"Molecular definition of a novel human galectin which is immunogenic
in patients with Hodgkin's disease.";
J. Biol. Chem. 272:6416-6422(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Gastric carcinoma;
Kato S.;
"Human galectin-9 isoform full-length cDNA from gastric
adenocarcinoma.";
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND VARIANT SER-5.
PubMed=9642261; DOI=10.1074/jbc.273.27.16976;
Matsumoto R., Matsumoto H., Seki M., Hata M., Asano Y., Kanegasaki S.,
Stevens R.L., Hirashima M.;
"Human ecalectin, a variant of human galectin-9, is a novel eosinophil
chemoattractant produced by T lymphocytes.";
J. Biol. Chem. 273:16976-16984(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Stomach;
Nakajima H., Shichiri M., Hamaguchi T.;
"Cloning and expression of human urate transporter mRNA.";
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS
1 AND 3).
Akiyama S.;
"Homo sapiens galectin-9 (LGALS9) / ecalectin gene.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Graessler J., Spitzenberger F., Schroeder H.E.;
"Genomic organization of the human galectin-9 gene.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-5.
TISSUE=Gastric mucosa;
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
FUNCTION.
PubMed=16116184; DOI=10.4049/jimmunol.175.5.2974;
Dai S.Y., Nakagawa R., Itoh A., Murakami H., Kashio Y., Abe H.,
Katoh S., Kontani K., Kihara M., Zhang S.L., Hata T., Nakamura T.,
Yamauchi A., Hirashima M.;
"Galectin-9 induces maturation of human monocyte-derived dendritic
cells.";
J. Immunol. 175:2974-2981(2005).
[12]
FUNCTION AS LIGAND FOR HAVCR2/TIM3.
PubMed=16286920; DOI=10.1038/ni1271;
Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J.,
Zheng X.X., Strom T.B., Kuchroo V.K.;
"The Tim-3 ligand galectin-9 negatively regulates T helper type 1
immunity.";
Nat. Immunol. 6:1245-1252(2005).
[13]
FUNCTION, AND INDUCTION.
PubMed=20209097; DOI=10.1371/journal.pone.0009504;
Mengshol J.A., Golden-Mason L., Arikawa T., Smith M., Niki T.,
McWilliams R., Randall J.A., McMahan R., Zimmerman M.A.,
Rangachari M., Dobrinskikh E., Busson P., Polyak S.J., Hirashima M.,
Rosen H.R.;
"A crucial role for Kupffer cell-derived galectin-9 in regulation of T
cell immunity in hepatitis C infection.";
PLoS ONE 5:E9504-E9504(2010).
[14]
FUNCTION AS LIGAND FOR P4HB.
PubMed=21670307; DOI=10.1073/pnas.1017954108;
Bi S., Hong P.W., Lee B., Baum L.G.;
"Galectin-9 binding to cell surface protein disulfide isomerase
regulates the redox environment to enhance T-cell migration and HIV
entry.";
Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011).
[15]
SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE
SPECIFICITY.
PubMed=23242525; DOI=10.1095/biolreprod.112.105460;
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.;
"Profiling Lgals9 splice variant expression at the fetal-maternal
interface: implications in normal and pathological human pregnancy.";
Biol. Reprod. 88:22-22(2013).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=23817958; DOI=10.1002/eji.201343335;
Gieseke F., Kruchen A., Tzaribachev N., Bentzien F., Dominici M.,
Muller I.;
"Proinflammatory stimuli induce galectin-9 in human mesenchymal
stromal cells to suppress T-cell proliferation.";
Eur. J. Immunol. 43:2741-2749(2013).
[17]
FUNCTION.
PubMed=23408620; DOI=10.1128/JVI.01085-12;
Golden-Mason L., McMahan R.H., Strong M., Reisdorph R., Mahaffey S.,
Palmer B.E., Cheng L., Kulesza C., Hirashima M., Niki T., Rosen H.R.;
"Galectin-9 functionally impairs natural killer cells in humans and
mice.";
J. Virol. 87:4835-4845(2013).
[18]
INDUCTION.
PubMed=24786365; DOI=10.1089/AID.2014.0004;
Tandon R., Chew G.M., Byron M.M., Borrow P., Niki T., Hirashima M.,
Barbour J.D., Norris P.J., Lanteri M.C., Martin J.N., Deeks S.G.,
Ndhlovu L.C.;
"Galectin-9 is rapidly released during acute HIV-1 infection and
remains sustained at high levels despite viral suppression even in
elite controllers.";
AIDS Res. Hum. Retroviruses 30:654-664(2014).
[19]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND ALTERNATIVE
SPLICING (ISOFORMS 1; 2; 3; 4 AND 5).
PubMed=24333696; DOI=10.1016/j.bbadis.2013.12.003;
Heusschen R., Schulkens I.A., van Beijnum J., Griffioen A.W.,
Thijssen V.L.;
"Endothelial LGALS9 splice variant expression in endothelial cell
biology and angiogenesis.";
Biochim. Biophys. Acta 1842:284-292(2014).
[20]
FUNCTION.
PubMed=24465902; DOI=10.1371/journal.pone.0086106;
Kojima R., Ohno T., Iikura M., Niki T., Hirashima M., Iwaya K.,
Tsuda H., Nonoyama S., Matsuda A., Saito H., Matsumoto K., Nakae S.;
"Galectin-9 enhances cytokine secretion, but suppresses survival and
degranulation, in human mast cell line.";
PLoS ONE 9:E86106-E86106(2014).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=25578313; DOI=10.1038/cmi.2014.126;
Li Y.H., Zhou W.H., Tao Y., Wang S.C., Jiang Y.L., Zhang D.,
Piao H.L., Fu Q., Li D.J., Du M.R.;
"The Galectin-9/Tim-3 pathway is involved in the regulation of NK cell
function at the maternal-fetal interface in early pregnancy.";
Cell. Mol. Immunol. 13:73-81(2016).
[22]
FUNCTION, AND INDUCTION.
PubMed=25754930; DOI=10.1111/jcmm.12500;
Hsu Y.L., Wang M.Y., Ho L.J., Huang C.Y., Lai J.H.;
"Up-regulation of galectin-9 induces cell migration in human dendritic
cells infected with dengue virus.";
J. Cell. Mol. Med. 19:1065-1076(2015).
[23]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH
LACTOSE AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE
SPECIFICITY, AND FUNCTION.
PubMed=18005988; DOI=10.1016/j.jmb.2007.09.060;
Nagae M., Nishi N., Nakamura-Tsuruta S., Hirabayashi J., Wakatsuki S.,
Kato R.;
"Structural analysis of the human galectin-9 N-terminal carbohydrate
recognition domain reveals unexpected properties that differ from the
mouse orthologue.";
J. Mol. Biol. 375:119-135(2008).
[24]
X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-150 IN COMPLEX WITH
L-ACETYLLACTOSAMINE.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of N-terminal domain of human galectin-9 containing
L-acetyllactosamine.";
Submitted (APR-2008) to the PDB data bank.
[25]
X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1-148 IN COMPLEXES WITH
N-ACETYLLACTOSAMINE OLIGOMERS, AND FUNCTION.
PubMed=18977853; DOI=10.1093/glycob/cwn121;
Nagae M., Nishi N., Murata T., Usui T., Nakamura T., Wakatsuki S.,
Kato R.;
"Structural analysis of the recognition mechanism of poly-N-
acetyllactosamine by the human galectin-9 N-terminal carbohydrate
recognition domain.";
Glycobiology 19:112-117(2009).
[26]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-323 IN COMPLEXES WITH
OLIGOSACCHARIDES.
PubMed=20861009; DOI=10.1074/jbc.M110.163402;
Yoshida H., Teraoka M., Nishi N., Nakakita S., Nakamura T.,
Hirashima M., Kamitori S.;
"X-ray structures of human galectin-9 C-terminal domain in complexes
with a biantennary oligosaccharide and sialyllactose.";
J. Biol. Chem. 285:36969-36976(2010).
-!- FUNCTION: Binds galactosides (PubMed:18005988). Has high affinity
for the Forssman pentasaccharide (PubMed:18005988). Ligand for
HAVCR2/TIM3 (PubMed:16286920). Binding to HAVCR2 induces T-helper
type 1 lymphocyte (Th1) death (PubMed:16286920). Also stimulates
bactericidal activity in infected macrophages by causing
macrophage activation and IL1B secretion which restricts
intracellular bacterial growth (By similarity). 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 (By similarity).
Promotes ability of mesenchymal stromal cells to suppress T-cell
proliferation (PubMed:23817958). Expands regulatory T-cells and
induces cytotoxic T-cell apoptosis following virus infection
(PubMed:20209097). Activates ERK1/2 phosphorylation inducing
cytokine (IL-6, IL-8, IL-12) and chemokine (CCL2) production in
mast and dendritic cells (PubMed:24465902, PubMed:16116184).
Inhibits degranulation and induces apoptosis of mast cells
(PubMed:24465902). Induces maturation and migration of dendritic
cells (PubMed:25754930, PubMed:16116184). Inhibits natural killer
(NK) cell function (PubMed:23408620). Can transform NK cell
phenotype from peripheral to decidual during pregnancy
(PubMed:25578313). Astrocyte derived galectin-9 enhances
microglial TNF production (By similarity). 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). {ECO:0000250|UniProtKB:O08573,
ECO:0000250|UniProtKB:P97840, ECO:0000269|PubMed:16116184,
ECO:0000269|PubMed:16286920, ECO:0000269|PubMed:18005988,
ECO:0000269|PubMed:18977853, ECO:0000269|PubMed:20209097,
ECO:0000269|PubMed:21670307, ECO:0000269|PubMed:23408620,
ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:24465902,
ECO:0000269|PubMed:25578313, ECO:0000269|PubMed:25754930}.
-!- FUNCTION: Isoform 2: Acts as an eosinophil chemoattractant
(PubMed:9642261). It also inhibits angiogenesis (PubMed:24333696).
Suppresses IFNG production by natural killer cells (By
similarity). {ECO:0000250|UniProtKB:O08573,
ECO:0000269|PubMed:24333696, ECO:0000269|PubMed:9642261}.
-!- SUBUNIT: Monomer. {ECO:0000305|PubMed:18005988,
ECO:0000305|Ref.24}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}.
Nucleus {ECO:0000269|PubMed:23242525}. Secreted
{ECO:0000269|PubMed:23817958, ECO:0000269|PubMed:25578313}.
Note=May also be secreted by a non-classical secretory pathway (By
similarity). Secreted by mesenchymal stromal cells upon IFNG
stimulation (PubMed:23817958). {ECO:0000250|UniProtKB:O08573,
ECO:0000269|PubMed:23817958}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:24333696}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted
{ECO:0000269|PubMed:24333696}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Long, Gal-9FL {ECO:0000303|PubMed:24333696};
IsoId=O00182-1; Sequence=Displayed;
Name=2; Synonyms=Medium, Gal-9delta5
{ECO:0000303|PubMed:24333696}, D5 {ECO:0000303|PubMed:23242525};
IsoId=O00182-2; Sequence=VSP_003096;
Name=3; Synonyms=Short, Gal-9delta5/6
{ECO:0000303|PubMed:24333696}, D5/6 {ECO:0000303|PubMed:23242525};
IsoId=O00182-3; Sequence=VSP_003096, VSP_057842;
Name=4; Synonyms=Gal-9delta5/10 {ECO:0000303|PubMed:24333696},
D5/10 {ECO:0000303|PubMed:23242525};
IsoId=O00182-4; Sequence=VSP_003096, VSP_057843;
Name=5; Synonyms=Gal-9delta5/6/10 {ECO:0000303|PubMed:24333696},
D5/6/10 {ECO:0000303|PubMed:23242525};
IsoId=O00182-5; Sequence=VSP_003096, VSP_057842, VSP_057843;
Name=6; Synonyms=D6 {ECO:0000303|PubMed:23242525};
IsoId=O00182-6; Sequence=VSP_057842;
-!- TISSUE SPECIFICITY: Peripheral blood leukocytes and lymphatic
tissues. Expressed in lung, liver, breast and kidney with higher
levels in tumor endothelial cells than normal endothelium (at
protein level) (PubMed:24333696). Expressed in trophoblast cells
in decidua and placenta in pregnancy (at protein level)
(PubMed:23242525, PubMed:25578313). Isoform 2 is the most abundant
isoform expressed in endothelial cells (PubMed:24333696). Upon
endothelial cell activation isoform 2 expression decreases while
expression of isoform 3 and isoform 5 increases (PubMed:24333696).
Isoform 4 decreases in pathological pregnancy (PubMed:23242525).
{ECO:0000269|PubMed:23242525, ECO:0000269|PubMed:24333696,
ECO:0000269|PubMed:25578313}.
-!- INDUCTION: By toll-like receptor ligands zymosan (TLR2 ligand),
polyinosinic:polycytidylic acid (poly I:C) (TLR3 ligand) and
lipopolysaccharides (LPS) (TLR4 ligand) and by proinflammatory
cytokines IFNG, TNFA, IL1A and IL1B in mesenchymal stromal cells
(PubMed:23817958). By IFNG in macrophages (PubMed:20209097). Up-
regulated in dendritic cells following infection with dengue virus
(PubMed:25754930). Up-regulated in Kupffer cells following
infection with hepatitis C virus (PubMed:20209097). Up-regulated
in plasma following infection with HIV-1 (PubMed:24786365).
{ECO:0000269|PubMed:20209097, ECO:0000269|PubMed:23817958,
ECO:0000269|PubMed:24786365, ECO:0000269|PubMed:25754930}.
-!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
domains.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-9;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00120";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Z49107; CAA88922.1; -; mRNA.
EMBL; AB006782; BAA22166.1; -; mRNA.
EMBL; AB005894; BAA31542.1; -; mRNA.
EMBL; AB003517; BAF76327.1; -; mRNA.
EMBL; AB008492; BAF76328.1; -; mRNA.
EMBL; AB040130; BAB83623.1; -; Genomic_DNA.
EMBL; AB040130; BAB83625.1; -; Genomic_DNA.
EMBL; AB040130; BAB83624.1; -; Genomic_DNA.
EMBL; AJ288083; CAB93851.1; -; Genomic_DNA.
EMBL; AJ288084; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288085; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288086; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288087; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288088; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288089; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AJ288090; CAB93851.1; JOINED; Genomic_DNA.
EMBL; AK223232; BAD96952.1; -; mRNA.
EMBL; AC015688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471159; EAW51037.1; -; Genomic_DNA.
EMBL; CH471159; EAW51038.1; -; Genomic_DNA.
EMBL; CH471159; EAW51039.1; -; Genomic_DNA.
EMBL; CH471159; EAW51044.1; -; Genomic_DNA.
EMBL; BC105942; AAI05943.1; -; mRNA.
EMBL; BC105944; AAI05945.1; -; mRNA.
EMBL; BC110340; AAI10341.1; -; mRNA.
CCDS; CCDS11222.1; -. [O00182-1]
CCDS; CCDS32592.1; -. [O00182-2]
CCDS; CCDS82093.1; -. [O00182-4]
RefSeq; NP_001317092.1; NM_001330163.1. [O00182-4]
RefSeq; NP_002299.2; NM_002308.3. [O00182-2]
RefSeq; NP_033665.1; NM_009587.2. [O00182-1]
RefSeq; XP_006721955.1; XM_006721892.2. [O00182-3]
RefSeq; XP_006721958.1; XM_006721895.3. [O00182-5]
RefSeq; XP_016880112.1; XM_017024623.1. [O00182-6]
UniGene; Hs.81337; -.
PDB; 2EAK; X-ray; 1.97 A; A/B/C=1-148.
PDB; 2EAL; X-ray; 1.85 A; A/B=1-148.
PDB; 2YY1; X-ray; 2.17 A; A=1-147.
PDB; 2ZHK; X-ray; 1.80 A; A/B=1-148.
PDB; 2ZHL; X-ray; 1.75 A; A/B/C/D=1-148.
PDB; 2ZHM; X-ray; 1.84 A; A/B/C/D=1-148.
PDB; 2ZHN; X-ray; 1.30 A; A=1-148.
PDB; 3LSD; X-ray; 2.03 A; A=6-148.
PDB; 3LSE; X-ray; 2.69 A; A=6-148.
PDB; 3NV1; X-ray; 1.50 A; A=218-355.
PDB; 3NV2; X-ray; 2.34 A; A=218-355.
PDB; 3NV3; X-ray; 1.57 A; A=218-355.
PDB; 3NV4; X-ray; 1.99 A; A=218-355.
PDB; 3WLU; X-ray; 1.40 A; A/B/C/D=5-148.
PDB; 3WV6; X-ray; 1.95 A; A/B=1-148, A/B=178-355.
PDBsum; 2EAK; -.
PDBsum; 2EAL; -.
PDBsum; 2YY1; -.
PDBsum; 2ZHK; -.
PDBsum; 2ZHL; -.
PDBsum; 2ZHM; -.
PDBsum; 2ZHN; -.
PDBsum; 3LSD; -.
PDBsum; 3LSE; -.
PDBsum; 3NV1; -.
PDBsum; 3NV2; -.
PDBsum; 3NV3; -.
PDBsum; 3NV4; -.
PDBsum; 3WLU; -.
PDBsum; 3WV6; -.
ProteinModelPortal; O00182; -.
SMR; O00182; -.
BioGrid; 110156; 79.
IntAct; O00182; 13.
STRING; 9606.ENSP00000378856; -.
BindingDB; O00182; -.
ChEMBL; CHEMBL5474; -.
DrugBank; DB04472; (R)-1-Para-Nitro-Phenyl-2-Azido-Ethanol.
iPTMnet; O00182; -.
PhosphoSitePlus; O00182; -.
BioMuta; LGALS9; -.
EPD; O00182; -.
MaxQB; O00182; -.
PaxDb; O00182; -.
PeptideAtlas; O00182; -.
PRIDE; O00182; -.
Ensembl; ENST00000302228; ENSP00000306228; ENSG00000168961. [O00182-2]
Ensembl; ENST00000313648; ENSP00000318214; ENSG00000168961. [O00182-4]
Ensembl; ENST00000395473; ENSP00000378856; ENSG00000168961. [O00182-1]
GeneID; 3965; -.
KEGG; hsa:3965; -.
UCSC; uc002gzp.4; human. [O00182-1]
UCSC; uc060cvd.1; human.
CTD; 3965; -.
DisGeNET; 3965; -.
EuPathDB; HostDB:ENSG00000168961.16; -.
GeneCards; LGALS9; -.
HGNC; HGNC:6570; LGALS9.
HPA; HPA046876; -.
HPA; HPA047218; -.
MIM; 601879; gene.
neXtProt; NX_O00182; -.
OpenTargets; ENSG00000168961; -.
PharmGKB; PA30347; -.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00760000119105; -.
HOGENOM; HOG000290194; -.
HOVERGEN; HBG002412; -.
InParanoid; O00182; -.
KO; K10093; -.
OMA; VCNTRQN; -.
OrthoDB; EOG091G0WP8; -.
PhylomeDB; O00182; -.
TreeFam; TF315551; -.
Reactome; R-HSA-451927; Interleukin-2 family signaling.
ChiTaRS; LGALS9; human.
EvolutionaryTrace; O00182; -.
GeneWiki; LGALS9; -.
GenomeRNAi; 3965; -.
PRO; PR:O00182; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000168961; -.
CleanEx; HS_LGALS9; -.
ExpressionAtlas; O00182; baseline and differential.
Genevisible; O00182; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
GO; GO:0048030; F:disaccharide binding; IMP:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0005534; F:galactose binding; TAS:ProtInc.
GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IDA:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0007565; P:female pregnancy; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:UniProtKB.
GO; GO:0002519; P:natural killer cell tolerance induction; IMP:UniProtKB.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
GO; GO:0032682; P:negative regulation of chemokine production; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0043305; P:negative regulation of mast cell degranulation; IMP:UniProtKB.
GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0038066; P:p38MAPK cascade; IDA:UniProtKB.
GO; GO:0070241; P:positive regulation of activated T cell autonomous cell death; IDA:UniProtKB.
GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB.
GO; GO:0032834; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response; IDA:UniProtKB.
GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IDA:UniProtKB.
GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB.
GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:1902715; P:positive regulation of interferon-gamma secretion; IDA:UniProtKB.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IDA:UniProtKB.
GO; GO:2001181; P:positive regulation of interleukin-10 secretion; IDA:UniProtKB.
GO; GO:2001184; P:positive regulation of interleukin-12 secretion; IMP:UniProtKB.
GO; GO:2000667; P:positive regulation of interleukin-13 secretion; IDA:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; IMP:UniProtKB.
GO; GO:2000484; P:positive regulation of interleukin-8 secretion; IMP:UniProtKB.
GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:2001190; P:positive regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:UniProtKB.
GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:UniProtKB.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IDA:UniProtKB.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0070555; P:response to interleukin-1; IDA:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB.
CDD; cd00070; GLECT; 2.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR001079; Galectin_CRD.
Pfam; PF00337; Gal-bind_lectin; 2.
SMART; SM00908; Gal-bind_lectin; 2.
SMART; SM00276; GLECT; 2.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS51304; GALECTIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chemotaxis; Complete proteome;
Cytoplasm; Immunity; Lectin; Nucleus; Polymorphism;
Reference proteome; Repeat; Secreted.
CHAIN 1 355 Galectin-9.
/FTId=PRO_0000076946.
DOMAIN 17 148 Galectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
DOMAIN 227 355 Galectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 82 88 Beta-galactoside binding 1.
REGION 287 293 Beta-galactoside binding 2.
{ECO:0000250}.
BINDING 48 48 Beta-galactoside 1.
BINDING 61 61 Beta-galactoside 1.
BINDING 65 65 Beta-galactoside 1.
BINDING 75 75 Beta-galactoside 1.
BINDING 267 267 Beta-galactoside 2.
BINDING 271 271 Beta-galactoside 2.
BINDING 281 281 Beta-galactoside 2. {ECO:0000250}.
VAR_SEQ 149 180 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000269|PubMed:24333696,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9045665,
ECO:0000303|PubMed:9642261,
ECO:0000303|Ref.4, ECO:0000303|Ref.7}.
/FTId=VSP_003096.
VAR_SEQ 181 192 Missing (in isoform 3, isoform 5 and
isoform 6). {ECO:0000269|PubMed:23242525,
ECO:0000269|PubMed:24333696}.
/FTId=VSP_057842.
VAR_SEQ 254 355 FHINLCSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSL
PRKMPFVRGQSFSVWILCEAHCLKVAVDGQHLFEYYHRLRN
LPTINRLEVGGDIQLTHVQT -> CGSCVKLTASRWPWMVS
TCLNTTIA (in isoform 4 and isoform 5).
{ECO:0000269|PubMed:24333696}.
/FTId=VSP_057843.
VARIANT 5 5 G -> S (in dbSNP:rs3751093).
{ECO:0000269|PubMed:9642261,
ECO:0000269|Ref.7}.
/FTId=VAR_020453.
CONFLICT 48 48 N -> D (in Ref. 6; CAB93851).
{ECO:0000305}.
CONFLICT 79 81 NGS -> KGR (in Ref. 6; CAB93851).
{ECO:0000305}.
CONFLICT 88 88 K -> R (in Ref. 1; CAA88922).
{ECO:0000305}.
CONFLICT 89 89 T -> M (in Ref. 6; CAB93851).
{ECO:0000305}.
CONFLICT 93 93 F -> S (in Ref. 7; BAD96952).
{ECO:0000305}.
CONFLICT 135 135 S -> F (in Ref. 1; CAA88922).
{ECO:0000305}.
CONFLICT 270 270 P -> L (in Ref. 1; CAA88922).
{ECO:0000305}.
CONFLICT 313 313 E -> G (in Ref. 1; CAA88922).
{ECO:0000305}.
CONFLICT 326 326 L -> V (in Ref. 6; CAB93851).
{ECO:0000305}.
CONFLICT 341 341 R -> K (in Ref. 6; CAB93851).
{ECO:0000305}.
STRAND 5 7 {ECO:0000244|PDB:2ZHN}.
STRAND 10 12 {ECO:0000244|PDB:2ZHN}.
STRAND 15 20 {ECO:0000244|PDB:2ZHN}.
STRAND 30 37 {ECO:0000244|PDB:2ZHN}.
STRAND 39 41 {ECO:0000244|PDB:2ZHN}.
STRAND 43 56 {ECO:0000244|PDB:2ZHN}.
STRAND 58 65 {ECO:0000244|PDB:2ZHN}.
STRAND 71 78 {ECO:0000244|PDB:2ZHN}.
STRAND 86 89 {ECO:0000244|PDB:2ZHN}.
STRAND 98 105 {ECO:0000244|PDB:2ZHN}.
STRAND 107 114 {ECO:0000244|PDB:2ZHN}.
STRAND 117 123 {ECO:0000244|PDB:2ZHN}.
HELIX 128 130 {ECO:0000244|PDB:2ZHN}.
STRAND 133 146 {ECO:0000244|PDB:2ZHN}.
STRAND 225 230 {ECO:0000244|PDB:3NV1}.
STRAND 240 247 {ECO:0000244|PDB:3NV1}.
STRAND 253 260 {ECO:0000244|PDB:3NV1}.
STRAND 263 271 {ECO:0000244|PDB:3NV1}.
TURN 272 275 {ECO:0000244|PDB:3NV1}.
STRAND 276 283 {ECO:0000244|PDB:3NV1}.
STRAND 295 297 {ECO:0000244|PDB:3NV1}.
STRAND 305 312 {ECO:0000244|PDB:3NV1}.
STRAND 314 321 {ECO:0000244|PDB:3NV1}.
STRAND 324 330 {ECO:0000244|PDB:3NV1}.
HELIX 336 338 {ECO:0000244|PDB:3NV1}.
STRAND 341 354 {ECO:0000244|PDB:3NV1}.
SEQUENCE 355 AA; 39518 MW; 4748C22FCAFA536A CRC64;
MAFSGSQAPY LSPAVPFSGT IQGGLQDGLQ ITVNGTVLSS SGTRFAVNFQ TGFSGNDIAF
HFNPRFEDGG YVVCNTRQNG SWGPEERKTH MPFQKGMPFD LCFLVQSSDF KVMVNGILFV
QYFHRVPFHR VDTISVNGSV QLSYISFQNP RTVPVQPAFS TVPFSQPVCF PPRPRGRRQK
PPGVWPANPA PITQTVIHTV QSAPGQMFST PAIPPMMYPH PAYPMPFITT ILGGLYPSKS
ILLSGTVLPS AQRFHINLCS GNHIAFHLNP RFDENAVVRN TQIDNSWGSE ERSLPRKMPF
VRGQSFSVWI LCEAHCLKVA VDGQHLFEYY HRLRNLPTIN RLEVGGDIQL THVQT


Related products :

Catalog number Product name Quantity
29-012 SART3 is an RNA-binding nuclear protein that is a tumor-rejection antigen. This antigen possesses tumor epitopes capable of inducing HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes in ca 0.1 mg
E1108h ELISA kit Gal-8,Galectin-8,Homo sapiens,Human,LGALS8,PCTA-1,Po66 carbohydrate-binding protein,Po66-CBP,Prostate carcinoma tumor antigen 1 96T
U1108h CLIA Gal-8,Galectin-8,Homo sapiens,Human,LGALS8,PCTA-1,Po66 carbohydrate-binding protein,Po66-CBP,Prostate carcinoma tumor antigen 1 96T
E1108h ELISA Gal-8,Galectin-8,Homo sapiens,Human,LGALS8,PCTA-1,Po66 carbohydrate-binding protein,Po66-CBP,Prostate carcinoma tumor antigen 1 96T
E0928h ELISA Antigen NY-CO-13,Cellular tumor antigen p53,Homo sapiens,Human,P53,Phosphoprotein p53,TP53,Tumor suppressor p53 96T
E0928h ELISA kit Antigen NY-CO-13,Cellular tumor antigen p53,Homo sapiens,Human,P53,Phosphoprotein p53,TP53,Tumor suppressor p53 96T
U0928h CLIA Antigen NY-CO-13,Cellular tumor antigen p53,Homo sapiens,Human,P53,Phosphoprotein p53,TP53,Tumor suppressor p53 96T
18-662-20095 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 ml
18-003-42884 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 mg Protein A
18-661-15115 Cellular tumor antigen p53 - Tumor suppressor p53; Phosphoprotein p53; Antigen NY-CO-13 Polyclonal 0.1 mg
EIAAB28233 Chronic myelogenous leukemia tumor antigen 66,CML66,Homo sapiens,Human,NudC domain-containing protein 1,NUDCD1,Tumor antigen CML66
E1278h ELISA kit ETAA1,ETAA16,Ewing's tumor-associated antigen 1,Ewing's tumor-associated antigen 16,Homo sapiens,Human 96T
E1278h ELISA ETAA1,ETAA16,Ewing's tumor-associated antigen 1,Ewing's tumor-associated antigen 16,Homo sapiens,Human 96T
U1278h CLIA ETAA1,ETAA16,Ewing's tumor-associated antigen 1,Ewing's tumor-associated antigen 16,Homo sapiens,Human 96T
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.05 mg
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.1 mg
EIAAB45969 HCC8,Hepatocellular carcinoma protein 8,Homo sapiens,Human,Tumor antigen HOM-HCC-8,Tumor antigen SLP-8p,Vacuolar protein sorting-associated protein 54,VPS54
orb80333 Human Galectin 4 protein Galectin 4 produced in E.coli is a single, non-glycosylated polypeptide chain containing 343 amino acids (1-323 a.a.) and having a molecular mass of 38.1kDa.Galectin 4 is fuse 5
U0928p CLIA Cellular tumor antigen p53,P53,Pig,Sus scrofa,TP53,Tumor suppressor p53 96T
E0928p ELISA kit Cellular tumor antigen p53,P53,Pig,Sus scrofa,TP53,Tumor suppressor p53 96T
E0928p ELISA Cellular tumor antigen p53,P53,Pig,Sus scrofa,TP53,Tumor suppressor p53 96T
U0928r CLIA Cellular tumor antigen p53,P53,Rat,Rattus norvegicus,Tp53,Tumor suppressor p53 96T
U0928b CLIA Bos taurus,Bovine,Cellular tumor antigen p53,TP53,Tumor suppressor p53 96T
E0928b ELISA kit Bos taurus,Bovine,Cellular tumor antigen p53,TP53,Tumor suppressor p53 96T
E0928r ELISA kit Cellular tumor antigen p53,P53,Rat,Rattus norvegicus,Tp53,Tumor suppressor p53 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur