ID LEG9_HUMAN Reviewed; 355 AA. AC O00182; A7VJG6; F8W9W4; O14532; O75028; Q3B8N1; Q53FQ0; Q8WYQ7; Q9NQ58; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 27-MAR-2024, entry version 208. DE RecName: Full=Galectin-9; DE Short=Gal-9; DE AltName: Full=Ecalectin; DE AltName: Full=Tumor antigen HOM-HD-21; GN Name=LGALS9; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Spleen; RX PubMed=9045665; DOI=10.1074/jbc.272.10.6416; RA Tuereci O., Schmitt H., Fadle N., Pfreundschuh M., Sahin U.; RT "Molecular definition of a novel human galectin which is immunogenic in RT patients with Hodgkin's disease."; RL J. Biol. Chem. 272:6416-6422(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Gastric carcinoma; RA Kato S.; RT "Human galectin-9 isoform full-length cDNA from gastric adenocarcinoma."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND VARIANT SER-5. RX PubMed=9642261; DOI=10.1074/jbc.273.27.16976; RA Matsumoto R., Matsumoto H., Seki M., Hata M., Asano Y., Kanegasaki S., RA Stevens R.L., Hirashima M.; RT "Human ecalectin, a variant of human galectin-9, is a novel eosinophil RT chemoattractant produced by T lymphocytes."; RL J. Biol. Chem. 273:16976-16984(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Kidney, and Stomach; RA Nakajima H., Shichiri M., Hamaguchi T.; RT "Cloning and expression of human urate transporter mRNA."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORMS 1 AND RP 3). RA Akiyama S.; RT "Homo sapiens galectin-9 (LGALS9) / ecalectin gene."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Graessler J., Spitzenberger F., Schroeder H.E.; RT "Genomic organization of the human galectin-9 gene."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT SER-5. RC TISSUE=Gastric mucosa; RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP FUNCTION. RX PubMed=16116184; DOI=10.4049/jimmunol.175.5.2974; RA Dai S.Y., Nakagawa R., Itoh A., Murakami H., Kashio Y., Abe H., Katoh S., RA Kontani K., Kihara M., Zhang S.L., Hata T., Nakamura T., Yamauchi A., RA Hirashima M.; RT "Galectin-9 induces maturation of human monocyte-derived dendritic cells."; RL J. Immunol. 175:2974-2981(2005). RN [12] RP FUNCTION AS LIGAND FOR HAVCR2/TIM3. RX PubMed=16286920; DOI=10.1038/ni1271; RA Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J., RA Zheng X.X., Strom T.B., Kuchroo V.K.; RT "The Tim-3 ligand galectin-9 negatively regulates T helper type 1 RT immunity."; RL Nat. Immunol. 6:1245-1252(2005). RN [13] RP FUNCTION, AND INDUCTION. RX PubMed=20209097; DOI=10.1371/journal.pone.0009504; RA Mengshol J.A., Golden-Mason L., Arikawa T., Smith M., Niki T., RA McWilliams R., Randall J.A., McMahan R., Zimmerman M.A., Rangachari M., RA Dobrinskikh E., Busson P., Polyak S.J., Hirashima M., Rosen H.R.; RT "A crucial role for Kupffer cell-derived galectin-9 in regulation of T cell RT immunity in hepatitis C infection."; RL PLoS ONE 5:E9504-E9504(2010). RN [14] RP FUNCTION AS LIGAND FOR P4HB. RX PubMed=21670307; DOI=10.1073/pnas.1017954108; RA Bi S., Hong P.W., Lee B., Baum L.G.; RT "Galectin-9 binding to cell surface protein disulfide isomerase regulates RT the redox environment to enhance T-cell migration and HIV entry."; RL Proc. Natl. Acad. Sci. U.S.A. 108:10650-10655(2011). RN [15] RP SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE RP SPECIFICITY. RX PubMed=23242525; DOI=10.1095/biolreprod.112.105460; RA Heusschen R., Freitag N., Tirado-Gonzalez I., Barrientos G., Moschansky P., RA Munoz-Fernandez R., Leno-Duran E., Klapp B.F., Thijssen V.L., Blois S.M.; RT "Profiling Lgals9 splice variant expression at the fetal-maternal RT interface: implications in normal and pathological human pregnancy."; RL Biol. Reprod. 88:22-22(2013). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION. RX PubMed=23817958; DOI=10.1002/eji.201343335; RA Gieseke F., Kruchen A., Tzaribachev N., Bentzien F., Dominici M., RA Muller I.; RT "Proinflammatory stimuli induce galectin-9 in human mesenchymal stromal RT cells to suppress T-cell proliferation."; RL Eur. J. Immunol. 43:2741-2749(2013). RN [17] RP FUNCTION. RX PubMed=23408620; DOI=10.1128/jvi.01085-12; RA Golden-Mason L., McMahan R.H., Strong M., Reisdorph R., Mahaffey S., RA Palmer B.E., Cheng L., Kulesza C., Hirashima M., Niki T., Rosen H.R.; RT "Galectin-9 functionally impairs natural killer cells in humans and mice."; RL J. Virol. 87:4835-4845(2013). RN [18] RP INDUCTION. RX PubMed=24786365; DOI=10.1089/aid.2014.0004; RA Tandon R., Chew G.M., Byron M.M., Borrow P., Niki T., Hirashima M., RA Barbour J.D., Norris P.J., Lanteri M.C., Martin J.N., Deeks S.G., RA Ndhlovu L.C.; RT "Galectin-9 is rapidly released during acute HIV-1 infection and remains RT sustained at high levels despite viral suppression even in elite RT controllers."; RL AIDS Res. Hum. Retroviruses 30:654-664(2014). RN [19] RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND ALTERNATIVE RP SPLICING (ISOFORMS 1; 2; 3; 4 AND 5). RX PubMed=24333696; DOI=10.1016/j.bbadis.2013.12.003; RA Heusschen R., Schulkens I.A., van Beijnum J., Griffioen A.W., RA Thijssen V.L.; RT "Endothelial LGALS9 splice variant expression in endothelial cell biology RT and angiogenesis."; RL Biochim. Biophys. Acta 1842:284-292(2014). RN [20] RP FUNCTION. RX PubMed=24465902; DOI=10.1371/journal.pone.0086106; RA Kojima R., Ohno T., Iikura M., Niki T., Hirashima M., Iwaya K., Tsuda H., RA Nonoyama S., Matsuda A., Saito H., Matsumoto K., Nakae S.; RT "Galectin-9 enhances cytokine secretion, but suppresses survival and RT degranulation, in human mast cell line."; RL PLoS ONE 9:E86106-E86106(2014). RN [21] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=25578313; DOI=10.1038/cmi.2014.126; RA Li Y.H., Zhou W.H., Tao Y., Wang S.C., Jiang Y.L., Zhang D., Piao H.L., RA Fu Q., Li D.J., Du M.R.; RT "The Galectin-9/Tim-3 pathway is involved in the regulation of NK cell RT function at the maternal-fetal interface in early pregnancy."; RL Cell. Mol. Immunol. 13:73-81(2016). RN [22] RP FUNCTION, AND INDUCTION. RX PubMed=25754930; DOI=10.1111/jcmm.12500; RA Hsu Y.L., Wang M.Y., Ho L.J., Huang C.Y., Lai J.H.; RT "Up-regulation of galectin-9 induces cell migration in human dendritic RT cells infected with dengue virus."; RL J. Cell. Mol. Med. 19:1065-1076(2015). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH LACTOSE RP AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE SPECIFICITY, AND RP FUNCTION. RX PubMed=18005988; DOI=10.1016/j.jmb.2007.09.060; RA Nagae M., Nishi N., Nakamura-Tsuruta S., Hirabayashi J., Wakatsuki S., RA Kato R.; RT "Structural analysis of the human galectin-9 N-terminal carbohydrate RT recognition domain reveals unexpected properties that differ from the mouse RT orthologue."; RL J. Mol. Biol. 375:119-135(2008). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) OF 1-150 IN COMPLEX WITH RP L-ACETYLLACTOSAMINE. RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of N-terminal domain of human galectin-9 containing L- RT acetyllactosamine."; RL Submitted (APR-2008) to the PDB data bank. RN [25] RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1-148 IN COMPLEXES WITH RP N-ACETYLLACTOSAMINE OLIGOMERS, AND FUNCTION. RX PubMed=18977853; DOI=10.1093/glycob/cwn121; RA Nagae M., Nishi N., Murata T., Usui T., Nakamura T., Wakatsuki S., Kato R.; RT "Structural analysis of the recognition mechanism of poly-N- RT acetyllactosamine by the human galectin-9 N-terminal carbohydrate RT recognition domain."; RL Glycobiology 19:112-117(2009). RN [26] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 186-323 IN COMPLEXES WITH RP OLIGOSACCHARIDES. RX PubMed=20861009; DOI=10.1074/jbc.m110.163402; RA Yoshida H., Teraoka M., Nishi N., Nakakita S., Nakamura T., Hirashima M., RA Kamitori S.; RT "X-ray structures of human galectin-9 C-terminal domain in complexes with a RT biantennary oligosaccharide and sialyllactose."; RL J. Biol. Chem. 285:36969-36976(2010). CC -!- FUNCTION: Binds galactosides (PubMed:18005988). Has high affinity for CC the Forssman pentasaccharide (PubMed:18005988). Ligand for HAVCR2/TIM3 CC (PubMed:16286920). Binding to HAVCR2 induces T-helper type 1 lymphocyte CC (Th1) death (PubMed:16286920). Also stimulates bactericidal activity in CC infected macrophages by causing macrophage activation and IL1B CC secretion which restricts intracellular bacterial growth (By CC similarity). Ligand for P4HB; the interaction retains P4HB at the cell CC surface of Th2 T-helper cells, increasing disulfide reductase activity CC at the plasma membrane, altering the plasma membrane redox state and CC enhancing cell migration (PubMed:21670307). Ligand for CD44; the CC interaction enhances binding of SMAD3 to the FOXP3 promoter, leading to CC up-regulation of FOXP3 expression and increased induced regulatory T CC (iTreg) cell stability and suppressive function (By similarity). CC Promotes ability of mesenchymal stromal cells to suppress T-cell CC proliferation (PubMed:23817958). Expands regulatory T-cells and induces CC cytotoxic T-cell apoptosis following virus infection (PubMed:20209097). CC Activates ERK1/2 phosphorylation inducing cytokine (IL-6, IL-8, IL-12) CC and chemokine (CCL2) production in mast and dendritic cells CC (PubMed:24465902, PubMed:16116184). Inhibits degranulation and induces CC apoptosis of mast cells (PubMed:24465902). Induces maturation and CC migration of dendritic cells (PubMed:25754930, PubMed:16116184). CC Inhibits natural killer (NK) cell function (PubMed:23408620). Can CC transform NK cell phenotype from peripheral to decidual during CC pregnancy (PubMed:25578313). Astrocyte derived galectin-9 enhances CC microglial TNF production (By similarity). May play a role in CC thymocyte-epithelial interactions relevant to the biology of the CC thymus. May provide the molecular basis for urate flux across cell CC membranes, allowing urate that is formed during purine metabolism to CC efflux from cells and serving as an electrogenic transporter that plays CC an important role in renal and gastrointestinal urate excretion (By CC similarity). Highly selective to the anion urate (By similarity). CC {ECO:0000250|UniProtKB:O08573, ECO:0000250|UniProtKB:P97840, CC ECO:0000269|PubMed:16116184, ECO:0000269|PubMed:16286920, CC ECO:0000269|PubMed:18005988, ECO:0000269|PubMed:18977853, CC ECO:0000269|PubMed:20209097, ECO:0000269|PubMed:21670307, CC ECO:0000269|PubMed:23408620, ECO:0000269|PubMed:23817958, CC ECO:0000269|PubMed:24465902, ECO:0000269|PubMed:25578313, CC ECO:0000269|PubMed:25754930}. CC -!- FUNCTION: [Isoform 2]: Acts as an eosinophil chemoattractant CC (PubMed:9642261). It also inhibits angiogenesis (PubMed:24333696). CC Suppresses IFNG production by natural killer cells (By similarity). CC {ECO:0000250|UniProtKB:O08573, ECO:0000269|PubMed:24333696, CC ECO:0000269|PubMed:9642261}. CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:18005988, ECO:0000305|Ref.24}. CC -!- INTERACTION: CC O00182-2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-12130578, EBI-724310; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23242525}. Nucleus CC {ECO:0000269|PubMed:23242525}. Secreted {ECO:0000269|PubMed:23817958, CC ECO:0000269|PubMed:25578313}. Note=May also be secreted by a non- CC classical secretory pathway (By similarity). Secreted by mesenchymal CC stromal cells upon IFNG stimulation (PubMed:23817958). CC {ECO:0000250|UniProtKB:O08573, ECO:0000269|PubMed:23817958}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted CC {ECO:0000269|PubMed:24333696}. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Secreted CC {ECO:0000269|PubMed:24333696}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=Long, Gal-9FL {ECO:0000303|PubMed:24333696}; CC IsoId=O00182-1; Sequence=Displayed; CC Name=2; Synonyms=Medium, Gal-9delta5 {ECO:0000303|PubMed:24333696}, D5 CC {ECO:0000303|PubMed:23242525}; CC IsoId=O00182-2; Sequence=VSP_003096; CC Name=3; Synonyms=Short, Gal-9delta5/6 {ECO:0000303|PubMed:24333696}, CC D5/6 {ECO:0000303|PubMed:23242525}; CC IsoId=O00182-3; Sequence=VSP_003096, VSP_057842; CC Name=4; Synonyms=Gal-9delta5/10 {ECO:0000303|PubMed:24333696}, D5/10 CC {ECO:0000303|PubMed:23242525}; CC IsoId=O00182-4; Sequence=VSP_003096, VSP_057843; CC Name=5; Synonyms=Gal-9delta5/6/10 {ECO:0000303|PubMed:24333696}, CC D5/6/10 {ECO:0000303|PubMed:23242525}; CC IsoId=O00182-5; Sequence=VSP_003096, VSP_057842, VSP_057843; CC Name=6; Synonyms=D6 {ECO:0000303|PubMed:23242525}; CC IsoId=O00182-6; Sequence=VSP_057842; CC -!- TISSUE SPECIFICITY: Peripheral blood leukocytes and lymphatic tissues. CC Expressed in lung, liver, breast and kidney with higher levels in tumor CC endothelial cells than normal endothelium (at protein level) CC (PubMed:24333696). Expressed in trophoblast cells in decidua and CC placenta in pregnancy (at protein level) (PubMed:23242525, CC PubMed:25578313). Isoform 2 is the most abundant isoform expressed in CC endothelial cells (PubMed:24333696). Upon endothelial cell activation CC isoform 2 expression decreases while expression of isoform 3 and CC isoform 5 increases (PubMed:24333696). Isoform 4 decreases in CC pathological pregnancy (PubMed:23242525). {ECO:0000269|PubMed:23242525, CC ECO:0000269|PubMed:24333696, ECO:0000269|PubMed:25578313}. CC -!- INDUCTION: By toll-like receptor ligands zymosan (TLR2 ligand), CC polyinosinic:polycytidylic acid (poly I:C) (TLR3 ligand) and CC lipopolysaccharides (LPS) (TLR4 ligand) and by pro-inflammatory CC cytokines IFNG, TNFA, IL1A and IL1B in mesenchymal stromal cells CC (PubMed:23817958). By IFNG in macrophages (PubMed:20209097). Up- CC regulated in dendritic cells following infection with dengue virus CC (PubMed:25754930). Up-regulated in Kupffer cells following infection CC with hepatitis C virus (PubMed:20209097). Up-regulated in plasma CC following infection with HIV-1 (PubMed:24786365). CC {ECO:0000269|PubMed:20209097, ECO:0000269|PubMed:23817958, CC ECO:0000269|PubMed:24786365, ECO:0000269|PubMed:25754930}. CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding CC domains. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding; CC Note=Galectin-9; CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00120"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z49107; CAA88922.1; -; mRNA. DR EMBL; AB006782; BAA22166.1; -; mRNA. DR EMBL; AB005894; BAA31542.1; -; mRNA. DR EMBL; AB003517; BAF76327.1; -; mRNA. DR EMBL; AB008492; BAF76328.1; -; mRNA. DR EMBL; AB040130; BAB83623.1; -; Genomic_DNA. DR EMBL; AB040130; BAB83625.1; -; Genomic_DNA. DR EMBL; AB040130; BAB83624.1; -; Genomic_DNA. DR EMBL; AJ288083; CAB93851.1; -; Genomic_DNA. DR EMBL; AJ288084; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288085; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288086; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288087; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288088; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288089; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AJ288090; CAB93851.1; JOINED; Genomic_DNA. DR EMBL; AK223232; BAD96952.1; -; mRNA. DR EMBL; AC015688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471159; EAW51037.1; -; Genomic_DNA. DR EMBL; CH471159; EAW51038.1; -; Genomic_DNA. DR EMBL; CH471159; EAW51039.1; -; Genomic_DNA. DR EMBL; CH471159; EAW51044.1; -; Genomic_DNA. DR EMBL; BC105942; AAI05943.1; -; mRNA. DR EMBL; BC105944; AAI05945.1; -; mRNA. DR EMBL; BC110340; AAI10341.1; -; mRNA. DR CCDS; CCDS11222.1; -. [O00182-1] DR CCDS; CCDS32592.1; -. [O00182-2] DR CCDS; CCDS82093.1; -. [O00182-4] DR RefSeq; NP_001317092.1; NM_001330163.1. [O00182-4] DR RefSeq; NP_002299.2; NM_002308.3. [O00182-2] DR RefSeq; NP_033665.1; NM_009587.2. [O00182-1] DR RefSeq; XP_006721955.1; XM_006721892.2. [O00182-3] DR RefSeq; XP_006721958.1; XM_006721895.3. [O00182-5] DR RefSeq; XP_016880112.1; XM_017024623.1. DR PDB; 2EAK; X-ray; 1.97 A; A/B/C=1-148. DR PDB; 2EAL; X-ray; 1.85 A; A/B=1-148. DR PDB; 2YY1; X-ray; 2.17 A; A=1-147. DR PDB; 2ZHK; X-ray; 1.80 A; A/B=1-148. DR PDB; 2ZHL; X-ray; 1.75 A; A/B/C/D=1-148. DR PDB; 2ZHM; X-ray; 1.84 A; A/B/C/D=1-148. DR PDB; 2ZHN; X-ray; 1.30 A; A=1-148. DR PDB; 3LSD; X-ray; 2.03 A; A=6-148. DR PDB; 3LSE; X-ray; 2.69 A; A=6-148. DR PDB; 3NV1; X-ray; 1.50 A; A=218-355. DR PDB; 3NV2; X-ray; 2.34 A; A=218-355. DR PDB; 3NV3; X-ray; 1.57 A; A=218-355. DR PDB; 3NV4; X-ray; 1.99 A; A=218-355. DR PDB; 3WLU; X-ray; 1.40 A; A/B/C/D=5-148. DR PDB; 3WV6; X-ray; 1.95 A; A/B=1-355. DR PDBsum; 2EAK; -. DR PDBsum; 2EAL; -. DR PDBsum; 2YY1; -. DR PDBsum; 2ZHK; -. DR PDBsum; 2ZHL; -. DR PDBsum; 2ZHM; -. DR PDBsum; 2ZHN; -. DR PDBsum; 3LSD; -. DR PDBsum; 3LSE; -. DR PDBsum; 3NV1; -. DR PDBsum; 3NV2; -. DR PDBsum; 3NV3; -. DR PDBsum; 3NV4; -. DR PDBsum; 3WLU; -. DR PDBsum; 3WV6; -. DR AlphaFoldDB; O00182; -. DR SMR; O00182; -. DR BioGRID; 110156; 591. DR IntAct; O00182; 79. DR MINT; O00182; -. DR STRING; 9606.ENSP00000378856; -. DR BindingDB; O00182; -. DR ChEMBL; CHEMBL5474; -. DR DrugBank; DB04472; (R)-1-Para-Nitro-Phenyl-2-Azido-Ethanol. DR DrugCentral; O00182; -. DR UniLectin; O00182; -. DR iPTMnet; O00182; -. DR PhosphoSitePlus; O00182; -. DR BioMuta; LGALS9; -. DR EPD; O00182; -. DR jPOST; O00182; -. DR MassIVE; O00182; -. DR MaxQB; O00182; -. DR PaxDb; 9606-ENSP00000378856; -. DR PeptideAtlas; O00182; -. DR ProteomicsDB; 30394; -. DR ProteomicsDB; 47764; -. [O00182-1] DR ProteomicsDB; 47765; -. [O00182-2] DR ProteomicsDB; 75191; -. DR Antibodypedia; 26196; 727 antibodies from 40 providers. DR CPTC; O00182; 1 antibody. DR DNASU; 3965; -. DR Ensembl; ENST00000302228.9; ENSP00000306228.5; ENSG00000168961.17. [O00182-2] DR Ensembl; ENST00000313648.10; ENSP00000318214.6; ENSG00000168961.17. [O00182-4] DR Ensembl; ENST00000395473.7; ENSP00000378856.2; ENSG00000168961.17. [O00182-1] DR GeneID; 3965; -. DR KEGG; hsa:3965; -. DR MANE-Select; ENST00000395473.7; ENSP00000378856.2; NM_009587.3; NP_033665.1. DR UCSC; uc002gzp.4; human. [O00182-1] DR UCSC; uc060cvd.1; human. DR AGR; HGNC:6570; -. DR CTD; 3965; -. DR DisGeNET; 3965; -. DR GeneCards; LGALS9; -. DR HGNC; HGNC:6570; LGALS9. DR HPA; ENSG00000168961; Tissue enhanced (intestine, stomach). DR MIM; 601879; gene. DR neXtProt; NX_O00182; -. DR OpenTargets; ENSG00000168961; -. DR PharmGKB; PA30347; -. DR VEuPathDB; HostDB:ENSG00000168961; -. DR eggNOG; KOG3587; Eukaryota. DR GeneTree; ENSGT00940000162701; -. DR HOGENOM; CLU_037794_1_0_1; -. DR InParanoid; O00182; -. DR OMA; HCRELWL; -. DR OrthoDB; 4125409at2759; -. DR PhylomeDB; O00182; -. DR TreeFam; TF315551; -. DR PathwayCommons; O00182; -. DR Reactome; R-HSA-451927; Interleukin-2 family signaling. DR SignaLink; O00182; -. DR BioGRID-ORCS; 3965; 136 hits in 1150 CRISPR screens. DR ChiTaRS; LGALS9; human. DR EvolutionaryTrace; O00182; -. DR GeneWiki; LGALS9; -. DR GenomeRNAi; 3965; -. DR Pharos; O00182; Tchem. DR PRO; PR:O00182; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O00182; Protein. DR Bgee; ENSG00000168961; Expressed in monocyte and 176 other cell types or tissues. DR ExpressionAtlas; O00182; baseline and differential. DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB. DR GO; GO:0048030; F:disaccharide binding; IMP:UniProtKB. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0005534; F:galactose binding; TAS:ProtInc. DR GO; GO:0016936; F:galactoside binding; IBA:GO_Central. DR GO; GO:0071346; P:cellular response to type II interferon; IDA:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB. DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW. DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IDA:UniProtKB. DR GO; GO:0007565; P:female pregnancy; IDA:UniProtKB. DR GO; GO:0006954; P:inflammatory response; IDA:UniProtKB. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:UniProtKB. DR GO; GO:0002519; P:natural killer cell tolerance induction; IMP:UniProtKB. DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB. DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB. DR GO; GO:0032682; P:negative regulation of chemokine production; IMP:UniProtKB. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB. DR GO; GO:0043305; P:negative regulation of mast cell degranulation; IMP:UniProtKB. DR GO; GO:0045953; P:negative regulation of natural killer cell mediated cytotoxicity; IDA:UniProtKB. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB. DR GO; GO:0032689; P:negative regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0038066; P:p38MAPK cascade; IDA:UniProtKB. DR GO; GO:0070241; P:positive regulation of activated T cell autonomous cell death; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; IDA:UniProtKB. DR GO; GO:0032834; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response; IDA:UniProtKB. DR GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:2000670; P:positive regulation of dendritic cell apoptotic process; IDA:UniProtKB. DR GO; GO:2000510; P:positive regulation of dendritic cell chemotaxis; IMP:UniProtKB. DR GO; GO:2001200; P:positive regulation of dendritic cell differentiation; IMP:UniProtKB. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB. DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IDA:UniProtKB. DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:UniProtKB. DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IMP:UniProtKB. DR GO; GO:0032736; P:positive regulation of interleukin-13 production; IDA:UniProtKB. DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IDA:UniProtKB. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:UniProtKB. DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IMP:UniProtKB. DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:UniProtKB. DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IMP:UniProtKB. DR 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. DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:UniProtKB. DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:UniProtKB. DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB. DR GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB. DR GO; GO:0070555; P:response to interleukin-1; IDA:UniProtKB. DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:UniProtKB. DR CDD; cd00070; GLECT; 2. DR Gene3D; 2.60.120.200; -; 2. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR044156; Galectin-like. DR InterPro; IPR001079; Galectin_CRD. DR PANTHER; PTHR11346; GALECTIN; 1. DR PANTHER; PTHR11346:SF170; GALECTIN-9; 1. DR Pfam; PF00337; Gal-bind_lectin; 2. DR SMART; SM00908; Gal-bind_lectin; 2. DR SMART; SM00276; GLECT; 2. DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2. DR PROSITE; PS51304; GALECTIN; 2. DR Genevisible; O00182; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chemotaxis; Cytoplasm; Immunity; KW Lectin; Nucleus; Reference proteome; Repeat; Secreted. FT CHAIN 1..355 FT /note="Galectin-9" FT /id="PRO_0000076946" FT DOMAIN 17..148 FT /note="Galectin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639" FT DOMAIN 227..355 FT /note="Galectin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639" FT BINDING 48 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="1" FT BINDING 61 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="1" FT BINDING 65 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="1" FT BINDING 75 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="1" FT BINDING 82..88 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="1" FT BINDING 267 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="2" FT BINDING 271 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="2" FT BINDING 281 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 287..293 FT /ligand="a beta-D-galactoside" FT /ligand_id="ChEBI:CHEBI:28034" FT /ligand_label="2" FT /evidence="ECO:0000250" FT VAR_SEQ 149..180 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000269|PubMed:24333696, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9045665, FT ECO:0000303|PubMed:9642261, ECO:0000303|Ref.4, FT ECO:0000303|Ref.7" FT /id="VSP_003096" FT VAR_SEQ 181..192 FT /note="Missing (in isoform 3, isoform 5 and isoform 6)" FT /evidence="ECO:0000269|PubMed:23242525, FT ECO:0000269|PubMed:24333696" FT /id="VSP_057842" FT VAR_SEQ 254..355 FT /note="FHINLCSGNHIAFHLNPRFDENAVVRNTQIDNSWGSEERSLPRKMPFVRGQS FT FSVWILCEAHCLKVAVDGQHLFEYYHRLRNLPTINRLEVGGDIQLTHVQT -> CGSCV FT KLTASRWPWMVSTCLNTTIA (in isoform 4 and isoform 5)" FT /evidence="ECO:0000269|PubMed:24333696" FT /id="VSP_057843" FT VARIANT 5 FT /note="G -> S (in dbSNP:rs3751093)" FT /evidence="ECO:0000269|PubMed:9642261, ECO:0000269|Ref.7" FT /id="VAR_020453" FT CONFLICT 48 FT /note="N -> D (in Ref. 6; CAB93851)" FT /evidence="ECO:0000305" FT CONFLICT 79..81 FT /note="NGS -> KGR (in Ref. 6; CAB93851)" FT /evidence="ECO:0000305" FT CONFLICT 88 FT /note="K -> R (in Ref. 1; CAA88922)" FT /evidence="ECO:0000305" FT CONFLICT 89 FT /note="T -> M (in Ref. 6; CAB93851)" FT /evidence="ECO:0000305" FT CONFLICT 93 FT /note="F -> S (in Ref. 7; BAD96952)" FT /evidence="ECO:0000305" FT CONFLICT 135 FT /note="S -> F (in Ref. 1; CAA88922)" FT /evidence="ECO:0000305" FT CONFLICT 270 FT /note="P -> L (in Ref. 1; CAA88922)" FT /evidence="ECO:0000305" FT CONFLICT 313 FT /note="E -> G (in Ref. 1; CAA88922)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="L -> V (in Ref. 6; CAB93851)" FT /evidence="ECO:0000305" FT CONFLICT 341 FT /note="R -> K (in Ref. 6; CAB93851)" FT /evidence="ECO:0000305" FT STRAND 5..7 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 15..20 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 30..37 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 39..41 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 43..56 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 58..65 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 71..78 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 86..89 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 98..105 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 107..114 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 117..123 FT /evidence="ECO:0007829|PDB:2ZHN" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 133..146 FT /evidence="ECO:0007829|PDB:2ZHN" FT STRAND 225..230 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 240..247 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 253..260 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 263..271 FT /evidence="ECO:0007829|PDB:3NV1" FT TURN 272..275 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 276..283 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 305..312 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 314..321 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 324..330 FT /evidence="ECO:0007829|PDB:3NV1" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:3NV1" FT STRAND 341..354 FT /evidence="ECO:0007829|PDB:3NV1" SQ 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 //