LEG9_HUMAN
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 03-AUG-2022, entry version 199.
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";
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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. [O00182-6]
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; 587.
DR IntAct; O00182; 78.
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; O00182; -.
DR PeptideAtlas; O00182; -.
DR PRIDE; O00182; -.
DR ProteomicsDB; 30394; -.
DR ProteomicsDB; 47764; -. [O00182-1]
DR ProteomicsDB; 47765; -. [O00182-2]
DR ProteomicsDB; 75191; -.
DR Antibodypedia; 26196; 648 antibodies from 39 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 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; VGFKVTC; -.
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 1073 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 175 other tissues.
DR ExpressionAtlas; O00182; baseline and differential.
DR Genevisible; O00182; HS.
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 interferon-gamma; 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:0032689; P:negative regulation of interferon-gamma production; 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: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: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:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; 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 NIK/NF-kappaB signaling; 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: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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR Pfam; PF00337; Gal-bind_lectin; 2.
DR SMART; SM00908; Gal-bind_lectin; 2.
DR SMART; SM00276; GLECT; 2.
DR SUPFAM; SSF49899; SSF49899; 2.
DR PROSITE; PS51304; GALECTIN; 2.
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
