Full text data of LGALS9
LGALS9
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Galectin-9; Gal-9 (Ecalectin; Tumor antigen HOM-HD-21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Galectin-9; Gal-9 (Ecalectin; Tumor antigen HOM-HD-21)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00010477
IPI00010477 Splice isoform Long of O00182 Galectin-9 Splice isoform Long of O00182 Galectin-9 membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a extracellular splice isoform Long or Short found at its expected molecular weight found at molecular weight
IPI00010477 Splice isoform Long of O00182 Galectin-9 Splice isoform Long of O00182 Galectin-9 membrane n/a n/a n/a n/a n/a n/a n/a n/a 2 n/a n/a n/a n/a n/a n/a n/a n/a 1 n/a n/a extracellular splice isoform Long or Short found at its expected molecular weight found at molecular weight
UniProt
O00182
ID LEG9_HUMAN Reviewed; 355 AA.
AC O00182; A7VJG6; O14532; O75028; Q3B8N1; Q53FQ0; Q9NQ58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
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
RT in patients with Hodgkin's disease.";
RL J. Biol. Chem. 272:6416-6422(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Gastric carcinoma;
RA Kato S.;
RT "Human galectin-9 isoform full-length cDNA from gastric
RT adenocarcinoma.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), 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 LONG AND SHORT).
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].
RA Akiyama S.;
RT "Homo sapiens galectin-9 (LGALS9) / ecalectin gene, exon 2 through
RT 11.";
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 SHORT), AND VARIANT
RP 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH
RP LACTOSE AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE
RP SPECIFICITY, AND 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
RT mouse orthologue.";
RL J. Mol. Biol. 375:119-135(2008).
RN [12]
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
RT L-acetyllactosamine.";
RL Submitted (APR-2008) to the PDB data bank.
RN [13]
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.,
RA 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 [14]
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.,
RA Hirashima M., Kamitori S.;
RT "X-ray structures of human galectin-9 C-terminal domain in complexes
RT with a biantennary oligosaccharide and sialyllactose.";
RL J. Biol. Chem. 285:36969-36976(2010).
CC -!- FUNCTION: Binds galactosides. Has high affinity for the Forssman
CC pentasaccharide. May play a role in thymocyte-epithelial
CC interactions relevant to the biology of the thymus. Inhibits cell
CC proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper
CC type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil
CC chemoattractant.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By
CC similarity). Note=May also be secreted by a non-classical
CC secretory pathway (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=Long;
CC IsoId=O00182-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00182-2; Sequence=VSP_003096;
CC -!- TISSUE SPECIFICITY: Peripheral blood leukocytes and lymphatic
CC tissues. Overexpressed in Hodgkin disease tissue.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- SIMILARITY: Contains 2 galectin 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; 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; CH471159; EAW51037.1; -; 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 RefSeq; NP_002299.2; NM_002308.3.
DR RefSeq; NP_033665.1; NM_009587.2.
DR UniGene; Hs.81337; -.
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 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 ProteinModelPortal; O00182; -.
DR SMR; O00182; 3-355.
DR IntAct; O00182; 12.
DR STRING; 9606.ENSP00000378856; -.
DR BindingDB; O00182; -.
DR ChEMBL; CHEMBL5474; -.
DR PhosphoSite; O00182; -.
DR PRIDE; O00182; -.
DR Ensembl; ENST00000302228; ENSP00000306228; ENSG00000168961.
DR Ensembl; ENST00000395473; ENSP00000378856; ENSG00000168961.
DR GeneID; 3965; -.
DR KEGG; hsa:3965; -.
DR UCSC; uc002gzp.3; human.
DR CTD; 3965; -.
DR GeneCards; GC17P025956; -.
DR HGNC; HGNC:6570; LGALS9.
DR MIM; 601879; gene.
DR neXtProt; NX_O00182; -.
DR PharmGKB; PA30347; -.
DR HOGENOM; HOG000290194; -.
DR HOVERGEN; HBG002412; -.
DR InParanoid; O00182; -.
DR KO; K10093; -.
DR OMA; VCNTRQN; -.
DR OrthoDB; EOG73Z2TM; -.
DR PhylomeDB; O00182; -.
DR ChiTaRS; lgals9; human.
DR EvolutionaryTrace; O00182; -.
DR GeneWiki; LGALS9; -.
DR GenomeRNAi; 3965; -.
DR NextBio; 15562; -.
DR PRO; PR:O00182; -.
DR ArrayExpress; O00182; -.
DR Bgee; O00182; -.
DR CleanEx; HS_LGALS9; -.
DR Genevestigator; O00182; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005534; F:galactose binding; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Lectin; Polymorphism; Reference proteome; Repeat; Secreted.
FT CHAIN 1 355 Galectin-9.
FT /FTId=PRO_0000076946.
FT DOMAIN 17 148 Galectin 1.
FT DOMAIN 227 355 Galectin 2.
FT REGION 82 88 Beta-galactoside binding 1.
FT REGION 287 293 Beta-galactoside binding 2 (By
FT similarity).
FT BINDING 48 48 Beta-galactoside 1.
FT BINDING 61 61 Beta-galactoside 1.
FT BINDING 65 65 Beta-galactoside 1.
FT BINDING 75 75 Beta-galactoside 1.
FT BINDING 267 267 Beta-galactoside 2.
FT BINDING 271 271 Beta-galactoside 2.
FT BINDING 281 281 Beta-galactoside 2 (By similarity).
FT VAR_SEQ 149 180 Missing (in isoform Short).
FT /FTId=VSP_003096.
FT VARIANT 5 5 G -> S (in dbSNP:rs3751093).
FT /FTId=VAR_020453.
FT CONFLICT 48 48 N -> D (in Ref. 6; CAB93851).
FT CONFLICT 79 81 NGS -> KGR (in Ref. 6; CAB93851).
FT CONFLICT 88 88 K -> R (in Ref. 1; CAA88922).
FT CONFLICT 89 89 T -> M (in Ref. 6; CAB93851).
FT CONFLICT 93 93 F -> S (in Ref. 7; BAD96952).
FT CONFLICT 135 135 S -> F (in Ref. 1; CAA88922).
FT CONFLICT 270 270 P -> L (in Ref. 1; CAA88922).
FT CONFLICT 313 313 E -> G (in Ref. 1; CAA88922).
FT CONFLICT 326 326 L -> V (in Ref. 6; CAB93851).
FT CONFLICT 341 341 R -> K (in Ref. 6; CAB93851).
FT STRAND 5 7
FT STRAND 10 12
FT STRAND 15 20
FT STRAND 30 37
FT STRAND 39 41
FT STRAND 43 56
FT STRAND 58 65
FT STRAND 71 78
FT STRAND 86 89
FT STRAND 98 105
FT STRAND 107 114
FT STRAND 117 123
FT HELIX 128 130
FT STRAND 133 146
FT STRAND 225 230
FT STRAND 240 247
FT STRAND 253 260
FT STRAND 263 271
FT TURN 272 275
FT STRAND 276 283
FT STRAND 295 297
FT STRAND 305 312
FT STRAND 314 321
FT STRAND 324 330
FT HELIX 336 338
FT STRAND 341 354
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
//
ID LEG9_HUMAN Reviewed; 355 AA.
AC O00182; A7VJG6; O14532; O75028; Q3B8N1; Q53FQ0; Q9NQ58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 15-JUL-1998, sequence version 2.
DT 22-JAN-2014, entry version 131.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
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
RT in patients with Hodgkin's disease.";
RL J. Biol. Chem. 272:6416-6422(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RC TISSUE=Gastric carcinoma;
RA Kato S.;
RT "Human galectin-9 isoform full-length cDNA from gastric
RT adenocarcinoma.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), 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 LONG AND SHORT).
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].
RA Akiyama S.;
RT "Homo sapiens galectin-9 (LGALS9) / ecalectin gene, exon 2 through
RT 11.";
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 SHORT), AND VARIANT
RP 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
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 [11]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 1-148 IN COMPLEXES WITH
RP LACTOSE AND COMPLEX BETA-GALACTOSIDE, SUBUNIT, CARBOHYDRATE
RP SPECIFICITY, AND 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
RT mouse orthologue.";
RL J. Mol. Biol. 375:119-135(2008).
RN [12]
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
RT L-acetyllactosamine.";
RL Submitted (APR-2008) to the PDB data bank.
RN [13]
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.,
RA 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 [14]
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.,
RA Hirashima M., Kamitori S.;
RT "X-ray structures of human galectin-9 C-terminal domain in complexes
RT with a biantennary oligosaccharide and sialyllactose.";
RL J. Biol. Chem. 285:36969-36976(2010).
CC -!- FUNCTION: Binds galactosides. Has high affinity for the Forssman
CC pentasaccharide. May play a role in thymocyte-epithelial
CC interactions relevant to the biology of the thymus. Inhibits cell
CC proliferation. It is a ligand for HAVCR2/TIM3. Induces T-helper
CC type 1 lymphocyte (Th1) death. Isoform Short acts as an eosinophil
CC chemoattractant.
CC -!- SUBUNIT: Monomer (Probable).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Secreted (By
CC similarity). Note=May also be secreted by a non-classical
CC secretory pathway (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist;
CC Name=Long;
CC IsoId=O00182-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=O00182-2; Sequence=VSP_003096;
CC -!- TISSUE SPECIFICITY: Peripheral blood leukocytes and lymphatic
CC tissues. Overexpressed in Hodgkin disease tissue.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- SIMILARITY: Contains 2 galectin 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; 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; CH471159; EAW51037.1; -; 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 RefSeq; NP_002299.2; NM_002308.3.
DR RefSeq; NP_033665.1; NM_009587.2.
DR UniGene; Hs.81337; -.
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 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 ProteinModelPortal; O00182; -.
DR SMR; O00182; 3-355.
DR IntAct; O00182; 12.
DR STRING; 9606.ENSP00000378856; -.
DR BindingDB; O00182; -.
DR ChEMBL; CHEMBL5474; -.
DR PhosphoSite; O00182; -.
DR PRIDE; O00182; -.
DR Ensembl; ENST00000302228; ENSP00000306228; ENSG00000168961.
DR Ensembl; ENST00000395473; ENSP00000378856; ENSG00000168961.
DR GeneID; 3965; -.
DR KEGG; hsa:3965; -.
DR UCSC; uc002gzp.3; human.
DR CTD; 3965; -.
DR GeneCards; GC17P025956; -.
DR HGNC; HGNC:6570; LGALS9.
DR MIM; 601879; gene.
DR neXtProt; NX_O00182; -.
DR PharmGKB; PA30347; -.
DR HOGENOM; HOG000290194; -.
DR HOVERGEN; HBG002412; -.
DR InParanoid; O00182; -.
DR KO; K10093; -.
DR OMA; VCNTRQN; -.
DR OrthoDB; EOG73Z2TM; -.
DR PhylomeDB; O00182; -.
DR ChiTaRS; lgals9; human.
DR EvolutionaryTrace; O00182; -.
DR GeneWiki; LGALS9; -.
DR GenomeRNAi; 3965; -.
DR NextBio; 15562; -.
DR PRO; PR:O00182; -.
DR ArrayExpress; O00182; -.
DR Bgee; O00182; -.
DR CleanEx; HS_LGALS9; -.
DR Genevestigator; O00182; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005534; F:galactose binding; TAS:ProtInc.
DR GO; GO:0004871; F:signal transducer activity; IMP:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Lectin; Polymorphism; Reference proteome; Repeat; Secreted.
FT CHAIN 1 355 Galectin-9.
FT /FTId=PRO_0000076946.
FT DOMAIN 17 148 Galectin 1.
FT DOMAIN 227 355 Galectin 2.
FT REGION 82 88 Beta-galactoside binding 1.
FT REGION 287 293 Beta-galactoside binding 2 (By
FT similarity).
FT BINDING 48 48 Beta-galactoside 1.
FT BINDING 61 61 Beta-galactoside 1.
FT BINDING 65 65 Beta-galactoside 1.
FT BINDING 75 75 Beta-galactoside 1.
FT BINDING 267 267 Beta-galactoside 2.
FT BINDING 271 271 Beta-galactoside 2.
FT BINDING 281 281 Beta-galactoside 2 (By similarity).
FT VAR_SEQ 149 180 Missing (in isoform Short).
FT /FTId=VSP_003096.
FT VARIANT 5 5 G -> S (in dbSNP:rs3751093).
FT /FTId=VAR_020453.
FT CONFLICT 48 48 N -> D (in Ref. 6; CAB93851).
FT CONFLICT 79 81 NGS -> KGR (in Ref. 6; CAB93851).
FT CONFLICT 88 88 K -> R (in Ref. 1; CAA88922).
FT CONFLICT 89 89 T -> M (in Ref. 6; CAB93851).
FT CONFLICT 93 93 F -> S (in Ref. 7; BAD96952).
FT CONFLICT 135 135 S -> F (in Ref. 1; CAA88922).
FT CONFLICT 270 270 P -> L (in Ref. 1; CAA88922).
FT CONFLICT 313 313 E -> G (in Ref. 1; CAA88922).
FT CONFLICT 326 326 L -> V (in Ref. 6; CAB93851).
FT CONFLICT 341 341 R -> K (in Ref. 6; CAB93851).
FT STRAND 5 7
FT STRAND 10 12
FT STRAND 15 20
FT STRAND 30 37
FT STRAND 39 41
FT STRAND 43 56
FT STRAND 58 65
FT STRAND 71 78
FT STRAND 86 89
FT STRAND 98 105
FT STRAND 107 114
FT STRAND 117 123
FT HELIX 128 130
FT STRAND 133 146
FT STRAND 225 230
FT STRAND 240 247
FT STRAND 253 260
FT STRAND 263 271
FT TURN 272 275
FT STRAND 276 283
FT STRAND 295 297
FT STRAND 305 312
FT STRAND 314 321
FT STRAND 324 330
FT HELIX 336 338
FT STRAND 341 354
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
//
MIM
601879
*RECORD*
*FIELD* NO
601879
*FIELD* TI
*601879 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 9; LGALS9
;;GALECTIN 9
ECALECTIN, INCLUDED
read more*FIELD* TX
Specific interactions between carbohydrate moieties and their putative
binding proteins (i.e., lectins) play a critical role in various
developmental, physiologic, and pathologic processes. Mammalian lectins
are classified into 4 categories: C-type lectins (including selectins),
P-type lectins, pentraxins, and galectins. Wada et al. (1997) stated
that 10 mammalian galectins had been cloned, sequenced, and functionally
characterized, namely galectin-1 to -10 (see 150570). Galectin-9 was
isolated from mouse embryonic kidney and characterized by Wada and
Kanwar (1997). From studies of its expression in embryonic, newborn, and
adult mouse tissues, Wada et al. (1997) demonstrated that its expression
is widely distributed and developmentally regulated. Its expression was
accentuated in liver and thymus of embryonic mice. In postnatal mice,
antigalectin-9 immunoreactivity was observed in various tissues,
including thymic epithelial cells. Galectin-9 induced apoptosis in
thymocytes but not in hepatocytes. Wada et al. (1997) concluded that
galectin-9 plays a role in thymocyte-epithelial interactions relevant to
the biology of the thymus.
Tureci et al. (1997) used autologous serum to immunoscreen a cDNA
expression library derived from tissue involved by Hodgkin disease
(236000). They detected a 36-kD protein with the galactoside-binding
characteristics of galectins. This human galectin (designated galectin-9
by them) has a predicted length of 323 amino acids and shares sequence
similarity with other galectins.
Ecalectin is an eosinophil chemoattractant (ECA) produced by
antigen-activated T cells. Matsumoto et al. (1998) partially purified
ecalectin from the conditioned medium of a human T cell-derived cell
line. By screening a human T-cell cDNA expression library with
antibodies against ecalectin, they isolated cDNAs encoding ecalectin.
The deduced ecalectin protein has 323 amino acids. Although ecalectin is
secreted, it lacks a predicted hydrophobic signal peptide. Ecalectin is
not related to any known cytokine or chemokine but rather is related to
the galectin family of carbohydrate-binding proteins. Matsumoto et al.
(1998) stated that ecalectin and galectin-9 are likely 2 allelic
variants of the same gene because they encode deduced proteins that
differ by only a few amino acids, they have identical 5-prime
untranslated regions (UTRs), their 3-prime UTRs differ by only 1
nucleotide, and both are expressed in peripheral blood cells.
Recombinant ecalectin expressed in COS cells or insect cells exhibited
potent ECA activity and attracted eosinophils in vitro and in vivo in a
dose-dependent manner; ecalectin did not induce chemotaxis of
neutrophils, lymphocytes, or monocytes. Northern blot analysis of human
tissues detected an approximately 1.8-kb ecalectin transcript that was
expressed most abundantly in lymphoid tissues, namely spleen and
peripheral blood lymphocytes, and at lower levels in stomach, small
intestine, and lung. Ecalectin expression increased substantially in
antigen-activated peripheral blood mononuclear cells. Matsumoto et al.
(1998) suggested that ecalectin is an important T cell-derived regulator
of eosinophil recruitment in tissues during inflammatory reactions.
*FIELD* RF
1. 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.
2. Tureci, 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.
3. Wada, J.; Kanwar, Y. S.: Identification and characterization of
galectin-9, a novel beta-galactoside-binding mammalian lectin. J.
Biol. Chem. 272: 6078-6086, 1997.
4. Wada, J.; Ota, K.; Kumar, A.; Wallner, E. I.; Kanwar, Y. S.: Developmental
regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside
binding lectin. J. Clin. Invest. 99: 2452-2461, 1997.
*FIELD* CN
Patti M. Sherman - updated: 6/23/2000
*FIELD* CD
Victor A. McKusick: 6/19/1997
*FIELD* ED
mcapotos: 06/26/2000
psherman: 6/23/2000
dkim: 7/21/1998
mark: 6/25/1997
mark: 6/23/1997
jenny: 6/23/1997
alopez: 6/19/1997
*RECORD*
*FIELD* NO
601879
*FIELD* TI
*601879 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 9; LGALS9
;;GALECTIN 9
ECALECTIN, INCLUDED
read more*FIELD* TX
Specific interactions between carbohydrate moieties and their putative
binding proteins (i.e., lectins) play a critical role in various
developmental, physiologic, and pathologic processes. Mammalian lectins
are classified into 4 categories: C-type lectins (including selectins),
P-type lectins, pentraxins, and galectins. Wada et al. (1997) stated
that 10 mammalian galectins had been cloned, sequenced, and functionally
characterized, namely galectin-1 to -10 (see 150570). Galectin-9 was
isolated from mouse embryonic kidney and characterized by Wada and
Kanwar (1997). From studies of its expression in embryonic, newborn, and
adult mouse tissues, Wada et al. (1997) demonstrated that its expression
is widely distributed and developmentally regulated. Its expression was
accentuated in liver and thymus of embryonic mice. In postnatal mice,
antigalectin-9 immunoreactivity was observed in various tissues,
including thymic epithelial cells. Galectin-9 induced apoptosis in
thymocytes but not in hepatocytes. Wada et al. (1997) concluded that
galectin-9 plays a role in thymocyte-epithelial interactions relevant to
the biology of the thymus.
Tureci et al. (1997) used autologous serum to immunoscreen a cDNA
expression library derived from tissue involved by Hodgkin disease
(236000). They detected a 36-kD protein with the galactoside-binding
characteristics of galectins. This human galectin (designated galectin-9
by them) has a predicted length of 323 amino acids and shares sequence
similarity with other galectins.
Ecalectin is an eosinophil chemoattractant (ECA) produced by
antigen-activated T cells. Matsumoto et al. (1998) partially purified
ecalectin from the conditioned medium of a human T cell-derived cell
line. By screening a human T-cell cDNA expression library with
antibodies against ecalectin, they isolated cDNAs encoding ecalectin.
The deduced ecalectin protein has 323 amino acids. Although ecalectin is
secreted, it lacks a predicted hydrophobic signal peptide. Ecalectin is
not related to any known cytokine or chemokine but rather is related to
the galectin family of carbohydrate-binding proteins. Matsumoto et al.
(1998) stated that ecalectin and galectin-9 are likely 2 allelic
variants of the same gene because they encode deduced proteins that
differ by only a few amino acids, they have identical 5-prime
untranslated regions (UTRs), their 3-prime UTRs differ by only 1
nucleotide, and both are expressed in peripheral blood cells.
Recombinant ecalectin expressed in COS cells or insect cells exhibited
potent ECA activity and attracted eosinophils in vitro and in vivo in a
dose-dependent manner; ecalectin did not induce chemotaxis of
neutrophils, lymphocytes, or monocytes. Northern blot analysis of human
tissues detected an approximately 1.8-kb ecalectin transcript that was
expressed most abundantly in lymphoid tissues, namely spleen and
peripheral blood lymphocytes, and at lower levels in stomach, small
intestine, and lung. Ecalectin expression increased substantially in
antigen-activated peripheral blood mononuclear cells. Matsumoto et al.
(1998) suggested that ecalectin is an important T cell-derived regulator
of eosinophil recruitment in tissues during inflammatory reactions.
*FIELD* RF
1. 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.
2. Tureci, 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.
3. Wada, J.; Kanwar, Y. S.: Identification and characterization of
galectin-9, a novel beta-galactoside-binding mammalian lectin. J.
Biol. Chem. 272: 6078-6086, 1997.
4. Wada, J.; Ota, K.; Kumar, A.; Wallner, E. I.; Kanwar, Y. S.: Developmental
regulation, expression, and apoptotic potential of galectin-9, a beta-galactoside
binding lectin. J. Clin. Invest. 99: 2452-2461, 1997.
*FIELD* CN
Patti M. Sherman - updated: 6/23/2000
*FIELD* CD
Victor A. McKusick: 6/19/1997
*FIELD* ED
mcapotos: 06/26/2000
psherman: 6/23/2000
dkim: 7/21/1998
mark: 6/25/1997
mark: 6/23/1997
jenny: 6/23/1997
alopez: 6/19/1997