LEG9_BOVIN
ID LEG9_BOVIN Reviewed; 355 AA.
AC Q3MHZ8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Galectin-9;
DE Short=Gal-9;
GN Name=LGALS9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds galactosides. Has high affinity for the Forssman
CC pentasaccharide. Ligand for HAVCR2/TIM3. Binding to HAVCR2 induces T-
CC helper type 1 lymphocyte (Th1) death. Also stimulates bactericidal
CC activity in infected macrophages by causing macrophage activation and
CC IL1B secretion which restricts intracellular bacterial growth. Ligand
CC for P4HB; the interaction retains P4HB at the cell surface of Th2 T
CC helper cells, increasing disulfide reductase activity at the plasma
CC membrane, altering the plasma membrane redox state and enhancing cell
CC migration. Ligand for CD44; the interaction enhances binding of SMAD3
CC to the FOXP3 promoter, leading to up-regulation of FOXP3 expression and
CC increased induced regulatory T (iTreg) cell stability and suppressive
CC function. Promotes ability of mesenchymal stromal cells to suppress T-
CC cell proliferation. Expands regulatory T-cells and induces cytotoxic T-
CC cell apoptosis following virus infection. Activates ERK1/2
CC phosphorylation inducing cytokine (IL-6, IL-8, IL-12) and chemokine
CC (CCL2) production in mast and dendritic cells. Inhibits degranulation
CC and induces apoptosis of mast cells. Induces maturation and migration
CC of dendritic cells. Inhibits natural killer (NK) cell function. Can
CC transform NK cell phenotype from peripheral to decidual during
CC pregnancy. Astrocyte derived galectin-9 enhances microglial TNF
CC production. May play a role in thymocyte-epithelial interactions
CC relevant to the biology of the thymus. May provide the molecular basis
CC for urate flux across cell membranes, allowing urate that is formed
CC during purine metabolism to efflux from cells and serving as an
CC electrogenic transporter that plays an important role in renal and
CC gastrointestinal urate excretion. Highly selective to the anion urate.
CC {ECO:0000250|UniProtKB:O00182, ECO:0000250|UniProtKB:O08573,
CC ECO:0000250|UniProtKB:P97840}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O00182}. Nucleus
CC {ECO:0000250|UniProtKB:O00182}. Secreted
CC {ECO:0000250|UniProtKB:O00182}. Note=May also be secreted by a non-
CC classical secretory pathway. Secreted by mesenchymal stromal cells upon
CC IFNG stimulation. {ECO:0000250|UniProtKB:O00182,
CC ECO:0000250|UniProtKB:O08573}.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
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DR EMBL; BC104505; AAI04506.1; -; mRNA.
DR RefSeq; NP_001034266.1; NM_001039177.2.
DR AlphaFoldDB; Q3MHZ8; -.
DR SMR; Q3MHZ8; -.
DR STRING; 9913.ENSBTAP00000009025; -.
DR PaxDb; Q3MHZ8; -.
DR PRIDE; Q3MHZ8; -.
DR GeneID; 510813; -.
DR KEGG; bta:510813; -.
DR CTD; 3965; -.
DR eggNOG; KOG3587; Eukaryota.
DR InParanoid; Q3MHZ8; -.
DR OrthoDB; 829777at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; ISS:UniProtKB.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Cytoplasm; Immunity; Lectin; Nucleus; Reference proteome; Repeat; Secreted.
FT CHAIN 1..355
FT /note="Galectin-9"
FT /id="PRO_0000283031"
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 /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 65
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 75
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82..88
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 267
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 355 AA; 39334 MW; FB56142FC54747FB CRC64;
MAFGGAQASY INPVVPFTGM IQGGLQDGHK ITIIGAVLPS GGNRFAVNLQ TGYNDSDIAF
HFNPRFEEGG YVVCNTKQRG SWGTEERKMH MPFQRGCSFE LCFQVQSSDF RVMVNGNLFT
QYAHRVPFHR IDAISITGVV QLSSISFQNI RAAPKQPACS KVQFSQAVCL PPRPRGRKSN
PPGIWPANSA PIAQTFVHTI HSAPGQMFPN PVIPPAVYPN PVYQLPFFTS ILGGLYPSKS
ILVSGTILPS AQRFYINLRS GSDIAFHLNP RFNENAVVRN TQINGSWGSE ERSLPRGMPF
FRGQSFSVWI MCEGHCFKVA VDSQHLFEYH HRLKNLPAIN NLEVGGDIQL THVQT
