ID   LEG8_RAT                Reviewed;         316 AA.
AC   Q62665;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 123.
DE   RecName: Full=Galectin-8;
DE            Short=Gal-8;
DE   AltName: Full=30 kDa S-type lectin;
DE   AltName: Full=RL-30;
GN   Name=Lgals8;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley; TISSUE=Liver;
RX   PubMed=7852431; DOI=10.1074/jbc.270.7.3447;
RA   Hadari Y.R., Paz K., Dekel R., Mestrovic T., Accili D., Zick Y.;
RT   "Galectin-8. A new rat lectin, related to galectin-4.";
RL   J. Biol. Chem. 270:3447-3453(1995).
CC   -!- FUNCTION: Beta-galactoside-binding lectin that acts as a sensor of
CC       membrane damage caused by infection and restricts the proliferation of
CC       infecting pathogens by targeting them for autophagy. Detects membrane
CC       rupture by binding beta-galactoside ligands located on the lumenal side
CC       of the endosome membrane; these ligands becoming exposed to the
CC       cytoplasm following rupture. Restricts infection by initiating
CC       autophagy via interaction with CALCOCO2/NDP52. Required to restrict
CC       infection of bacterial invasion such as S.typhimurium. Also required to
CC       restrict infection of Picornaviridae viruses. Has a marked preference
CC       for 3'-O-sialylated and 3'-O-sulfated glycans.
CC       {ECO:0000250|UniProtKB:O00214}.
CC   -!- SUBUNIT: Homodimer. Interacts with CALCOCO2/NDP52. Interacts with PDPN;
CC       the interaction is glycosylation-dependent; may participate in
CC       connection of the lymphatic endothelium to the surrounding
CC       extracellular matrix. {ECO:0000250|UniProtKB:O00214}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC       {ECO:0000250|UniProtKB:O00214}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:O00214}.
CC   -!- TISSUE SPECIFICITY: Expressed in liver, kidney, cardiac muscle, lung,
CC       and brain.
CC   -!- DEVELOPMENTAL STAGE: Very low levels in whole embryos, high levels in
CC       adult tissues.
CC   -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC       domains.
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DR   EMBL; U09824; AAA66359.1; -; mRNA.
DR   PIR; A55975; A55975.
DR   AlphaFoldDB; Q62665; -.
DR   SMR; Q62665; -.
DR   STRING; 10116.ENSRNOP00000040412; -.
DR   PhosphoSitePlus; Q62665; -.
DR   PaxDb; 10116-ENSRNOP00000040412; -.
DR   UCSC; RGD:621272; rat.
DR   AGR; RGD:621272; -.
DR   RGD; 621272; Lgals8.
DR   eggNOG; KOG3587; Eukaryota.
DR   InParanoid; Q62665; -.
DR   PhylomeDB; Q62665; -.
DR   PRO; PR:Q62665; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISS:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; ISS:GO_Central.
DR   GO; GO:0005178; F:integrin binding; ISO:RGD.
DR   GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB.
DR   GO; GO:1904977; P:lymphatic endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0002317; P:plasma cell differentiation; ISO:RGD.
DR   GO; GO:0031295; P:T cell costimulation; ISO:RGD.
DR   GO; GO:0098792; P:xenophagy; ISS:GO_Central.
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:SF147; GALECTIN; 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.
PE   2: Evidence at transcript level;
KW   Autophagy; Cytoplasm; Cytoplasmic vesicle; Lectin; Reference proteome;
KW   Repeat.
FT   CHAIN           1..316
FT                   /note="Galectin-8"
FT                   /id="PRO_0000076945"
FT   DOMAIN          18..151
FT                   /note="Galectin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   DOMAIN          186..316
FT                   /note="Galectin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT   BINDING         68
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:O00214"
FT   BINDING         78
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:O00214"
FT   BINDING         88
FT                   /ligand="a carbohydrate"
FT                   /ligand_id="ChEBI:CHEBI:16646"
FT                   /evidence="ECO:0000250|UniProtKB:O00214"
FT   BINDING         248..254
FT                   /ligand="a beta-D-galactoside"
FT                   /ligand_id="ChEBI:CHEBI:28034"
FT                   /evidence="ECO:0000250"
FT   SITE            58
FT                   /note="Critical for binding to sialylated and sulfated
FT                   oligosaccharides"
FT                   /evidence="ECO:0000250|UniProtKB:O00214"
SQ   SEQUENCE   316 AA;  36038 MW;  C04B766CFE913D59 CRC64;
     MLSLSNLQNI IYNPTIPYVS TITEQLKPGS LIVIRGHVPK DSERFQVDFQ HGNSLKPRAD
     VAFHFNPRFK RSNCIVCNTL TNEKWGWEEI THDMPFRKEK SFEIVIMVLK NKFHVAVNGK
     HILLYAHRIN PEKIDTLGIF GKVNIHSIGF RFSSDLQSME TSTLGLTQIS KENIQKSGKL
     HLSLPFEARL NASMGPGRTV VVKGEVNTNA TSFNVDLVAG RSRDIALHLN PRLNVKAFVR
     NSFLQDAWGE EERNITCFPF SSGMYFEMII YCDVREFKVA VNGVHSLEYK HRFKDLSSID
     TLAVDGDIRL LDVRSW
//