LEG8_RAT
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 03-AUG-2022, entry version 118.
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 PaxDb; Q62665; -.
DR UCSC; RGD:621272; rat.
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 InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR030638; Galectin_8.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF22; PTHR11346:SF22; 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 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