LEG8_MOUSE
ID LEG8_MOUSE Reviewed; 316 AA.
AC Q9JL15;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Galectin-8;
DE Short=Gal-8;
DE AltName: Full=LGALS-8;
GN Name=Lgals8;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Maier C., Haeussler J., Roesch K., Moschgath E., Haeusler J., Vogel W.;
RT "The human Lgals-8 gene: genomic sequence and expression of the prostate
RT carcinoma tumour antigen (PCTA-1) and the Po66 carbohydrate binding
RT protein.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-8;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Stlect_203";
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DR EMBL; AF218069; AAF27645.1; -; mRNA.
DR EMBL; AK029526; BAC26495.1; -; mRNA.
DR EMBL; BC040243; AAH40243.1; -; mRNA.
DR CCDS; CCDS36592.1; -.
DR RefSeq; NP_001185972.1; NM_001199043.1.
DR RefSeq; NP_061374.1; NM_018886.5.
DR RefSeq; XP_006516777.1; XM_006516714.2.
DR RefSeq; XP_006516778.1; XM_006516715.2.
DR AlphaFoldDB; Q9JL15; -.
DR SMR; Q9JL15; -.
DR BioGRID; 207794; 3.
DR STRING; 10090.ENSMUSP00000097408; -.
DR ChEMBL; CHEMBL4105945; -.
DR iPTMnet; Q9JL15; -.
DR PhosphoSitePlus; Q9JL15; -.
DR jPOST; Q9JL15; -.
DR MaxQB; Q9JL15; -.
DR PaxDb; Q9JL15; -.
DR PRIDE; Q9JL15; -.
DR ProteomicsDB; 264935; -.
DR Antibodypedia; 34699; 410 antibodies from 36 providers.
DR DNASU; 56048; -.
DR Ensembl; ENSMUST00000099820; ENSMUSP00000097408; ENSMUSG00000057554.
DR Ensembl; ENSMUST00000099821; ENSMUSP00000097409; ENSMUSG00000057554.
DR Ensembl; ENSMUST00000124888; ENSMUSP00000115094; ENSMUSG00000057554.
DR GeneID; 56048; -.
DR KEGG; mmu:56048; -.
DR UCSC; uc007plm.3; mouse.
DR CTD; 3964; -.
DR MGI; MGI:1928481; Lgals8.
DR VEuPathDB; HostDB:ENSMUSG00000057554; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000155727; -.
DR HOGENOM; CLU_037794_1_0_1; -.
DR InParanoid; Q9JL15; -.
DR PhylomeDB; Q9JL15; -.
DR TreeFam; TF315551; -.
DR BioGRID-ORCS; 56048; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Lgals8; mouse.
DR PRO; PR:Q9JL15; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9JL15; protein.
DR Bgee; ENSMUSG00000057554; Expressed in spermatid and 249 other tissues.
DR ExpressionAtlas; Q9JL15; baseline and differential.
DR Genevisible; Q9JL15; MM.
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; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0031295; P:T cell costimulation; IDA:MGI.
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 1: Evidence at protein level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Lectin; Reference proteome;
KW Repeat.
FT CHAIN 1..316
FT /note="Galectin-8"
FT /id="PRO_0000076944"
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; 36162 MW; 11A20309AEF52C69 CRC64;
MLSLNNLQNI IYNPIIPYVG TITEQLKPGS LIVIRGHVPK DSERFQVDFQ LGNSLKPRAD
VAFHFNPRFK RSSCIVCNTL TQEKWGWEEI TYDMPFRKEK SFEIVFMVLK NKFQVAVNGR
HVLLYAHRIS PEQIDTVGIY GKVNIHSIGF RFSSDLQSME TSALGLTQIN RENIQKPGKL
QLSLPFEARL NASMGPGRTV VIKGEVNTNA RSFNVDLVAG KTRDIALHLN PRLNVKAFVR
NSFLQDAWGE EERNITCFPF SSGMYFEMII YCDVREFKVA INGVHSLEYK HRFKDLSSID
TLSVDGDIRL LDVRSW
