LEG8_HUMAN
ID LEG8_HUMAN Reviewed; 317 AA.
AC O00214; O15215; Q5T3P5; Q5T3Q4; Q8TEV1; Q96B92; Q9BXC8; Q9H584; Q9H585;
AC Q9UEZ6; Q9UP32; Q9UP33; Q9UP34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 4.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Galectin-8 {ECO:0000303|Ref.2};
DE Short=Gal-8;
DE AltName: Full=Po66 carbohydrate-binding protein;
DE Short=Po66-CBP;
DE AltName: Full=Prostate carcinoma tumor antigen 1 {ECO:0000303|PubMed:8692978};
DE Short=PCTA-1 {ECO:0000303|PubMed:8692978};
GN Name=LGALS8 {ECO:0000312|HGNC:HGNC:6569};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-56 AND SER-184.
RC TISSUE=Prostate;
RX PubMed=8692978; DOI=10.1073/pnas.93.14.7252;
RA Su Z.-Z., Lin J., Shen R., Fisher P.E., Goldstein N.I., Fisher P.B.;
RT "Surface-epitope masking and expression cloning identifies the human
RT prostate carcinoma tumor antigen gene PCTA-1 a member of the galectin gene
RT family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:7252-7257(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Hippocampus;
RA Hadari Y.R., Eisenstein M., Zakut R., Zick Y.;
RT "Galectin-8: on the road from structure to function.";
RL Trends Glycosci. Glycotechnol. 9:103-112(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, AND
RP VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
RC TISSUE=Lung carcinoma;
RA Brichory F., Bidon N., Desrues B., Bourguet P., Le Pennec J.-P., Dazord L.;
RT "Molecular cloning of a beta-galactoside-binding lectin related to
RT galectin-8 and identified in human lung carcinoma.";
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-19; CYS-36; VAL-56 AND
RP SER-184.
RA Maier C., Haeussler J., Roesch K., Moschgath E., Vogel W.;
RT "Genomic organization and expression of the human galectin-8 gene.";
RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10980616; DOI=10.1038/sj.onc.1203767;
RA Gopalkrishnan R.V., Roberts T., Tuli S., Kang D., Christiansen K.A.,
RA Fisher P.B.;
RT "Molecular characterization of prostate carcinoma tumor antigen-1, PCTA-1,
RT a human galectin-8 related gene.";
RL Oncogene 19:4405-4416(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon carcinoma;
RA Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B.,
RA Kaltner H., Wolf E., Gabius H.-J.;
RT "Coca (colorectal carcinoma-derived) galectin-8 variant I full-length cDNA
RT from a human colorectal carcinoma cell line.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Colon carcinoma;
RA Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B.,
RA Kaltner H., Wolf E., Gabius H.-J.;
RT "Coca (Colorectal carcinoma-derived) galectin-8 variant II.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS TYR-19; CYS-36 AND
RP VAL-56.
RA Moisan S., Mercier J., Demers M., Belanger S.D., Alain T.,
RA Kossakowska A.E., Potworowski E.F., St-Pierre Y.;
RT "Galectins in murine and human non-Hodgkin's lymphomas.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP TYR-19; CYS-36; VAL-56 AND SER-184.
RC TISSUE=Brain, and Skin;
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 [11]
RP INTERACTION WITH PDPN.
RX PubMed=19268462; DOI=10.1016/j.yexcr.2009.02.021;
RA Cueni L.N., Detmar M.;
RT "Galectin-8 interacts with podoplanin and modulates lymphatic endothelial
RT cell functions.";
RL Exp. Cell Res. 315:1715-1723(2009).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CALCOCO2, AND MUTAGENESIS
RP OF ARG-69 AND ARG-190.
RX PubMed=22246324; DOI=10.1038/nature10744;
RA Thurston T.L., Wandel M.P., von Muhlinen N., Foeglein A., Randow F.;
RT "Galectin 8 targets damaged vesicles for autophagy to defend cells against
RT bacterial invasion.";
RL Nature 482:414-418(2012).
RN [13]
RP FUNCTION.
RX PubMed=28077878; DOI=10.1038/nature21032;
RA Staring J., von Castelmur E., Blomen V.A., van den Hengel L.G.,
RA Brockmann M., Baggen J., Thibaut H.J., Nieuwenhuis J., Janssen H.,
RA van Kuppeveld F.J., Perrakis A., Carette J.E., Brummelkamp T.R.;
RT "PLA2G16 represents a switch between entry and clearance of
RT Picornaviridae.";
RL Nature 541:412-416(2017).
RN [14]
RP STRUCTURE BY NMR OF 176-317.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal Gal-bind lectin protein from human
RT galectin-8.";
RL Submitted (FEB-2008) to the PDB data bank.
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-152 IN COMPLEX WITH LACTOSE.
RG RIKEN structural genomics initiative (RSGI);
RT "Crystal structure of N-terminal domain of human galectin-8.";
RL Submitted (MAY-2008) to the PDB data bank.
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-154 ALONE AND IN COMPLEX WITH
RP CARBOHYDRATES, FUNCTION, AND SUBUNIT.
RX PubMed=21288902; DOI=10.1074/jbc.m110.195925;
RA Ideo H., Matsuzaka T., Nonaka T., Seko A., Yamashita K.;
RT "Galectin-8-N-domain recognition mechanism for sialylated and sulfated
RT glycans.";
RL J. Biol. Chem. 286:11346-11355(2011).
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 (PubMed:22246324,
CC PubMed:28077878). Detects membrane rupture by binding beta-galactoside
CC ligands located on the lumenal side of the endosome membrane; these
CC ligands becoming exposed to the cytoplasm following rupture
CC (PubMed:22246324, PubMed:28077878). Restricts infection by initiating
CC autophagy via interaction with CALCOCO2/NDP52 (PubMed:22246324,
CC PubMed:28077878). Required to restrict infection of bacterial invasion
CC such as S.typhimurium (PubMed:22246324). Also required to restrict
CC infection of Picornaviridae viruses (PubMed:28077878). Has a marked
CC preference for 3'-O-sialylated and 3'-O-sulfated glycans
CC (PubMed:21288902). {ECO:0000269|PubMed:21288902,
CC ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:28077878}.
CC -!- SUBUNIT: Homodimer (PubMed:21288902, Ref.15). Interacts with
CC CALCOCO2/NDP52 (PubMed:22246324). Interacts with PDPN; the interaction
CC is glycosylation-dependent; may participate in connection of the
CC lymphatic endothelium to the surrounding extracellular matrix.
CC {ECO:0000269|PubMed:21288902, ECO:0000269|PubMed:22246324,
CC ECO:0000269|Ref.15}.
CC -!- INTERACTION:
CC O00214; P13798: APEH; NbExp=4; IntAct=EBI-740058, EBI-723792;
CC O00214; Q13137: CALCOCO2; NbExp=7; IntAct=EBI-740058, EBI-739580;
CC O00214; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-740058, EBI-10172526;
CC O00214; Q86VP1: TAX1BP1; NbExp=4; IntAct=EBI-740058, EBI-529518;
CC O00214; Q15583: TGIF1; NbExp=10; IntAct=EBI-740058, EBI-714215;
CC O00214; P36406: TRIM23; NbExp=4; IntAct=EBI-740058, EBI-740098;
CC O00214; O76024: WFS1; NbExp=3; IntAct=EBI-740058, EBI-720609;
CC O00214; P0DTC2: S; Xeno; NbExp=2; IntAct=EBI-740058, EBI-25474821;
CC O00214-2; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-12069522, EBI-739580;
CC O00214-2; P27797: CALR; NbExp=3; IntAct=EBI-12069522, EBI-1049597;
CC O00214-2; P36957: DLST; NbExp=3; IntAct=EBI-12069522, EBI-351007;
CC O00214-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-12069522, EBI-10172526;
CC O00214-2; Q96RE7: NACC1; NbExp=3; IntAct=EBI-12069522, EBI-7950997;
CC O00214-2; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-12069522, EBI-1055945;
CC O00214-2; Q6NSM0: NR1D2; NbExp=3; IntAct=EBI-12069522, EBI-10250949;
CC O00214-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-12069522, EBI-529518;
CC O00214-2; Q969T9: WBP2; NbExp=3; IntAct=EBI-12069522, EBI-727055;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
CC {ECO:0000269|PubMed:22246324}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:22246324}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=I;
CC IsoId=O00214-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00214-2; Sequence=VSP_003094;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Selective expression by prostate
CC carcinomas versus normal prostate and benign prostatic hypertrophy.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51605.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD45402.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD45403.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD45404.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD45404.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=AAH15818.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH16486.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-8 C-terminal CRD;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_832";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-8 long isoform;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_833";
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-8 long isoform;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_834";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L78132; AAB51605.1; ALT_INIT; mRNA.
DR EMBL; X91790; CAA62904.1; -; mRNA.
DR EMBL; AF074000; AAD45402.1; ALT_INIT; mRNA.
DR EMBL; AF074001; AAD45403.1; ALT_INIT; mRNA.
DR EMBL; AF074002; AAD45404.1; ALT_SEQ; mRNA.
DR EMBL; AF193806; AAF19370.1; -; Genomic_DNA.
DR EMBL; AF193805; AAF19370.1; JOINED; Genomic_DNA.
DR EMBL; AF342815; AAK16735.1; -; mRNA.
DR EMBL; AF342816; AAK16736.1; -; mRNA.
DR EMBL; AF468213; AAL77076.1; -; mRNA.
DR EMBL; AL359921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC015818; AAH15818.1; ALT_INIT; mRNA.
DR EMBL; BC016486; AAH16486.2; ALT_INIT; mRNA.
DR CCDS; CCDS1611.1; -. [O00214-2]
DR CCDS; CCDS1612.1; -. [O00214-1]
DR PIR; JC6147; JC6147.
DR RefSeq; NP_006490.3; NM_006499.4. [O00214-2]
DR RefSeq; NP_963837.1; NM_201543.2. [O00214-1]
DR RefSeq; NP_963838.1; NM_201544.2. [O00214-1]
DR RefSeq; NP_963839.1; NM_201545.2. [O00214-2]
DR PDB; 2YRO; NMR; -; A=176-317.
DR PDB; 2YV8; X-ray; 1.92 A; A=1-152.
DR PDB; 2YXS; X-ray; 2.13 A; A=1-152.
DR PDB; 3AP4; X-ray; 2.33 A; A/B/C/D=1-154.
DR PDB; 3AP5; X-ray; 1.92 A; A=1-154.
DR PDB; 3AP6; X-ray; 1.58 A; A/B/C/D=1-154.
DR PDB; 3AP7; X-ray; 1.53 A; A=1-154.
DR PDB; 3AP9; X-ray; 1.33 A; A=1-154.
DR PDB; 3APB; X-ray; 1.95 A; A/B=1-154.
DR PDB; 3OJB; X-ray; 3.01 A; A/B/C/D=186-315.
DR PDB; 3VKL; X-ray; 2.55 A; A/B=1-155, A/B=184-317.
DR PDB; 3VKM; X-ray; 2.98 A; A/B=1-155, A/B=184-317.
DR PDB; 3VKN; X-ray; 1.98 A; A/B=1-153.
DR PDB; 3VKO; X-ray; 2.08 A; A/B=1-153.
DR PDB; 4BMB; X-ray; 1.35 A; A=4-153.
DR PDB; 4BME; X-ray; 2.00 A; A/B=4-155.
DR PDB; 4FQZ; X-ray; 2.80 A; A=1-155, A=184-317.
DR PDB; 4GXL; X-ray; 2.02 A; A=186-317.
DR PDB; 4HAN; X-ray; 2.55 A; A/B=1-155, A/B=184-317.
DR PDB; 5GZC; X-ray; 1.08 A; A=7-158.
DR PDB; 5GZD; X-ray; 1.19 A; A=7-154.
DR PDB; 5GZE; X-ray; 1.32 A; A=7-154.
DR PDB; 5GZF; X-ray; 2.00 A; A=1-186.
DR PDB; 5GZG; X-ray; 2.00 A; A=1-186.
DR PDB; 5T7I; X-ray; 2.00 A; A=1-155.
DR PDB; 5T7S; X-ray; 1.90 A; A=1-155.
DR PDB; 5T7T; X-ray; 1.96 A; A=1-155.
DR PDB; 5T7U; X-ray; 1.58 A; A=1-155.
DR PDB; 5VWG; X-ray; 2.10 A; A=1-155.
DR PDB; 6W4Z; X-ray; 1.59 A; A/B=2-154.
DR PDB; 6Z6Y; X-ray; 1.34 A; A=1-163.
DR PDB; 7AEN; X-ray; 1.60 A; A/B=7-156.
DR PDB; 7ALS; X-ray; 1.35 A; A/B=4-158.
DR PDB; 7P1M; X-ray; 1.52 A; A/B=6-156.
DR PDBsum; 2YRO; -.
DR PDBsum; 2YV8; -.
DR PDBsum; 2YXS; -.
DR PDBsum; 3AP4; -.
DR PDBsum; 3AP5; -.
DR PDBsum; 3AP6; -.
DR PDBsum; 3AP7; -.
DR PDBsum; 3AP9; -.
DR PDBsum; 3APB; -.
DR PDBsum; 3OJB; -.
DR PDBsum; 3VKL; -.
DR PDBsum; 3VKM; -.
DR PDBsum; 3VKN; -.
DR PDBsum; 3VKO; -.
DR PDBsum; 4BMB; -.
DR PDBsum; 4BME; -.
DR PDBsum; 4FQZ; -.
DR PDBsum; 4GXL; -.
DR PDBsum; 4HAN; -.
DR PDBsum; 5GZC; -.
DR PDBsum; 5GZD; -.
DR PDBsum; 5GZE; -.
DR PDBsum; 5GZF; -.
DR PDBsum; 5GZG; -.
DR PDBsum; 5T7I; -.
DR PDBsum; 5T7S; -.
DR PDBsum; 5T7T; -.
DR PDBsum; 5T7U; -.
DR PDBsum; 5VWG; -.
DR PDBsum; 6W4Z; -.
DR PDBsum; 6Z6Y; -.
DR PDBsum; 7AEN; -.
DR PDBsum; 7ALS; -.
DR PDBsum; 7P1M; -.
DR AlphaFoldDB; O00214; -.
DR SMR; O00214; -.
DR BioGRID; 110155; 173.
DR IntAct; O00214; 112.
DR MINT; O00214; -.
DR BindingDB; O00214; -.
DR ChEMBL; CHEMBL5475; -.
DR DrugCentral; O00214; -.
DR UniLectin; O00214; -.
DR iPTMnet; O00214; -.
DR PhosphoSitePlus; O00214; -.
DR BioMuta; LGALS8; -.
DR EPD; O00214; -.
DR jPOST; O00214; -.
DR MassIVE; O00214; -.
DR MaxQB; O00214; -.
DR PeptideAtlas; O00214; -.
DR PRIDE; O00214; -.
DR ProteomicsDB; 47785; -. [O00214-1]
DR ProteomicsDB; 47786; -. [O00214-2]
DR Antibodypedia; 34699; 410 antibodies from 36 providers.
DR DNASU; 3964; -.
DR Ensembl; ENST00000341872.10; ENSP00000342139.6; ENSG00000116977.19. [O00214-1]
DR Ensembl; ENST00000352231.6; ENSP00000309576.2; ENSG00000116977.19. [O00214-2]
DR Ensembl; ENST00000366584.9; ENSP00000355543.4; ENSG00000116977.19. [O00214-1]
DR Ensembl; ENST00000450372.6; ENSP00000408657.2; ENSG00000116977.19. [O00214-2]
DR Ensembl; ENST00000526589.5; ENSP00000435460.1; ENSG00000116977.19. [O00214-2]
DR Ensembl; ENST00000526634.5; ENSP00000437040.1; ENSG00000116977.19. [O00214-1]
DR Ensembl; ENST00000527974.5; ENSP00000431398.1; ENSG00000116977.19. [O00214-2]
DR GeneID; 3964; -.
DR KEGG; hsa:3964; -.
DR MANE-Select; ENST00000366584.9; ENSP00000355543.4; NM_201544.4; NP_963838.1.
DR UCSC; uc001hxw.3; human. [O00214-1]
DR CTD; 3964; -.
DR DisGeNET; 3964; -.
DR GeneCards; LGALS8; -.
DR HGNC; HGNC:6569; LGALS8.
DR HPA; ENSG00000116977; Low tissue specificity.
DR MIM; 606099; gene.
DR neXtProt; NX_O00214; -.
DR OpenTargets; ENSG00000116977; -.
DR PharmGKB; PA30346; -.
DR VEuPathDB; HostDB:ENSG00000116977; -.
DR GeneTree; ENSGT00940000155727; -.
DR InParanoid; O00214; -.
DR OMA; LYAHRIK; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; O00214; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; O00214; -.
DR SignaLink; O00214; -.
DR BioGRID-ORCS; 3964; 10 hits in 1085 CRISPR screens.
DR ChiTaRS; LGALS8; human.
DR EvolutionaryTrace; O00214; -.
DR GeneWiki; Galectin-8; -.
DR GeneWiki; LGALS8; -.
DR GenomeRNAi; 3964; -.
DR Pharos; O00214; Tchem.
DR PRO; PR:O00214; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O00214; protein.
DR Bgee; ENSG00000116977; Expressed in sperm and 198 other tissues.
DR ExpressionAtlas; O00214; baseline and differential.
DR Genevisible; O00214; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IDA:GO_Central.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030246; F:carbohydrate binding; IDA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
DR GO; GO:1904977; P:lymphatic endothelial cell migration; IDA:UniProtKB.
DR GO; GO:0098792; P:xenophagy; IMP:UniProtKB.
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 3D-structure; Alternative splicing; Autophagy; Cytoplasm;
KW Cytoplasmic vesicle; Lectin; Reference proteome; Repeat.
FT CHAIN 1..317
FT /note="Galectin-8"
FT /id="PRO_0000076943"
FT DOMAIN 19..152
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 187..317
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 69
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21288902"
FT BINDING 79
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21288902"
FT BINDING 89
FT /ligand="a carbohydrate"
FT /ligand_id="ChEBI:CHEBI:16646"
FT /evidence="ECO:0000269|PubMed:21288902"
FT BINDING 249..255
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT SITE 59
FT /note="Critical for binding to sialylated and sulfated
FT oligosaccharides"
FT /evidence="ECO:0000269|PubMed:21288902"
FT VAR_SEQ 183
FT /note="L -> LPSNRGGDISKIAPRTVYTKSKDSTVNHTLTCTKIPPMNYVSK (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3,
FT ECO:0000303|Ref.7, ECO:0000303|Ref.8"
FT /id="VSP_003094"
FT VARIANT 19
FT /note="F -> Y (in dbSNP:rs1126407)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.8"
FT /id="VAR_012990"
FT VARIANT 36
FT /note="R -> C (in dbSNP:rs1041935)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.8"
FT /id="VAR_009710"
FT VARIANT 56
FT /note="M -> V (in dbSNP:rs1041937)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8692978, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4, ECO:0000269|Ref.8"
FT /id="VAR_012991"
FT VARIANT 184
FT /note="R -> S (in dbSNP:rs2243525)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:8692978, ECO:0000269|Ref.3,
FT ECO:0000269|Ref.4"
FT /id="VAR_063506"
FT MUTAGEN 69
FT /note="R->H: Abolishes localization to cytoplasmic vesicles
FT in case of infection by S.typhimurium."
FT /evidence="ECO:0000269|PubMed:22246324"
FT MUTAGEN 190
FT /note="R->H: Does not affect localization to cytoplasmic
FT vesicles in case of infection by S.typhimurium."
FT /evidence="ECO:0000269|PubMed:22246324"
FT CONFLICT 14
FT /note="N -> S (in Ref. 8; AAL77076)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..100
FT /note="KRE -> QKEK (in Ref. 2; CAA62904)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="D -> A (in Ref. 2; CAA62904)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="S -> V (in Ref. 1; AAB51605)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="R -> G (in Ref. 8; AAL77076)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="K -> Q (in Ref. 1; AAB51605)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="D -> H (in Ref. 8; AAL77076)"
FT /evidence="ECO:0000305"
FT CONFLICT 259
FT /note="F -> L (in Ref. 7; AAK16736)"
FT /evidence="ECO:0000305"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:4FQZ"
FT STRAND 9..14
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 44..53
FT /evidence="ECO:0007829|PDB:5GZC"
FT TURN 56..59
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3VKL"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:5GZC"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:5GZC"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:5GZC"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:6Z6Y"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 213..220
FT /evidence="ECO:0007829|PDB:4GXL"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 225..233
FT /evidence="ECO:0007829|PDB:4GXL"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:3VKL"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3OJB"
FT STRAND 266..273
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 275..282
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 285..291
FT /evidence="ECO:0007829|PDB:4GXL"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:4GXL"
FT STRAND 302..317
FT /evidence="ECO:0007829|PDB:4GXL"
FT CONFLICT O00214-2:220
FT /note="M -> T (in Ref. 8; AAL77076)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 317 AA; 35808 MW; AA13116AC5C0D69A CRC64;
MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA
DVAFHFNPRF KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG
KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST QASSLELTEI SRENVPKSGT
PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV
RNSFLQESWG EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI
DTLEINGDIH LLEVRSW
