Full text data of LGALS8
LGALS8
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Galectin-8; Gal-8 (Po66 carbohydrate-binding protein; Po66-CBP; Prostate carcinoma tumor antigen 1; PCTA-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Galectin-8; Gal-8 (Po66 carbohydrate-binding protein; Po66-CBP; Prostate carcinoma tumor antigen 1; PCTA-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Comments
Isoform O00214-2 was detected.
Isoform O00214-2 was detected.
UniProt
O00214
ID LEG8_HUMAN Reviewed; 317 AA.
AC O00214; O15215; Q5T3P5; Q5T3Q4; Q8TEV1; Q96B92; Q9BXC8; Q9H584;
read moreAC Q9H585; Q9UEZ6; Q9UP32; Q9UP33; Q9UP34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Galectin-8;
DE Short=Gal-8;
DE AltName: Full=Po66 carbohydrate-binding protein;
DE Short=Po66-CBP;
DE AltName: Full=Prostate carcinoma tumor antigen 1;
DE Short=PCTA-1;
GN Name=LGALS8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-56 AND
RP 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
RT gene 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,
RP AND 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.,
RA 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
RP AND 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,
RT PCTA-1, 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
RT cDNA 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
RP AND 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP VARIANTS 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
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
RT human galectin-8.";
RL Submitted (FEB-2008) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-152 IN COMPLEX WITH
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-154 ALONE AND IN COMPLEX
RP WITH 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: Lectin with a marked preference for 3'-O-sialylated and
CC 3'-O-sulfated glycans.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q15583:TGIF1; NbExp=10; IntAct=EBI-740058, EBI-714215;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
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 Note=Ref.8 (AAL77076) sequence is in conflict in position:
CC 220:M->T;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Selective expression by prostate
CC carcinomas versus normal prostate and benign prostatic
CC hypertrophy.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- SIMILARITY: Contains 2 galectin domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51605.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45402.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45403.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45404.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45404.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAH15818.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH16486.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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";
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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; CAI13773.1; -; Genomic_DNA.
DR EMBL; AL359921; CAI13774.1; -; Genomic_DNA.
DR EMBL; BC015818; AAH15818.1; ALT_INIT; mRNA.
DR EMBL; BC016486; AAH16486.2; ALT_INIT; mRNA.
DR PIR; JC6147; JC6147.
DR RefSeq; NP_006490.3; NM_006499.4.
DR RefSeq; NP_963837.1; NM_201543.2.
DR RefSeq; NP_963838.1; NM_201544.2.
DR RefSeq; NP_963839.1; NM_201545.2.
DR RefSeq; XP_005273184.1; XM_005273127.1.
DR UniGene; Hs.4082; -.
DR UniGene; Hs.708114; -.
DR UniGene; Hs.735982; -.
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=1-317.
DR PDB; 3VKM; X-ray; 2.98 A; A/B=1-317.
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; 4FQZ; X-ray; 2.80 A; A=1-317.
DR PDB; 4GXL; X-ray; 2.02 A; A=186-317.
DR PDB; 4HAN; X-ray; 2.55 A; A/B=1-317.
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; 4FQZ; -.
DR PDBsum; 4GXL; -.
DR PDBsum; 4HAN; -.
DR ProteinModelPortal; O00214; -.
DR SMR; O00214; 1-317.
DR IntAct; O00214; 2.
DR MINT; MINT-1458207; -.
DR BindingDB; O00214; -.
DR ChEMBL; CHEMBL5475; -.
DR PhosphoSite; O00214; -.
DR PaxDb; O00214; -.
DR PRIDE; O00214; -.
DR DNASU; 3964; -.
DR Ensembl; ENST00000341872; ENSP00000342139; ENSG00000116977.
DR Ensembl; ENST00000352231; ENSP00000309576; ENSG00000116977.
DR Ensembl; ENST00000366584; ENSP00000355543; ENSG00000116977.
DR Ensembl; ENST00000450372; ENSP00000408657; ENSG00000116977.
DR Ensembl; ENST00000526589; ENSP00000435460; ENSG00000116977.
DR Ensembl; ENST00000526634; ENSP00000437040; ENSG00000116977.
DR Ensembl; ENST00000527974; ENSP00000431398; ENSG00000116977.
DR GeneID; 3964; -.
DR KEGG; hsa:3964; -.
DR UCSC; uc001hxz.2; human.
DR CTD; 3964; -.
DR GeneCards; GC01P236681; -.
DR HGNC; HGNC:6569; LGALS8.
DR HPA; HPA030491; -.
DR MIM; 606099; gene.
DR neXtProt; NX_O00214; -.
DR PharmGKB; PA30346; -.
DR eggNOG; NOG264430; -.
DR HOVERGEN; HBG002412; -.
DR KO; K06832; -.
DR OMA; VNIHSVG; -.
DR ChiTaRS; LGALS8; human.
DR EvolutionaryTrace; O00214; -.
DR GeneWiki; Galectin-8; -.
DR GeneWiki; LGALS8; -.
DR GenomeRNAi; 3964; -.
DR NextBio; 15552; -.
DR PRO; PR:O00214; -.
DR ArrayExpress; O00214; -.
DR Bgee; O00214; -.
DR Genevestigator; O00214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Lectin; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 317 Galectin-8.
FT /FTId=PRO_0000076943.
FT DOMAIN 19 152 Galectin 1.
FT DOMAIN 187 317 Galectin 2.
FT REGION 249 255 Beta-galactoside binding (By similarity).
FT BINDING 69 69 Carbohydrate.
FT BINDING 79 79 Carbohydrate.
FT BINDING 89 89 Carbohydrate.
FT SITE 59 59 Critical for binding to sialylated and
FT sulfated oligosaccharides.
FT VAR_SEQ 183 183 L -> LPSNRGGDISKIAPRTVYTKSKDSTVNHTLTCTKIP
FT PMNYVSK (in isoform 2).
FT /FTId=VSP_003094.
FT VARIANT 19 19 F -> Y (in dbSNP:rs2737713).
FT /FTId=VAR_012990.
FT VARIANT 36 36 R -> C (in dbSNP:rs1041935).
FT /FTId=VAR_009710.
FT VARIANT 56 56 M -> V (in dbSNP:rs1041937).
FT /FTId=VAR_012991.
FT VARIANT 184 184 R -> S (in dbSNP:rs2243525).
FT /FTId=VAR_063506.
FT CONFLICT 14 14 N -> S (in Ref. 8; AAL77076).
FT CONFLICT 98 100 KRE -> QKEK (in Ref. 2; CAA62904).
FT CONFLICT 112 112 D -> A (in Ref. 2; CAA62904).
FT CONFLICT 171 171 S -> V (in Ref. 1; AAB51605).
FT CONFLICT 199 199 R -> G (in Ref. 8; AAL77076).
FT CONFLICT 204 204 K -> Q (in Ref. 1; AAB51605).
FT CONFLICT 225 225 D -> H (in Ref. 8; AAL77076).
FT CONFLICT 259 259 F -> L (in Ref. 7; AAK16736).
FT STRAND 4 6
FT STRAND 8 14
FT STRAND 17 22
FT STRAND 32 38
FT STRAND 44 53
FT TURN 56 59
FT STRAND 61 69
FT STRAND 71 73
FT STRAND 75 82
FT STRAND 90 92
FT STRAND 102 109
FT STRAND 111 118
FT STRAND 121 127
FT HELIX 132 134
FT STRAND 137 143
FT STRAND 145 152
FT STRAND 186 190
FT STRAND 200 207
FT STRAND 213 220
FT TURN 221 224
FT STRAND 225 233
FT TURN 234 237
FT STRAND 238 245
FT STRAND 246 249
FT STRAND 256 258
FT STRAND 266 273
FT STRAND 275 282
FT STRAND 285 291
FT HELIX 297 299
FT STRAND 302 317
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
//
ID LEG8_HUMAN Reviewed; 317 AA.
AC O00214; O15215; Q5T3P5; Q5T3Q4; Q8TEV1; Q96B92; Q9BXC8; Q9H584;
read moreAC Q9H585; Q9UEZ6; Q9UP32; Q9UP33; Q9UP34;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 4.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Galectin-8;
DE Short=Gal-8;
DE AltName: Full=Po66 carbohydrate-binding protein;
DE Short=Po66-CBP;
DE AltName: Full=Prostate carcinoma tumor antigen 1;
DE Short=PCTA-1;
GN Name=LGALS8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-56 AND
RP 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
RT gene 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,
RP AND 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.,
RA 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
RP AND 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,
RT PCTA-1, 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
RT cDNA 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
RP AND 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.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP VARIANTS 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
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
RT human galectin-8.";
RL Submitted (FEB-2008) to the PDB data bank.
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-152 IN COMPLEX WITH
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-154 ALONE AND IN COMPLEX
RP WITH 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: Lectin with a marked preference for 3'-O-sialylated and
CC 3'-O-sulfated glycans.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q15583:TGIF1; NbExp=10; IntAct=EBI-740058, EBI-714215;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Probable).
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 Note=Ref.8 (AAL77076) sequence is in conflict in position:
CC 220:M->T;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Selective expression by prostate
CC carcinomas versus normal prostate and benign prostatic
CC hypertrophy.
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- SIMILARITY: Contains 2 galectin domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51605.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45402.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45403.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45404.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAD45404.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact;
CC Sequence=AAH15818.1; Type=Erroneous initiation; Note=Translation N-terminally extended;
CC Sequence=AAH16486.2; Type=Erroneous initiation; Note=Translation N-terminally extended;
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 -----------------------------------------------------------------------
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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; CAI13773.1; -; Genomic_DNA.
DR EMBL; AL359921; CAI13774.1; -; Genomic_DNA.
DR EMBL; BC015818; AAH15818.1; ALT_INIT; mRNA.
DR EMBL; BC016486; AAH16486.2; ALT_INIT; mRNA.
DR PIR; JC6147; JC6147.
DR RefSeq; NP_006490.3; NM_006499.4.
DR RefSeq; NP_963837.1; NM_201543.2.
DR RefSeq; NP_963838.1; NM_201544.2.
DR RefSeq; NP_963839.1; NM_201545.2.
DR RefSeq; XP_005273184.1; XM_005273127.1.
DR UniGene; Hs.4082; -.
DR UniGene; Hs.708114; -.
DR UniGene; Hs.735982; -.
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=1-317.
DR PDB; 3VKM; X-ray; 2.98 A; A/B=1-317.
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; 4FQZ; X-ray; 2.80 A; A=1-317.
DR PDB; 4GXL; X-ray; 2.02 A; A=186-317.
DR PDB; 4HAN; X-ray; 2.55 A; A/B=1-317.
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; 4FQZ; -.
DR PDBsum; 4GXL; -.
DR PDBsum; 4HAN; -.
DR ProteinModelPortal; O00214; -.
DR SMR; O00214; 1-317.
DR IntAct; O00214; 2.
DR MINT; MINT-1458207; -.
DR BindingDB; O00214; -.
DR ChEMBL; CHEMBL5475; -.
DR PhosphoSite; O00214; -.
DR PaxDb; O00214; -.
DR PRIDE; O00214; -.
DR DNASU; 3964; -.
DR Ensembl; ENST00000341872; ENSP00000342139; ENSG00000116977.
DR Ensembl; ENST00000352231; ENSP00000309576; ENSG00000116977.
DR Ensembl; ENST00000366584; ENSP00000355543; ENSG00000116977.
DR Ensembl; ENST00000450372; ENSP00000408657; ENSG00000116977.
DR Ensembl; ENST00000526589; ENSP00000435460; ENSG00000116977.
DR Ensembl; ENST00000526634; ENSP00000437040; ENSG00000116977.
DR Ensembl; ENST00000527974; ENSP00000431398; ENSG00000116977.
DR GeneID; 3964; -.
DR KEGG; hsa:3964; -.
DR UCSC; uc001hxz.2; human.
DR CTD; 3964; -.
DR GeneCards; GC01P236681; -.
DR HGNC; HGNC:6569; LGALS8.
DR HPA; HPA030491; -.
DR MIM; 606099; gene.
DR neXtProt; NX_O00214; -.
DR PharmGKB; PA30346; -.
DR eggNOG; NOG264430; -.
DR HOVERGEN; HBG002412; -.
DR KO; K06832; -.
DR OMA; VNIHSVG; -.
DR ChiTaRS; LGALS8; human.
DR EvolutionaryTrace; O00214; -.
DR GeneWiki; Galectin-8; -.
DR GeneWiki; LGALS8; -.
DR GenomeRNAi; 3964; -.
DR NextBio; 15552; -.
DR PRO; PR:O00214; -.
DR ArrayExpress; O00214; -.
DR Bgee; O00214; -.
DR Genevestigator; O00214; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
DR GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
DR Gene3D; 2.60.120.200; -; 2.
DR InterPro; IPR008985; ConA-like_lec_gl_sf.
DR InterPro; IPR013320; ConA-like_subgrp.
DR InterPro; IPR001079; Galectin_CRD.
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; Complete proteome; Cytoplasm;
KW Lectin; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 317 Galectin-8.
FT /FTId=PRO_0000076943.
FT DOMAIN 19 152 Galectin 1.
FT DOMAIN 187 317 Galectin 2.
FT REGION 249 255 Beta-galactoside binding (By similarity).
FT BINDING 69 69 Carbohydrate.
FT BINDING 79 79 Carbohydrate.
FT BINDING 89 89 Carbohydrate.
FT SITE 59 59 Critical for binding to sialylated and
FT sulfated oligosaccharides.
FT VAR_SEQ 183 183 L -> LPSNRGGDISKIAPRTVYTKSKDSTVNHTLTCTKIP
FT PMNYVSK (in isoform 2).
FT /FTId=VSP_003094.
FT VARIANT 19 19 F -> Y (in dbSNP:rs2737713).
FT /FTId=VAR_012990.
FT VARIANT 36 36 R -> C (in dbSNP:rs1041935).
FT /FTId=VAR_009710.
FT VARIANT 56 56 M -> V (in dbSNP:rs1041937).
FT /FTId=VAR_012991.
FT VARIANT 184 184 R -> S (in dbSNP:rs2243525).
FT /FTId=VAR_063506.
FT CONFLICT 14 14 N -> S (in Ref. 8; AAL77076).
FT CONFLICT 98 100 KRE -> QKEK (in Ref. 2; CAA62904).
FT CONFLICT 112 112 D -> A (in Ref. 2; CAA62904).
FT CONFLICT 171 171 S -> V (in Ref. 1; AAB51605).
FT CONFLICT 199 199 R -> G (in Ref. 8; AAL77076).
FT CONFLICT 204 204 K -> Q (in Ref. 1; AAB51605).
FT CONFLICT 225 225 D -> H (in Ref. 8; AAL77076).
FT CONFLICT 259 259 F -> L (in Ref. 7; AAK16736).
FT STRAND 4 6
FT STRAND 8 14
FT STRAND 17 22
FT STRAND 32 38
FT STRAND 44 53
FT TURN 56 59
FT STRAND 61 69
FT STRAND 71 73
FT STRAND 75 82
FT STRAND 90 92
FT STRAND 102 109
FT STRAND 111 118
FT STRAND 121 127
FT HELIX 132 134
FT STRAND 137 143
FT STRAND 145 152
FT STRAND 186 190
FT STRAND 200 207
FT STRAND 213 220
FT TURN 221 224
FT STRAND 225 233
FT TURN 234 237
FT STRAND 238 245
FT STRAND 246 249
FT STRAND 256 258
FT STRAND 266 273
FT STRAND 275 282
FT STRAND 285 291
FT HELIX 297 299
FT STRAND 302 317
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
//
MIM
606099
*RECORD*
*FIELD* NO
606099
*FIELD* TI
*606099 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 8; LGALS8
;;GALECTIN 8;;
PROSTATE CARCINOMA TUMOR ANTIGEN 1; PCTA1
read more*FIELD* TX
DESCRIPTION
Galectins, such as LGALS8, are beta-galactoside-binding animal lectins
with conserved carbohydrate recognition domains (CRDs). Galectins are
involved in various biologic processes, including cell signaling,
proliferative control, cell adhesion, and cell migration (summary by Su
et al. (1996) and Gopalkrishnan et al. (2000)).
CLONING
By surface-epitope masking and expression cloning using a prostate
cancer cDNA library, Su et al. (1996) isolated a cDNA encoding LGALS8,
which they called PCTA1. The deduced 317-amino acid protein is 81%
homologous to rat galectin-8 (Hadari et al., 1995), which contains 2
CRDs.
By Northern blot analysis, Gopalkrishnan et al. (2000) detected wide but
variable expression of 3 major LGALS8 transcripts of 1.6, 2.6, and 6.0
kb in normal tissue. Fluorescence microscopy demonstrated cytoplasmic
expression.
GENE FUNCTION
Using RT-PCR analysis, Su et al. (1996) detected expression of LGALS8 in
all 7 prostate carcinomas tested, but in only in 1 of 4 benign prostatic
hypertrophy samples tested.
By screening for innate proteins that could recognize human blood group
antigens, Stowell et al. (2010) identified GAL4 (LGALS4; 602518) and
GAL8, both of which are expressed in the intestinal tract, as proteins
that recognized and killed E. coli expressing blood group antigen, but
not bacteria that did not express such antigens. Video, fluorescence,
and electron microscopy showed that bacterial cells lost motility and
membrane integrity upon treatment with these lectins. Mutation analysis
indicated that the killing activity was mediated by the C-terminal
domains of GAL4 and GAL8 in a rapid, complement-independent manner.
Stowell et al. (2010) concluded that innate defense lectins provide
immunity against pathogens expressing blood group-like antigens on their
surface.
Thurston et al. (2012) demonstrated in human cells that galectin-8, a
cytosolic lectin also known as LGALS8, is a danger receptor that
restricts Salmonella proliferation. Galectin-8 monitors endosomal and
lysosomal integrity and detects bacterial invasion by binding host
glycans exposed on damaged Salmonella-containing vacuoles. By recruiting
NDP52 (CALCOCO2; 604587), galectin-8 activates antibacterial autophagy.
Galectin-8-dependent recruitment of NDP52 to Salmonella-containing
vesicles is transient and followed by ubiquitin-dependent NDP52
recruitment. Because galectin-8 also detects sterile damage to endosomes
or lysosomes, as well as invasion by Listeria or Shigella, Thurston et
al. (2012) suggested that galectin-8 serves as a versatile receptor for
vesicle-damaging pathogens. The results of Thurston et al. (2012) also
illustrated how cells deploy the danger receptor galectin-8 to combat
infection by monitoring endosomal and lysosomal integrity on the basis
of the specific lack of complex carbohydrates in the cytosol.
GENE STRUCTURE
By genomic sequence analysis, Gopalkrishnan et al. (2000) determined
that the LGALS8 gene contains a TATA box and 10 exons, 8 of which are
expressed constitutively. The additional exons, 7-prime and
7-double-prime, are present in splice variants.
MAPPING
By radiation hybrid analysis, Gopalkrishnan et al. (2000) mapped the
LGALS8 gene to chromosome 1q42-q43, a region that contains a gene
predisposing to early-onset prostate cancer (PCAP; 602759).
*FIELD* RF
1. Gopalkrishnan, R. V.; Roberts, T.; Tuli, S.; Kang, D.; Christiansen,
K. A.; Fisher, P. B.: Molecular characterization of prostate carcinoma
tumor antigen-1, PCTA-1, a human Galectin-8 related gene. Oncogene 19:
4405-4416, 2000.
2. Hadari, Y. R.; Paz, K.; Dekel, R.; Mestrovic, T.; Accili, D.; Zick,
Y.: Galectin-8: a new rat lectin, related to galectin-4. J. Biol.
Chem. 270: 3447-3453, 1995.
3. Stowell, S. R.; Arthur, C. M.; Dias-Baruffi, M.; Rodrigues, L.
C.; Gourdine, J.-P.; Heimburg-Molinaro, J.; Ju, T.; Molinaro, R. J.;
Rivera-Marrero, C.; Xia, B.; Smith, D. F.; Cummings, R. D.: Innate
immune lectins kill bacteria expressing blood group antigen. Nature
Med. 16: 295-301, 2010.
4. Su, Z.; Lin, J.; Shen, R.; Fisher, P. E.; Goldstein, N. I.; Fisher,
P. B.: Surface-epitope masking and expression cloning identifies
the human prostate carcinoma tumor antigen gene PCTA-1 a member of
the galectin gene family. Proc. Nat. Acad. Sci. 93: 7252-7257, 1996.
5. Thurston, T. L. M.; Wandel, M. P.; von Muhlinen, N.; Foeglein,
A.; Randow, F.: Galectin 8 targets damaged vesicles for autophagy
to defend cells against bacterial invasion. Nature 482: 414-418,
2012.
*FIELD* CN
Ada Hamosh - updated: 2/27/2012
Paul J. Converse - updated: 5/18/2010
*FIELD* CD
Paul J. Converse: 7/11/2001
*FIELD* ED
alopez: 02/28/2012
terry: 2/27/2012
mgross: 5/18/2010
terry: 5/18/2010
mgross: 7/11/2001
*RECORD*
*FIELD* NO
606099
*FIELD* TI
*606099 LECTIN, GALACTOSIDE-BINDING, SOLUBLE, 8; LGALS8
;;GALECTIN 8;;
PROSTATE CARCINOMA TUMOR ANTIGEN 1; PCTA1
read more*FIELD* TX
DESCRIPTION
Galectins, such as LGALS8, are beta-galactoside-binding animal lectins
with conserved carbohydrate recognition domains (CRDs). Galectins are
involved in various biologic processes, including cell signaling,
proliferative control, cell adhesion, and cell migration (summary by Su
et al. (1996) and Gopalkrishnan et al. (2000)).
CLONING
By surface-epitope masking and expression cloning using a prostate
cancer cDNA library, Su et al. (1996) isolated a cDNA encoding LGALS8,
which they called PCTA1. The deduced 317-amino acid protein is 81%
homologous to rat galectin-8 (Hadari et al., 1995), which contains 2
CRDs.
By Northern blot analysis, Gopalkrishnan et al. (2000) detected wide but
variable expression of 3 major LGALS8 transcripts of 1.6, 2.6, and 6.0
kb in normal tissue. Fluorescence microscopy demonstrated cytoplasmic
expression.
GENE FUNCTION
Using RT-PCR analysis, Su et al. (1996) detected expression of LGALS8 in
all 7 prostate carcinomas tested, but in only in 1 of 4 benign prostatic
hypertrophy samples tested.
By screening for innate proteins that could recognize human blood group
antigens, Stowell et al. (2010) identified GAL4 (LGALS4; 602518) and
GAL8, both of which are expressed in the intestinal tract, as proteins
that recognized and killed E. coli expressing blood group antigen, but
not bacteria that did not express such antigens. Video, fluorescence,
and electron microscopy showed that bacterial cells lost motility and
membrane integrity upon treatment with these lectins. Mutation analysis
indicated that the killing activity was mediated by the C-terminal
domains of GAL4 and GAL8 in a rapid, complement-independent manner.
Stowell et al. (2010) concluded that innate defense lectins provide
immunity against pathogens expressing blood group-like antigens on their
surface.
Thurston et al. (2012) demonstrated in human cells that galectin-8, a
cytosolic lectin also known as LGALS8, is a danger receptor that
restricts Salmonella proliferation. Galectin-8 monitors endosomal and
lysosomal integrity and detects bacterial invasion by binding host
glycans exposed on damaged Salmonella-containing vacuoles. By recruiting
NDP52 (CALCOCO2; 604587), galectin-8 activates antibacterial autophagy.
Galectin-8-dependent recruitment of NDP52 to Salmonella-containing
vesicles is transient and followed by ubiquitin-dependent NDP52
recruitment. Because galectin-8 also detects sterile damage to endosomes
or lysosomes, as well as invasion by Listeria or Shigella, Thurston et
al. (2012) suggested that galectin-8 serves as a versatile receptor for
vesicle-damaging pathogens. The results of Thurston et al. (2012) also
illustrated how cells deploy the danger receptor galectin-8 to combat
infection by monitoring endosomal and lysosomal integrity on the basis
of the specific lack of complex carbohydrates in the cytosol.
GENE STRUCTURE
By genomic sequence analysis, Gopalkrishnan et al. (2000) determined
that the LGALS8 gene contains a TATA box and 10 exons, 8 of which are
expressed constitutively. The additional exons, 7-prime and
7-double-prime, are present in splice variants.
MAPPING
By radiation hybrid analysis, Gopalkrishnan et al. (2000) mapped the
LGALS8 gene to chromosome 1q42-q43, a region that contains a gene
predisposing to early-onset prostate cancer (PCAP; 602759).
*FIELD* RF
1. Gopalkrishnan, R. V.; Roberts, T.; Tuli, S.; Kang, D.; Christiansen,
K. A.; Fisher, P. B.: Molecular characterization of prostate carcinoma
tumor antigen-1, PCTA-1, a human Galectin-8 related gene. Oncogene 19:
4405-4416, 2000.
2. Hadari, Y. R.; Paz, K.; Dekel, R.; Mestrovic, T.; Accili, D.; Zick,
Y.: Galectin-8: a new rat lectin, related to galectin-4. J. Biol.
Chem. 270: 3447-3453, 1995.
3. Stowell, S. R.; Arthur, C. M.; Dias-Baruffi, M.; Rodrigues, L.
C.; Gourdine, J.-P.; Heimburg-Molinaro, J.; Ju, T.; Molinaro, R. J.;
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*FIELD* CN
Ada Hamosh - updated: 2/27/2012
Paul J. Converse - updated: 5/18/2010
*FIELD* CD
Paul J. Converse: 7/11/2001
*FIELD* ED
alopez: 02/28/2012
terry: 2/27/2012
mgross: 5/18/2010
terry: 5/18/2010
mgross: 7/11/2001