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Galectin-8 (Gal-8) (Po66 carbohydrate-binding protein) (Po66-CBP) (Prostate carcinoma tumor antigen 1) (PCTA-1)

 LEG8_HUMAN              Reviewed;         317 AA.
O00214; O15215; Q5T3P5; Q5T3Q4; Q8TEV1; Q96B92; Q9BXC8; Q9H584;
Q9H585; Q9UEZ6; Q9UP32; Q9UP33; Q9UP34;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
23-MAR-2010, sequence version 4.
18-JUL-2018, entry version 178.
RecName: Full=Galectin-8 {ECO:0000303|Ref.2};
Short=Gal-8;
AltName: Full=Po66 carbohydrate-binding protein;
Short=Po66-CBP;
AltName: Full=Prostate carcinoma tumor antigen 1 {ECO:0000303|PubMed:8692978};
Short=PCTA-1 {ECO:0000303|PubMed:8692978};
Name=LGALS8 {ECO:0000312|HGNC:HGNC:6569};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-56 AND
SER-184.
TISSUE=Prostate;
PubMed=8692978; DOI=10.1073/pnas.93.14.7252;
Su Z.-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. Natl. Acad. Sci. U.S.A. 93:7252-7257(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Hippocampus;
Hadari Y.R., Eisenstein M., Zakut R., Zick Y.;
"Galectin-8: on the road from structure to function.";
Trends Glycosci. Glycotechnol. 9:103-112(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING,
AND VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
TISSUE=Lung carcinoma;
Brichory F., Bidon N., Desrues B., Bourguet P., Le Pennec J.-P.,
Dazord L.;
"Molecular cloning of a beta-galactoside-binding lectin related to
galectin-8 and identified in human lung carcinoma.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TYR-19; CYS-36; VAL-56
AND SER-184.
Maier C., Haeussler J., Roesch K., Moschgath E., Vogel W.;
"Genomic organization and expression of the human galectin-8 gene.";
Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10980616; DOI=10.1038/sj.onc.1203767;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon carcinoma;
Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B.,
Kaltner H., Wolf E., Gabius H.-J.;
"Coca (colorectal carcinoma-derived) galectin-8 variant I full-length
cDNA from a human colorectal carcinoma cell line.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Colon carcinoma;
Lahm H., Siebert H.-C., Andre S., Hoeflich A., Diehl D., Sordat B.,
Kaltner H., Wolf E., Gabius H.-J.;
"Coca (Colorectal carcinoma-derived) galectin-8 variant II.";
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS TYR-19; CYS-36
AND VAL-56.
Moisan S., Mercier J., Demers M., Belanger S.D., Alain T.,
Kossakowska A.E., Potworowski E.F., St-Pierre Y.;
"Galectins in murine and human non-Hodgkin's lymphomas.";
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS TYR-19; CYS-36; VAL-56 AND SER-184.
TISSUE=Brain, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
INTERACTION WITH PDPN.
PubMed=19268462; DOI=10.1016/j.yexcr.2009.02.021;
Cueni L.N., Detmar M.;
"Galectin-8 interacts with podoplanin and modulates lymphatic
endothelial cell functions.";
Exp. Cell Res. 315:1715-1723(2009).
[12]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CALCOCO2, AND
MUTAGENESIS OF ARG-69 AND ARG-190.
PubMed=22246324; DOI=10.1038/nature10744;
Thurston T.L., 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).
[13]
FUNCTION.
PubMed=28077878; DOI=10.1038/nature21032;
Staring J., von Castelmur E., Blomen V.A., van den Hengel L.G.,
Brockmann M., Baggen J., Thibaut H.J., Nieuwenhuis J., Janssen H.,
van Kuppeveld F.J., Perrakis A., Carette J.E., Brummelkamp T.R.;
"PLA2G16 represents a switch between entry and clearance of
Picornaviridae.";
Nature 541:412-416(2017).
[14]
STRUCTURE BY NMR OF 176-317.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the C-terminal Gal-bind lectin protein from
human galectin-8.";
Submitted (FEB-2008) to the PDB data bank.
[15]
X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-152 IN COMPLEX WITH
LACTOSE.
RIKEN structural genomics initiative (RSGI);
"Crystal structure of N-terminal domain of human galectin-8.";
Submitted (MAY-2008) to the PDB data bank.
[16]
X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 1-154 ALONE AND IN COMPLEX
WITH CARBOHYDRATES, FUNCTION, AND SUBUNIT.
PubMed=21288902; DOI=10.1074/jbc.M110.195925;
Ideo H., Matsuzaka T., Nonaka T., Seko A., Yamashita K.;
"Galectin-8-N-domain recognition mechanism for sialylated and sulfated
glycans.";
J. Biol. Chem. 286:11346-11355(2011).
-!- FUNCTION: Beta-galactoside-binding lectin that acts as a sensor of
membrane damage caused by infection and restricts the
proliferation of infecting pathogens by targeting them for
autophagy (PubMed:22246324, PubMed:28077878). Detects membrane
rupture by binding beta-galactoside ligands located on the lumenal
side of the endosome membrane; these ligands becoming exposed to
the cytoplasm following rupture (PubMed:22246324,
PubMed:28077878). Restricts infection by initiating autophagy via
interaction with CALCOCO2/NDP52 (PubMed:22246324,
PubMed:28077878). Required to restrict infection of bacterial
invasion such as S.typhimurium (PubMed:22246324). Also required to
restrict infection of Picornaviridae viruses (PubMed:28077878).
Has a marked preference for 3'-O-sialylated and 3'-O-sulfated
glycans (PubMed:21288902). {ECO:0000269|PubMed:21288902,
ECO:0000269|PubMed:22246324, ECO:0000269|PubMed:28077878}.
-!- SUBUNIT: Homodimer (PubMed:21288902, Ref.15). Interacts with
CALCOCO2/NDP52 (PubMed:22246324). Interacts with PDPN; the
interaction is glycosylation-dependent; may participate to
connection of the lymphatic endothelium to the surrounding
extracellular matrix. {ECO:0000269|PubMed:21288902,
ECO:0000269|PubMed:22246324, ECO:0000269|Ref.15}.
-!- INTERACTION:
P13798:APEH; NbExp=3; IntAct=EBI-740058, EBI-723792;
Q13137:CALCOCO2; NbExp=4; IntAct=EBI-740058, EBI-739580;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-740058, EBI-10172526;
Q86VP1:TAX1BP1; NbExp=3; IntAct=EBI-740058, EBI-529518;
Q15583:TGIF1; NbExp=10; IntAct=EBI-740058, EBI-714215;
P36406:TRIM23; NbExp=3; IntAct=EBI-740058, EBI-740098;
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle
{ECO:0000269|PubMed:22246324}. Cytoplasm, cytosol
{ECO:0000269|PubMed:22246324}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=I;
IsoId=O00214-1; Sequence=Displayed;
Name=2;
IsoId=O00214-2; Sequence=VSP_003094;
Note=Ref.8 (AAL77076) sequence is in conflict in position:
220:M->T. {ECO:0000305};
-!- TISSUE SPECIFICITY: Ubiquitous. Selective expression by prostate
carcinomas versus normal prostate and benign prostatic
hypertrophy.
-!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
domains.
-!- SEQUENCE CAUTION:
Sequence=AAB51605.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD45402.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD45403.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD45404.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAD45404.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
Sequence=AAH15818.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH16486.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-8 C-terminal CRD;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_832";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-8 long isoform;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_833";
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-8 long isoform;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_other_834";
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EMBL; L78132; AAB51605.1; ALT_INIT; mRNA.
EMBL; X91790; CAA62904.1; -; mRNA.
EMBL; AF074000; AAD45402.1; ALT_INIT; mRNA.
EMBL; AF074001; AAD45403.1; ALT_INIT; mRNA.
EMBL; AF074002; AAD45404.1; ALT_SEQ; mRNA.
EMBL; AF193806; AAF19370.1; -; Genomic_DNA.
EMBL; AF193805; AAF19370.1; JOINED; Genomic_DNA.
EMBL; AF342815; AAK16735.1; -; mRNA.
EMBL; AF342816; AAK16736.1; -; mRNA.
EMBL; AF468213; AAL77076.1; -; mRNA.
EMBL; AL359921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015818; AAH15818.1; ALT_INIT; mRNA.
EMBL; BC016486; AAH16486.2; ALT_INIT; mRNA.
CCDS; CCDS1611.1; -. [O00214-2]
CCDS; CCDS1612.1; -. [O00214-1]
PIR; JC6147; JC6147.
RefSeq; NP_006490.3; NM_006499.4. [O00214-2]
RefSeq; NP_963837.1; NM_201543.2. [O00214-1]
RefSeq; NP_963838.1; NM_201544.2. [O00214-1]
RefSeq; NP_963839.1; NM_201545.2. [O00214-2]
UniGene; Hs.4082; -.
UniGene; Hs.708114; -.
UniGene; Hs.735982; -.
PDB; 2YRO; NMR; -; A=176-317.
PDB; 2YV8; X-ray; 1.92 A; A=1-152.
PDB; 2YXS; X-ray; 2.13 A; A=1-152.
PDB; 3AP4; X-ray; 2.33 A; A/B/C/D=1-154.
PDB; 3AP5; X-ray; 1.92 A; A=1-154.
PDB; 3AP6; X-ray; 1.58 A; A/B/C/D=1-154.
PDB; 3AP7; X-ray; 1.53 A; A=1-154.
PDB; 3AP9; X-ray; 1.33 A; A=1-154.
PDB; 3APB; X-ray; 1.95 A; A/B=1-154.
PDB; 3OJB; X-ray; 3.01 A; A/B/C/D=186-315.
PDB; 3VKL; X-ray; 2.55 A; A/B=1-155, A/B=184-317.
PDB; 3VKM; X-ray; 2.98 A; A/B=1-155, A/B=184-317.
PDB; 3VKN; X-ray; 1.98 A; A/B=1-153.
PDB; 3VKO; X-ray; 2.08 A; A/B=1-153.
PDB; 4BMB; X-ray; 1.35 A; A=4-153.
PDB; 4BME; X-ray; 2.00 A; A/B=4-155.
PDB; 4FQZ; X-ray; 2.80 A; A=1-155, A=184-317.
PDB; 4GXL; X-ray; 2.02 A; A=186-317.
PDB; 4HAN; X-ray; 2.55 A; A/B=1-155, A/B=184-317.
PDB; 5GZC; X-ray; 1.08 A; A=7-158.
PDB; 5GZD; X-ray; 1.19 A; A=7-154.
PDB; 5GZE; X-ray; 1.32 A; A=7-154.
PDB; 5GZF; X-ray; 2.00 A; A=1-186.
PDB; 5GZG; X-ray; 2.00 A; A=1-186.
PDB; 5T7I; X-ray; 2.00 A; A=1-155.
PDB; 5T7S; X-ray; 1.90 A; A=1-155.
PDB; 5T7T; X-ray; 1.96 A; A=1-155.
PDB; 5T7U; X-ray; 1.58 A; A=1-155.
PDB; 5VWG; X-ray; 2.10 A; A=1-155.
PDBsum; 2YRO; -.
PDBsum; 2YV8; -.
PDBsum; 2YXS; -.
PDBsum; 3AP4; -.
PDBsum; 3AP5; -.
PDBsum; 3AP6; -.
PDBsum; 3AP7; -.
PDBsum; 3AP9; -.
PDBsum; 3APB; -.
PDBsum; 3OJB; -.
PDBsum; 3VKL; -.
PDBsum; 3VKM; -.
PDBsum; 3VKN; -.
PDBsum; 3VKO; -.
PDBsum; 4BMB; -.
PDBsum; 4BME; -.
PDBsum; 4FQZ; -.
PDBsum; 4GXL; -.
PDBsum; 4HAN; -.
PDBsum; 5GZC; -.
PDBsum; 5GZD; -.
PDBsum; 5GZE; -.
PDBsum; 5GZF; -.
PDBsum; 5GZG; -.
PDBsum; 5T7I; -.
PDBsum; 5T7S; -.
PDBsum; 5T7T; -.
PDBsum; 5T7U; -.
PDBsum; 5VWG; -.
ProteinModelPortal; O00214; -.
SMR; O00214; -.
BioGrid; 110155; 114.
IntAct; O00214; 11.
MINT; O00214; -.
BindingDB; O00214; -.
ChEMBL; CHEMBL5475; -.
UniLectin; O00214; -.
iPTMnet; O00214; -.
PhosphoSitePlus; O00214; -.
BioMuta; LGALS8; -.
EPD; O00214; -.
MaxQB; O00214; -.
PeptideAtlas; O00214; -.
PRIDE; O00214; -.
ProteomicsDB; 47785; -.
ProteomicsDB; 47786; -. [O00214-2]
DNASU; 3964; -.
Ensembl; ENST00000341872; ENSP00000342139; ENSG00000116977. [O00214-1]
Ensembl; ENST00000352231; ENSP00000309576; ENSG00000116977. [O00214-2]
Ensembl; ENST00000366584; ENSP00000355543; ENSG00000116977. [O00214-1]
Ensembl; ENST00000450372; ENSP00000408657; ENSG00000116977. [O00214-2]
Ensembl; ENST00000526589; ENSP00000435460; ENSG00000116977. [O00214-2]
Ensembl; ENST00000526634; ENSP00000437040; ENSG00000116977. [O00214-1]
Ensembl; ENST00000527974; ENSP00000431398; ENSG00000116977. [O00214-2]
GeneID; 3964; -.
KEGG; hsa:3964; -.
UCSC; uc001hxw.3; human. [O00214-1]
CTD; 3964; -.
DisGeNET; 3964; -.
EuPathDB; HostDB:ENSG00000116977.18; -.
GeneCards; LGALS8; -.
HGNC; HGNC:6569; LGALS8.
HPA; HPA012734; -.
HPA; HPA030491; -.
MIM; 606099; gene.
neXtProt; NX_O00214; -.
OpenTargets; ENSG00000116977; -.
PharmGKB; PA30346; -.
GeneTree; ENSGT00760000119105; -.
HOVERGEN; HBG002412; -.
InParanoid; O00214; -.
KO; K06832; -.
OMA; HASDYFK; -.
OrthoDB; EOG091G0WP8; -.
PhylomeDB; O00214; -.
TreeFam; TF315551; -.
ChiTaRS; LGALS8; human.
EvolutionaryTrace; O00214; -.
GeneWiki; Galectin-8; -.
GeneWiki; LGALS8; -.
GenomeRNAi; 3964; -.
PRO; PR:O00214; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116977; -.
ExpressionAtlas; O00214; baseline and differential.
Genevisible; O00214; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:GO_Central.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IDA:GO_Central.
GO; GO:0005178; F:integrin binding; IPI:UniProtKB.
GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
GO; GO:1904977; P:lymphatic endothelial cell migration; IDA:UniProtKB.
GO; GO:0098792; P:xenophagy; IMP:UniProtKB.
CDD; cd00070; GLECT; 2.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR030638; Galectin_8.
InterPro; IPR001079; Galectin_CRD.
PANTHER; PTHR11346:SF22; PTHR11346:SF22; 1.
Pfam; PF00337; Gal-bind_lectin; 2.
SMART; SM00908; Gal-bind_lectin; 2.
SMART; SM00276; GLECT; 2.
SUPFAM; SSF49899; SSF49899; 2.
PROSITE; PS51304; GALECTIN; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autophagy; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Lectin; Polymorphism;
Reference proteome; Repeat.
CHAIN 1 317 Galectin-8.
/FTId=PRO_0000076943.
DOMAIN 19 152 Galectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
DOMAIN 187 317 Galectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 249 255 Beta-galactoside binding. {ECO:0000250}.
BINDING 69 69 Carbohydrate.
{ECO:0000269|PubMed:21288902}.
BINDING 79 79 Carbohydrate.
{ECO:0000269|PubMed:21288902}.
BINDING 89 89 Carbohydrate.
{ECO:0000269|PubMed:21288902}.
SITE 59 59 Critical for binding to sialylated and
sulfated oligosaccharides.
{ECO:0000269|PubMed:21288902}.
VAR_SEQ 183 183 L -> LPSNRGGDISKIAPRTVYTKSKDSTVNHTLTCTKIP
PMNYVSK (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3, ECO:0000303|Ref.7,
ECO:0000303|Ref.8}.
/FTId=VSP_003094.
VARIANT 19 19 F -> Y (in dbSNP:rs1126407).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3, ECO:0000269|Ref.4,
ECO:0000269|Ref.8}.
/FTId=VAR_012990.
VARIANT 36 36 R -> C (in dbSNP:rs1041935).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3, ECO:0000269|Ref.4,
ECO:0000269|Ref.8}.
/FTId=VAR_009710.
VARIANT 56 56 M -> V (in dbSNP:rs1041937).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8692978,
ECO:0000269|Ref.3, ECO:0000269|Ref.4,
ECO:0000269|Ref.8}.
/FTId=VAR_012991.
VARIANT 184 184 R -> S (in dbSNP:rs2243525).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8692978,
ECO:0000269|Ref.3, ECO:0000269|Ref.4}.
/FTId=VAR_063506.
MUTAGEN 69 69 R->H: Abolishes localization to
cytoplasmic vesicles in case of infection
by S.typhimurium.
{ECO:0000269|PubMed:22246324}.
MUTAGEN 190 190 R->H: Does not affect localization to
cytoplasmic vesicles in case of infection
by S.typhimurium.
{ECO:0000269|PubMed:22246324}.
CONFLICT 14 14 N -> S (in Ref. 8; AAL77076).
{ECO:0000305}.
CONFLICT 98 100 KRE -> QKEK (in Ref. 2; CAA62904).
{ECO:0000305}.
CONFLICT 112 112 D -> A (in Ref. 2; CAA62904).
{ECO:0000305}.
CONFLICT 171 171 S -> V (in Ref. 1; AAB51605).
{ECO:0000305}.
CONFLICT 199 199 R -> G (in Ref. 8; AAL77076).
{ECO:0000305}.
CONFLICT 204 204 K -> Q (in Ref. 1; AAB51605).
{ECO:0000305}.
CONFLICT 225 225 D -> H (in Ref. 8; AAL77076).
{ECO:0000305}.
CONFLICT 259 259 F -> L (in Ref. 7; AAK16736).
{ECO:0000305}.
STRAND 4 6 {ECO:0000244|PDB:4FQZ}.
STRAND 9 14 {ECO:0000244|PDB:5GZC}.
STRAND 17 22 {ECO:0000244|PDB:5GZC}.
STRAND 32 38 {ECO:0000244|PDB:5GZC}.
STRAND 44 53 {ECO:0000244|PDB:5GZC}.
TURN 56 59 {ECO:0000244|PDB:5GZC}.
STRAND 61 69 {ECO:0000244|PDB:5GZC}.
STRAND 75 82 {ECO:0000244|PDB:5GZC}.
STRAND 90 92 {ECO:0000244|PDB:5GZC}.
STRAND 102 109 {ECO:0000244|PDB:5GZC}.
STRAND 111 118 {ECO:0000244|PDB:5GZC}.
STRAND 121 127 {ECO:0000244|PDB:5GZC}.
HELIX 132 134 {ECO:0000244|PDB:5GZC}.
STRAND 137 143 {ECO:0000244|PDB:5GZC}.
STRAND 145 152 {ECO:0000244|PDB:5GZC}.
STRAND 186 190 {ECO:0000244|PDB:4GXL}.
STRAND 200 207 {ECO:0000244|PDB:4GXL}.
STRAND 213 220 {ECO:0000244|PDB:4GXL}.
TURN 221 224 {ECO:0000244|PDB:4GXL}.
STRAND 225 233 {ECO:0000244|PDB:4GXL}.
TURN 234 237 {ECO:0000244|PDB:4GXL}.
STRAND 238 245 {ECO:0000244|PDB:4GXL}.
STRAND 253 257 {ECO:0000244|PDB:4FQZ}.
STRAND 266 273 {ECO:0000244|PDB:4GXL}.
STRAND 275 282 {ECO:0000244|PDB:4GXL}.
STRAND 285 291 {ECO:0000244|PDB:4GXL}.
HELIX 297 299 {ECO:0000244|PDB:4GXL}.
STRAND 302 317 {ECO:0000244|PDB:4GXL}.
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


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