LEG4_HUMAN
ID LEG4_HUMAN Reviewed; 323 AA.
AC P56470;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Galectin-4;
DE Short=Gal-4;
DE AltName: Full=Antigen NY-CO-27;
DE AltName: Full=L-36 lactose-binding protein;
DE Short=L36LBP;
DE AltName: Full=Lactose-binding lectin 4;
GN Name=LGALS4;
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].
RC TISSUE=Gastric carcinoma;
RA Kato S.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon carcinoma;
RX PubMed=9310382; DOI=10.1111/j.1432-1033.1997.00225.x;
RA Rechreche H., Mallo G.V., Montalto G., Dagorn J.-C., Iovanna J.L.;
RT "Cloning and expression of the mRNA of human galectin-4, an S-type lectin
RT down-regulated in colorectal cancer.";
RL Eur. J. Biochem. 248:225-230(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9162064; DOI=10.1074/jbc.272.22.14294;
RA Huflejt M.E., Jordan E.T., Gitt M.A., Barondes S.H., Leffler H.;
RT "Strikingly different localization of galectin-3 and galectin-4 in human
RT colon adenocarcinoma T84 cells. Galectin-4 is localized at sites of cell
RT adhesion.";
RL J. Biol. Chem. 272:14294-14303(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, 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 [5]
RP STRUCTURE BY NMR OF 173-323.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C-terminal Gal-bind lectin domain from human
RT galectin-4.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Galectin that binds lactose and a related range of sugars.
CC May be involved in the assembly of adherens junctions.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC P56470; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-720805, EBI-11524452;
CC P56470; Q53EZ4: CEP55; NbExp=3; IntAct=EBI-720805, EBI-747776;
CC P56470; O00167-2: EYA2; NbExp=3; IntAct=EBI-720805, EBI-12807776;
CC P56470; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-720805, EBI-5916454;
CC P56470; P49639: HOXA1; NbExp=3; IntAct=EBI-720805, EBI-740785;
CC P56470; O75031: HSF2BP; NbExp=3; IntAct=EBI-720805, EBI-7116203;
CC P56470; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-720805, EBI-1052037;
CC P56470; Q9NZQ3-3: NCKIPSD; NbExp=3; IntAct=EBI-720805, EBI-10963850;
CC P56470; Q8HWS3: RFX6; NbExp=3; IntAct=EBI-720805, EBI-746118;
CC P56470; Q6N022: TENM4; NbExp=3; IntAct=EBI-720805, EBI-12827077;
CC P56470; Q96NM4-3: TOX2; NbExp=3; IntAct=EBI-720805, EBI-12815137;
CC -!- DOMAIN: Contains two homologous but distinct carbohydrate-binding
CC domains.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Galectin-4;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00119";
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DR EMBL; AB006781; BAA22165.1; -; mRNA.
DR EMBL; AF014838; AAC51763.1; -; mRNA.
DR EMBL; U82953; AAB86590.1; -; mRNA.
DR EMBL; BC003661; AAH03661.1; -; mRNA.
DR EMBL; BC005146; AAH05146.1; -; mRNA.
DR EMBL; BC034750; AAH34750.1; -; mRNA.
DR CCDS; CCDS12521.1; -.
DR RefSeq; NP_006140.1; NM_006149.3.
DR PDB; 1X50; NMR; -; A=173-323.
DR PDB; 4XZP; X-ray; 1.48 A; A=1-152.
DR PDB; 4YLZ; X-ray; 2.10 A; A/B/C/D=171-323.
DR PDB; 4YM0; X-ray; 2.30 A; A/B/C/D=171-323.
DR PDB; 4YM1; X-ray; 2.00 A; A/B/C/D=171-323.
DR PDB; 4YM2; X-ray; 2.10 A; A/B/C/D=171-323.
DR PDB; 4YM3; X-ray; 1.89 A; A/B/C/D=171-323.
DR PDB; 5CBL; X-ray; 1.78 A; A/B/C/D=179-323.
DR PDB; 5DUU; X-ray; 2.00 A; A/B/C/D=1-155.
DR PDB; 5DUV; X-ray; 1.90 A; A/B/C/D=1-155.
DR PDB; 5DUW; X-ray; 1.70 A; A/B/C/D=1-155.
DR PDB; 5DUX; X-ray; 1.85 A; A/B/C/D=1-155.
DR PDB; 6WAB; X-ray; 2.28 A; A/B/C/D=184-323.
DR PDBsum; 1X50; -.
DR PDBsum; 4XZP; -.
DR PDBsum; 4YLZ; -.
DR PDBsum; 4YM0; -.
DR PDBsum; 4YM1; -.
DR PDBsum; 4YM2; -.
DR PDBsum; 4YM3; -.
DR PDBsum; 5CBL; -.
DR PDBsum; 5DUU; -.
DR PDBsum; 5DUV; -.
DR PDBsum; 5DUW; -.
DR PDBsum; 5DUX; -.
DR PDBsum; 6WAB; -.
DR AlphaFoldDB; P56470; -.
DR SMR; P56470; -.
DR BioGRID; 110151; 17.
DR IntAct; P56470; 16.
DR STRING; 9606.ENSP00000302100; -.
DR BindingDB; P56470; -.
DR ChEMBL; CHEMBL1671608; -.
DR UniLectin; P56470; -.
DR iPTMnet; P56470; -.
DR PhosphoSitePlus; P56470; -.
DR BioMuta; LGALS4; -.
DR DMDM; 3024079; -.
DR jPOST; P56470; -.
DR MassIVE; P56470; -.
DR PaxDb; P56470; -.
DR PeptideAtlas; P56470; -.
DR PRIDE; P56470; -.
DR ProteomicsDB; 56919; -.
DR Antibodypedia; 30166; 380 antibodies from 35 providers.
DR DNASU; 3960; -.
DR Ensembl; ENST00000307751.9; ENSP00000302100.3; ENSG00000171747.9.
DR Ensembl; ENST00000634573.2; ENSP00000489411.1; ENSG00000282992.2.
DR GeneID; 3960; -.
DR KEGG; hsa:3960; -.
DR MANE-Select; ENST00000307751.9; ENSP00000302100.3; NM_006149.4; NP_006140.1.
DR CTD; 3960; -.
DR DisGeNET; 3960; -.
DR GeneCards; LGALS4; -.
DR HGNC; HGNC:6565; LGALS4.
DR HPA; ENSG00000171747; Tissue enriched (intestine).
DR MIM; 602518; gene.
DR neXtProt; NX_P56470; -.
DR OpenTargets; ENSG00000171747; -.
DR PharmGKB; PA30342; -.
DR VEuPathDB; HostDB:ENSG00000171747; -.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000160378; -.
DR HOGENOM; CLU_037794_1_0_1; -.
DR InParanoid; P56470; -.
DR OMA; HWGGRFY; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; P56470; -.
DR TreeFam; TF315551; -.
DR PathwayCommons; P56470; -.
DR SignaLink; P56470; -.
DR BioGRID-ORCS; 3960; 15 hits in 1066 CRISPR screens.
DR ChiTaRS; LGALS4; human.
DR EvolutionaryTrace; P56470; -.
DR GeneWiki; LGALS4; -.
DR GenomeRNAi; 3960; -.
DR Pharos; P56470; Tchem.
DR PRO; PR:P56470; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P56470; protein.
DR Bgee; ENSG00000171747; Expressed in mucosa of transverse colon and 94 other tissues.
DR ExpressionAtlas; P56470; baseline and differential.
DR Genevisible; P56470; HS.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; TAS:ProtInc.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
DR GO; GO:0016936; F:galactoside binding; IEA:Ensembl.
DR GO; GO:0002780; P:antibacterial peptide biosynthetic process; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR CDD; cd00070; GLECT; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR015533; Galectin4/6.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF32; PTHR11346:SF32; 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; Lectin; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..323
FT /note="Galectin-4"
FT /id="PRO_0000076934"
FT DOMAIN 19..150
FT /note="Galectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT DOMAIN 194..323
FT /note="Galectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT BINDING 256..262
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38552"
FT VARIANT 16
FT /note="T -> M (in dbSNP:rs8106404)"
FT /id="VAR_049769"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 46..55
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 119..125
FT /evidence="ECO:0007829|PDB:4XZP"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 135..150
FT /evidence="ECO:0007829|PDB:4XZP"
FT STRAND 187..189
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:5CBL"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:4YM3"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:5CBL"
FT TURN 241..244
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 282..289
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:4YM3"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 309..315
FT /evidence="ECO:0007829|PDB:5CBL"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:5CBL"
SQ SEQUENCE 323 AA; 35941 MW; E79EC0A9AB3990EF CRC64;
MAYVPAPGYQ PTYNPTLPYY QPIPGGLNVG MSVYIQGVAS EHMKRFFVNF VVGQDPGSDV
AFHFNPRFDG WDKVVFNTLQ GGKWGSEERK RSMPFKKGAA FELVFIVLAE HYKVVVNGNP
FYEYGHRLPL QMVTHLQVDG DLQLQSINFI GGQPLRPQGP PMMPPYPGPG HCHQQLNSLP
TMEGPPTFNP PVPYFGRLQG GLTARRTIII KGYVPPTGKS FAINFKVGSS GDIALHINPR
MGNGTVVRNS LLNGSWGSEE KKITHNPFGP GQFFDLSIRC GLDRFKVYAN GQHLFDFAHR
LSAFQRVDTL EIQGDVTLSY VQI
