LEG3_MOUSE
ID LEG3_MOUSE Reviewed; 264 AA.
AC P16110;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Galectin-3;
DE Short=Gal-3;
DE AltName: Full=35 kDa lectin;
DE AltName: Full=Carbohydrate-binding protein 35;
DE Short=CBP 35;
DE AltName: Full=Galactose-specific lectin 3;
DE AltName: Full=IgE-binding protein;
DE AltName: Full=L-34 galactoside-binding lectin;
DE AltName: Full=Laminin-binding protein;
DE AltName: Full=Lectin L-29;
DE AltName: Full=Mac-2 antigen;
GN Name=Lgals3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=DBA/2J; TISSUE=Macrophage;
RX PubMed=2584931; DOI=10.1084/jem.170.6.1959;
RA Cherayil B.J., Weiner S.J., Pillai S.;
RT "The Mac-2 antigen is a galactose-specific lectin that binds IgE.";
RL J. Exp. Med. 170:1959-1972(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3360772; DOI=10.1016/s0021-9258(18)68739-3;
RA Jia S., Wang J.L.;
RT "Carbohydrate binding protein 35. Complementary DNA sequence reveals
RT homology with proteins of the heterogeneous nuclear RNP.";
RL J. Biol. Chem. 263:6009-6011(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2525069;
RA Raz A., Pazerini G., Carmi P.;
RT "Identification of the metastasis-associated, galactoside-binding lectin as
RT a chimeric gene product with homology to an IgE-binding protein.";
RL Cancer Res. 49:3489-3493(1989).
RN [4]
RP PROTEIN SEQUENCE OF 159-163; 166-175 AND 214-226.
RX PubMed=2332426; DOI=10.1016/s0021-9258(19)39081-7;
RA Woo H.-J., Shaw L.M., Messier J.M., Mercurio A.M.;
RT "The major non-integrin laminin binding protein of macrophages is identical
RT to carbohydrate binding protein 35 (Mac-2).";
RL J. Biol. Chem. 265:7097-7099(1990).
RN [5]
RP PROTEIN SEQUENCE OF 184-190 AND 201-213, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
RP DISULFIDE BOND.
RX PubMed=1917966; DOI=10.1016/s0021-9258(18)55075-4;
RA Woo H.-J., Lotz M.M., Jung J.U., Mercurio A.M.;
RT "Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin, forms
RT functional dimers using cysteine 186.";
RL J. Biol. Chem. 266:18419-18422(1991).
RN [7]
RP INTERACTION WITH CYHR1.
RX PubMed=10745073; DOI=10.1016/s0014-5793(00)01310-7;
RA Menon R.P., Strom M., Hughes R.C.;
RT "Interaction of a novel cysteine and histidine-rich cytoplasmic protein
RT with galectin-3 in a carbohydrate-independent manner galectin 3.";
RL FEBS Lett. 470:227-231(2000).
RN [8]
RP INTERACTION WITH UACA.
RX PubMed=14961764; DOI=10.1042/bj20031300;
RA Liu L., Sakai T., Sano N., Fukui K.;
RT "Nucling mediates apoptosis by inhibiting expression of galectin-3 through
RT interference with nuclear factor kappaB signalling.";
RL Biochem. J. 380:31-41(2004).
RN [9]
RP SUBCELLULAR LOCATION, INTERACTION WITH ITGB1; ITGA3 AND CSPG4, AND
RP FUNCTION.
RX PubMed=15181153; DOI=10.1091/mbc.e04-03-0236;
RA Fukushi J., Makagiansar I.T., Stallcup W.B.;
RT "NG2 proteoglycan promotes endothelial cell motility and angiogenesis via
RT engagement of galectin-3 and alpha3beta1 integrin.";
RL Mol. Biol. Cell 15:3580-3590(2004).
RN [10]
RP SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
RX PubMed=16473834; DOI=10.1093/glycob/cwj089;
RA Li S.Y., Davidson P.J., Lin N.Y., Patterson R.J., Wang J.L., Arnoys E.J.;
RT "Transport of galectin-3 between the nucleus and cytoplasm. II.
RT Identification of the signal for nuclear export.";
RL Glycobiology 16:612-622(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Galactose-specific lectin which binds IgE. May mediate with
CC the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial
CC cells migration. Together with DMBT1, required for terminal
CC differentiation of columnar epithelial cells during early
CC embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor.
CC Involved in acute inflammatory responses including neutrophil
CC activation and adhesion, chemoattraction of monocytes macrophages,
CC opsonization of apoptotic neutrophils, and activation of mast cells.
CC Together with TRIM16, coordinates the recognition of membrane damage
CC with mobilization of the core autophagy regulators ATG16L1 and BECN1 in
CC response to damaged endomembranes. {ECO:0000250,
CC ECO:0000269|PubMed:15181153}.
CC -!- SUBUNIT: Probably forms homo- or heterodimers. Interacts with DMBT1 (By
CC similarity). Interacts with CD6 and ALCAM. Forms a complex with the
CC ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP, LYPD3, CYHR1 and UACA.
CC Interacts with TRIM16; this interaction mediates autophagy of damage
CC endomembranes (By similarity). {ECO:0000250|UniProtKB:P08699,
CC ECO:0000250|UniProtKB:P17931, ECO:0000269|PubMed:10745073,
CC ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15181153}.
CC -!- INTERACTION:
CC P16110; Q61362: Chi3l1; NbExp=4; IntAct=EBI-3508325, EBI-8392424;
CC P16110; O88786: Il13ra2; NbExp=2; IntAct=EBI-3508325, EBI-20260800;
CC P16110; Q9Z0P7: Sufu; NbExp=5; IntAct=EBI-3508325, EBI-3508336;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17931}. Nucleus
CC {ECO:0000250|UniProtKB:P17931}. Secreted
CC {ECO:0000250|UniProtKB:P17931}. Note=Secreted by a non-classical
CC secretory pathway and associates with the cell surface. Can be
CC secreted; the secretion is dependent on protein unfolding and
CC facilitated by the cargo receptor TMED10; it results in protein
CC translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-
CC Golgi intermediate compartment) followed by vesicle entry and
CC secretion. {ECO:0000250|UniProtKB:P17931}.
CC -!- TISSUE SPECIFICITY: The highest levels are found in activated
CC macrophages.
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DR EMBL; X16834; CAA34736.1; -; mRNA.
DR EMBL; J03723; AAA37311.1; -; mRNA.
DR EMBL; X16074; CAA34206.1; -; mRNA.
DR CCDS; CCDS26986.1; -.
DR PIR; S08537; A28651.
DR PDB; 7CXB; X-ray; 1.46 A; A=122-264.
DR PDB; 7CXC; X-ray; 1.40 A; A/B=122-264.
DR PDB; 7DF6; X-ray; 1.80 A; A/B=122-264.
DR PDBsum; 7CXB; -.
DR PDBsum; 7CXC; -.
DR PDBsum; 7DF6; -.
DR AlphaFoldDB; P16110; -.
DR SMR; P16110; -.
DR DIP; DIP-2152N; -.
DR IntAct; P16110; 6.
DR STRING; 10090.ENSMUSP00000114350; -.
DR BindingDB; P16110; -.
DR ChEMBL; CHEMBL3668; -.
DR iPTMnet; P16110; -.
DR PhosphoSitePlus; P16110; -.
DR SwissPalm; P16110; -.
DR EPD; P16110; -.
DR jPOST; P16110; -.
DR MaxQB; P16110; -.
DR PaxDb; P16110; -.
DR PeptideAtlas; P16110; -.
DR PRIDE; P16110; -.
DR ProteomicsDB; 286183; -.
DR ABCD; P16110; 1 sequenced antibody.
DR MGI; MGI:96778; Lgals3.
DR eggNOG; KOG3587; Eukaryota.
DR InParanoid; P16110; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR ChiTaRS; Lgals3; mouse.
DR PRO; PR:P16110; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P16110; protein.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
DR GO; GO:0097386; C:glial cell projection; IDA:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0050785; F:advanced glycation end-product receptor activity; ISO:MGI.
DR GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
DR GO; GO:0048030; F:disaccharide binding; ISO:MGI.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; ISO:MGI.
DR GO; GO:0019863; F:IgE binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0048029; F:monosaccharide binding; ISO:MGI.
DR GO; GO:0070492; F:oligosaccharide binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISO:MGI.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; ISO:MGI.
DR GO; GO:0071674; P:mononuclear cell migration; ISO:MGI.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:1903769; P:negative regulation of cell proliferation in bone marrow; ISO:MGI.
DR GO; GO:0045806; P:negative regulation of endocytosis; IMP:BHF-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:2000521; P:negative regulation of immunological synapse formation; IMP:BHF-UCL.
DR GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IMP:BHF-UCL.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
DR GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISO:MGI.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0014064; P:positive regulation of serotonin secretion; ISO:MGI.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; ISO:MGI.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; IGI:MGI.
DR CDD; cd00070; GLECT; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR044156; Galectin-like.
DR InterPro; IPR015534; Galectin_3.
DR InterPro; IPR001079; Galectin_CRD.
DR PANTHER; PTHR11346; PTHR11346; 1.
DR PANTHER; PTHR11346:SF26; PTHR11346:SF26; 1.
DR Pfam; PF00337; Gal-bind_lectin; 1.
DR SMART; SM00908; Gal-bind_lectin; 1.
DR SMART; SM00276; GLECT; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS51304; GALECTIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Differentiation;
KW Direct protein sequencing; Disulfide bond; IgE-binding protein; Immunity;
KW Innate immunity; Lectin; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Secreted; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT CHAIN 2..264
FT /note="Galectin-3"
FT /id="PRO_0000076931"
FT REPEAT 35..43
FT /note="1"
FT REPEAT 44..52
FT /note="2"
FT REPEAT 53..61
FT /note="3"
FT REPEAT 62..70
FT /note="4"
FT REPEAT 71..79
FT /note="5"
FT REPEAT 80..88
FT /note="6"
FT REPEAT 89..97
FT /note="7"
FT REPEAT 98..107
FT /note="8"
FT REPEAT 108..114
FT /note="9; truncated"
FT DOMAIN 132..262
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..114
FT /note="9 X 9 AA tandem repeats of Y-P-G-X(3)-P-[GS]-A"
FT MOTIF 240..255
FT /note="Nuclear export signal"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..201
FT /ligand="a beta-D-galactoside"
FT /ligand_id="ChEBI:CHEBI:28034"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT MOD_RES 6
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17931"
FT DISULFID 187
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:1917966"
FT CONFLICT 2
FT /note="A -> R (in Ref. 2; AAA37311)"
FT /evidence="ECO:0000305"
FT CONFLICT 4
FT /note="S -> T (in Ref. 3; CAA34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 92..93
FT /note="QP -> ST (in Ref. 3; CAA34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 110..112
FT /note="QCS -> SAP (in Ref. 3; CAA34206)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="G -> R (in Ref. 2; AAA37311)"
FT /evidence="ECO:0000305"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 168..179
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 182..191
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 211..218
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 230..236
FT /evidence="ECO:0007829|PDB:7CXC"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7CXC"
FT STRAND 247..263
FT /evidence="ECO:0007829|PDB:7CXC"
SQ SEQUENCE 264 AA; 27515 MW; 1B5A8A81093D68F6 CRC64;
MADSFSLNDA LAGSGNPNPQ GYPGAWGNQP GAGGYPGAAY PGAYPGQAPP GAYPGQAPPG
AYPGQAPPSA YPGPTAPGAY PGPTAPGAYP GQPAPGAFPG QPGAPGAYPQ CSGGYPAAGP
YGVPAGPLTV PYDLPLPGGV MPRMLITIMG TVKPNANRIV LDFRRGNDVA FHFNPRFNEN
NRRVIVCNTK QDNNWGKEER QSAFPFESGK PFKIQVLVEA DHFKVAVNDA HLLQYNHRMK
NLREISQLGI SGDITLTSAN HAMI
