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Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (IgE-binding protein) (L-34 galactoside-binding lectin) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen)

 LEG3_MOUSE              Reviewed;         264 AA.
P16110;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 155.
RecName: Full=Galectin-3;
Short=Gal-3;
AltName: Full=35 kDa lectin;
AltName: Full=Carbohydrate-binding protein 35;
Short=CBP 35;
AltName: Full=Galactose-specific lectin 3;
AltName: Full=IgE-binding protein;
AltName: Full=L-34 galactoside-binding lectin;
AltName: Full=Laminin-binding protein;
AltName: Full=Lectin L-29;
AltName: Full=Mac-2 antigen;
Name=Lgals3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=DBA/2J; TISSUE=Macrophage;
PubMed=2584931; DOI=10.1084/jem.170.6.1959;
Cherayil B.J., Weiner S.J., Pillai S.;
"The Mac-2 antigen is a galactose-specific lectin that binds IgE.";
J. Exp. Med. 170:1959-1972(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3360772;
Jia S., Wang J.L.;
"Carbohydrate binding protein 35. Complementary DNA sequence reveals
homology with proteins of the heterogeneous nuclear RNP.";
J. Biol. Chem. 263:6009-6011(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2525069;
Raz A., Pazerini G., Carmi P.;
"Identification of the metastasis-associated, galactoside-binding
lectin as a chimeric gene product with homology to an IgE-binding
protein.";
Cancer Res. 49:3489-3493(1989).
[4]
PROTEIN SEQUENCE OF 159-163; 166-175 AND 214-226.
PubMed=2332426;
Woo H.-J., Shaw L.M., Messier J.M., Mercurio A.M.;
"The major non-integrin laminin binding protein of macrophages is
identical to carbohydrate binding protein 35 (Mac-2).";
J. Biol. Chem. 265:7097-7099(1990).
[5]
PROTEIN SEQUENCE OF 184-190 AND 201-213, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
DISULFIDE BOND.
PubMed=1917966;
Woo H.-J., Lotz M.M., Jung J.U., Mercurio A.M.;
"Carbohydrate-binding protein 35 (Mac-2), a laminin-binding lectin,
forms functional dimers using cysteine 186.";
J. Biol. Chem. 266:18419-18422(1991).
[7]
INTERACTION WITH CYHR1.
PubMed=10745073; DOI=10.1016/S0014-5793(00)01310-7;
Menon R.P., Strom M., Hughes R.C.;
"Interaction of a novel cysteine and histidine-rich cytoplasmic
protein with galectin-3 in a carbohydrate-independent manner galectin
3.";
FEBS Lett. 470:227-231(2000).
[8]
INTERACTION WITH UACA.
PubMed=14961764; DOI=10.1042/BJ20031300;
Liu L., Sakai T., Sano N., Fukui K.;
"Nucling mediates apoptosis by inhibiting expression of galectin-3
through interference with nuclear factor kappaB signalling.";
Biochem. J. 380:31-41(2004).
[9]
SUBCELLULAR LOCATION, INTERACTION WITH ITGB1; ITGA3 AND CSPG4, AND
FUNCTION.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[10]
SUBCELLULAR LOCATION, AND NUCLEAR EXPORT SIGNAL.
PubMed=16473834; DOI=10.1093/glycob/cwj089;
Li S.Y., Davidson P.J., Lin N.Y., Patterson R.J., Wang J.L.,
Arnoys E.J.;
"Transport of galectin-3 between the nucleus and cytoplasm. II.
Identification of the signal for nuclear export.";
Glycobiology 16:612-622(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Galactose-specific lectin which binds IgE. May mediate
with the alpha-3, beta-1 integrin the stimulation by CSPG4 of
endothelial cells migration. Together with DMBT1, required for
terminal differentiation of columnar epithelial cells during early
embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor.
Involved in acute inflammatory responses including neutrophil
activation and adhesion, chemoattraction of monocytes macrophages,
opsonization of apoptotic neutrophils, and activation of mast
cells (By similarity). {ECO:0000250, ECO:0000269|PubMed:15181153}.
-!- SUBUNIT: Probably forms homo- or heterodimers. Interacts with
DMBT1 (By similarity). Interacts with CD6 and ALCAM. Forms a
complex with the ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP,
LYPD3, CYHR1 and UACA (By similarity).
{ECO:0000250|UniProtKB:P08699, ECO:0000250|UniProtKB:P17931,
ECO:0000269|PubMed:10745073, ECO:0000269|PubMed:14961764,
ECO:0000269|PubMed:15181153}.
-!- INTERACTION:
Q9Z0P7:Sufu; NbExp=5; IntAct=EBI-3508325, EBI-3508336;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. Note=Secreted
by a non-classical secretory pathway and associates with the cell
surface.
-!- TISSUE SPECIFICITY: The highest levels are found in activated
macrophages.
-----------------------------------------------------------------------
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EMBL; X16834; CAA34736.1; -; mRNA.
EMBL; J03723; AAA37311.1; -; mRNA.
EMBL; X16074; CAA34206.1; -; mRNA.
CCDS; CCDS26986.1; -.
PIR; S08537; A28651.
UniGene; Mm.248615; -.
ProteinModelPortal; P16110; -.
SMR; P16110; -.
DIP; DIP-2152N; -.
IntAct; P16110; 4.
STRING; 10090.ENSMUSP00000114350; -.
BindingDB; P16110; -.
ChEMBL; CHEMBL3668; -.
iPTMnet; P16110; -.
PhosphoSitePlus; P16110; -.
EPD; P16110; -.
MaxQB; P16110; -.
PaxDb; P16110; -.
PeptideAtlas; P16110; -.
PRIDE; P16110; -.
MGI; MGI:96778; Lgals3.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
HOGENOM; HOG000246423; -.
HOVERGEN; HBG006255; -.
InParanoid; P16110; -.
Reactome; R-MMU-3000471; Scavenging by Class B Receptors.
ChiTaRS; Lgals3; mouse.
PRO; PR:P16110; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_LGALS3; -.
GO; GO:0009986; C:cell surface; IDA:CACAO.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0097386; C:glial cell projection; IDA:MGI.
GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0042056; F:chemoattractant activity; ISO:MGI.
GO; GO:0019863; F:IgE binding; ISO:MGI.
GO; GO:0043236; F:laminin binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0048245; P:eosinophil chemotaxis; ISO:MGI.
GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0048246; P:macrophage chemotaxis; ISO:MGI.
GO; GO:0002548; P:monocyte chemotaxis; ISO:MGI.
GO; GO:0071674; P:mononuclear cell migration; ISO:MGI.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045806; P:negative regulation of endocytosis; IMP:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:2000521; P:negative regulation of immunological synapse formation; IMP:BHF-UCL.
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.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; ISO:MGI.
GO; GO:0050918; P:positive chemotaxis; ISO:MGI.
GO; GO:0090280; P:positive regulation of calcium ion import; ISO:MGI.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI.
GO; GO:0070232; P:regulation of T cell apoptotic process; ISO:MGI.
GO; GO:0042129; P:regulation of T cell proliferation; ISO:MGI.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0001501; P:skeletal system development; IGI:MGI.
InterPro; IPR013320; ConA-like_dom.
InterPro; IPR015534; Galectin_3.
InterPro; IPR001079; Galectin_CRD.
PANTHER; PTHR11346:SF145; PTHR11346:SF145; 1.
Pfam; PF00337; Gal-bind_lectin; 1.
SMART; SM00908; Gal-bind_lectin; 1.
SMART; SM00276; GLECT; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51304; GALECTIN; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; Cytoplasm; Differentiation;
Direct protein sequencing; Disulfide bond; IgE-binding protein;
Immunity; Innate immunity; Lectin; mRNA processing; mRNA splicing;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Secreted;
Spliceosome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P38486}.
CHAIN 2 264 Galectin-3.
/FTId=PRO_0000076931.
REPEAT 35 43 1.
REPEAT 44 52 2.
REPEAT 53 61 3.
REPEAT 62 70 4.
REPEAT 71 79 5.
REPEAT 80 88 6.
REPEAT 89 97 7.
REPEAT 98 107 8.
REPEAT 108 114 9; truncated.
DOMAIN 132 262 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 35 114 9 X 9 AA tandem repeats of Y-P-G-X(3)-P-
[GS]-A.
REGION 195 201 Beta-galactoside binding. {ECO:0000250}.
MOTIF 240 255 Nuclear export signal.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 6 6 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 202 202 Phosphoserine.
{ECO:0000250|UniProtKB:P17931}.
DISULFID 187 187 Interchain. {ECO:0000269|PubMed:1917966}.
CONFLICT 2 2 A -> R (in Ref. 2; AAA37311).
{ECO:0000305}.
CONFLICT 4 4 S -> T (in Ref. 3; CAA34206).
{ECO:0000305}.
CONFLICT 92 93 QP -> ST (in Ref. 3; CAA34206).
{ECO:0000305}.
CONFLICT 110 112 QCS -> SAP (in Ref. 3; CAA34206).
{ECO:0000305}.
CONFLICT 252 252 G -> R (in Ref. 2; AAA37311).
{ECO:0000305}.
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


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