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

 LEG3_RABIT              Reviewed;         242 AA.
P47845;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 121.
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=Laminin-binding protein;
AltName: Full=Lectin L-29;
AltName: Full=Mac-2 antigen;
Name=LGALS3;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=New Zealand white; TISSUE=Aorta;
PubMed=7590275; DOI=10.1016/0378-1119(95)00388-M;
Gaudin J.-C., Monsigny M., Legrand A.;
"Cloning of the cDNA encoding rabbit galectin-3.";
Gene 163:249-252(1995).
-!- 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}.
-!- 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:P16110,
ECO:0000250|UniProtKB:P17931}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Secreted {ECO:0000250}. Note=Secreted by a non-
classical secretory pathway and associates with the cell surface.
{ECO:0000250}.
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EMBL; U06470; AAC48491.1; -; mRNA.
PIR; JC4300; JC4300.
RefSeq; NP_001075807.1; NM_001082338.1.
UniGene; Ocu.1223; -.
ProteinModelPortal; P47845; -.
SMR; P47845; -.
STRING; 9986.ENSOCUP00000002537; -.
PRIDE; P47845; -.
Ensembl; ENSOCUT00000002920; ENSOCUP00000002537; ENSOCUG00000002924.
GeneID; 100009187; -.
KEGG; ocu:100009187; -.
CTD; 3958; -.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00760000119105; -.
HOGENOM; HOG000246423; -.
HOVERGEN; HBG006255; -.
InParanoid; P47845; -.
KO; K06831; -.
OMA; SASHAMI; -.
OrthoDB; EOG091G0WP8; -.
TreeFam; TF315551; -.
Proteomes; UP000001811; Chromosome 17.
Bgee; ENSOCUG00000002924; -.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0031012; C:extracellular matrix; IEA:Ensembl.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0048245; P:eosinophil chemotaxis; IEA:Ensembl.
GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0048246; P:macrophage chemotaxis; IEA:Ensembl.
GO; GO:0002548; P:monocyte chemotaxis; IEA:Ensembl.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045806; P:negative regulation of endocytosis; IEA:Ensembl.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0030593; P:neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0090280; P:positive regulation of calcium ion import; IEA:Ensembl.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
GO; GO:0070232; P:regulation of T cell apoptotic process; IEA:Ensembl.
GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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.
2: Evidence at transcript level;
Acetylation; Complete proteome; Cytoplasm; Differentiation;
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 2 242 Galectin-3.
/FTId=PRO_0000076932.
REPEAT 35 43 1.
REPEAT 44 52 2.
REPEAT 53 61 3.
REPEAT 62 70 4.
REPEAT 71 80 5; approximate.
REPEAT 81 92 6; approximate.
REPEAT 93 98 7; truncated.
DOMAIN 110 240 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 35 98 7 X 9 AA tandem repeats of Y-P-G-X(3)-P-
[GS]-A.
REGION 173 181 Beta-galactoside binding. {ECO:0000250}.
MOTIF 218 233 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 6 6 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:P38486}.
DISULFID 165 165 Interchain. {ECO:0000250}.
SEQUENCE 242 AA; 25502 MW; 3EE396446074CF22 CRC64;
MADGFSLNDA LSGSGHPPNQ GWPGPWGNQP AGPGGYPGAA YPGAYPGHAP GAYPGQAPPG
PYPGPGAHGA YPGQPGGPGA YPSPGQPSGA GAYPGASPYS ASAGPLPVPY DLPLPGGVMP
RMLITIVGTV KPNANRLALD FKRGNDVAFH FNPRFNENNR RVIVCNTKVD NNWGREERQT
TFPFEIGKPF KIQVLVEPDH FKVAVNDAHL LQYNHRMRNL KEINKLGISG DIQLTSASHA
MI


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