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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.
05-DEC-2018, entry version 129.
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. Together with TRIM16, coordinates the recognition of
membrane damage with mobilization of the core autophagy regulators
ATG16L1 and BECN1 in response to damaged endomembranes.
{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. Interacts with TRIM16; this interaction
mediates autophagy of damage endomembranes (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; ENSGT00940000157224; -.
HOGENOM; HOG000246423; -.
HOVERGEN; HBG006255; -.
InParanoid; P47845; -.
KO; K06831; -.
OMA; YWGPEER; -.
OrthoDB; EOG091G0WP8; -.
TreeFam; TF315551; -.
Proteomes; UP000001811; Chromosome 17.
Bgee; ENSOCUG00000002924; Expressed in 3 organ(s), highest expression level in adult mammalian kidney.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0019903; F:protein phosphatase 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:0090073; P:positive regulation of protein homodimerization activity; IEA:Ensembl.
GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; 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.
CDD; cd00070; GLECT; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR015534; Galectin_3.
InterPro; IPR001079; Galectin_CRD.
PANTHER; PTHR11346:SF26; PTHR11346:SF26; 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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