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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_RAT                Reviewed;         262 AA.
P08699;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 157.
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;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2958848; DOI=10.1073/pnas.84.19.6859;
Albrandt K., Orida N.K., Liu F.-T.;
"An IgE-binding protein with a distinctive repetitive sequence and
homology with an IgG receptor.";
Proc. Natl. Acad. Sci. U.S.A. 84:6859-6863(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 120-145.
PubMed=2605254; DOI=10.1021/bi00449a039;
Lefler H., Masiarz F.R., Barondes S.H.;
"Soluble lactose-binding vertebrate lectins: a growing family.";
Biochemistry 28:9222-9229(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 125-262.
PubMed=3858867; DOI=10.1073/pnas.82.12.4100;
Liu F.-T., Albrandt K., Mendel E., Kulczycki A. Jr., Orida N.K.;
"Identification of an IgE-binding protein by molecular cloning.";
Proc. Natl. Acad. Sci. U.S.A. 82:4100-4104(1985).
[5]
PROTEIN SEQUENCE OF 164-174 AND 223-236, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
Lubec G., Afjehi-Sadat L.;
Submitted (NOV-2006) to UniProtKB.
[6]
PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
PubMed=8253805;
Herrmann J., Turck C.W., Atchison R.E., Huflejt M.E., Poulter L.,
Gitt M.A., Burlingame A.L., Barondes S.H., Leffler H.;
"Primary structure of the soluble lactose binding lectin L-29 from rat
and dog and interaction of its non-collagenous proline-, glycine-,
tyrosine-rich sequence with bacterial and tissue collagenase.";
J. Biol. Chem. 268:26704-26711(1993).
[7]
INTERACTION WITH DMBT1, AND FUNCTION.
PubMed=11121438; DOI=10.1083/jcb.151.6.1235;
Hikita C., Vijayakumar S., Takito J., Erdjument-Bromage H., Tempst P.,
Al-Awqati Q.;
"Induction of terminal differentiation in epithelial cells requires
polymerization of hensin by galectin 3.";
J. Cell Biol. 151:1235-1246(2000).
[8]
INTERACTION WITH LYPD3.
PubMed=15729693; DOI=10.1002/ijc.20977;
Paret C., Bourouba M., Beer A., Miyazaki K., Schnoelzer M.,
Fiedler S., Zoeller M.;
"Ly6 family member C4.4A binds laminins 1 and 5, associates with
galectin-3 and supports cell migration.";
Int. J. Cancer 115:724-733(2005).
-!- FUNCTION: Galactose-specific lectin which binds IgE. May mediate
with the alpha-3, beta-1 integrin the stimulation by CSPG4 of
endothelial cells migration. 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). Together with DMBT1,
required for terminal differentiation of columnar epithelial cells
during early embryogenesis. {ECO:0000250,
ECO:0000269|PubMed:11121438}.
-!- 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:P16110, ECO:0000250|UniProtKB:P17931,
ECO:0000269|PubMed:11121438, ECO:0000269|PubMed:15729693}.
-!- 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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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J02962; AAA40828.1; -; mRNA.
EMBL; BC089054; AAH89054.1; -; mRNA.
EMBL; M13697; AAA41378.1; -; mRNA.
PIR; A54889; A54889.
RefSeq; NP_114020.1; NM_031832.1.
UniGene; Rn.764; -.
ProteinModelPortal; P08699; -.
SMR; P08699; -.
STRING; 10116.ENSRNOP00000014216; -.
iPTMnet; P08699; -.
PhosphoSitePlus; P08699; -.
PaxDb; P08699; -.
PRIDE; P08699; -.
Ensembl; ENSRNOT00000014216; ENSRNOP00000014216; ENSRNOG00000010645.
GeneID; 83781; -.
KEGG; rno:83781; -.
UCSC; RGD:69356; rat.
CTD; 3958; -.
RGD; 69356; Lgals3.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00760000119105; -.
HOGENOM; HOG000246423; -.
HOVERGEN; HBG006255; -.
InParanoid; P08699; -.
KO; K06831; -.
PhylomeDB; P08699; -.
TreeFam; TF315551; -.
Reactome; R-RNO-6798695; Neutrophil degranulation.
PRO; PR:P08699; -.
Proteomes; UP000002494; Chromosome 15.
Bgee; ENSRNOG00000010645; -.
ExpressionAtlas; P08699; baseline and differential.
Genevisible; P08699; RN.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031012; C:extracellular matrix; ISO:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0097386; C:glial cell projection; ISO:RGD.
GO; GO:0001772; C:immunological synapse; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; ISO:RGD.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0050785; F:advanced glycation end-product receptor activity; IDA:RGD.
GO; GO:0042056; F:chemoattractant activity; ISO:RGD.
GO; GO:0048030; F:disaccharide binding; IDA:RGD.
GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:RGD.
GO; GO:0019863; F:IgE binding; IDA:RGD.
GO; GO:0043236; F:laminin binding; ISO:RGD.
GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
GO; GO:0003723; F:RNA binding; ISO:RGD.
GO; GO:0048245; P:eosinophil chemotaxis; ISO:RGD.
GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
GO; GO:0002548; P:monocyte chemotaxis; ISO:RGD.
GO; GO:0071674; P:mononuclear cell migration; ISO:RGD.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:1903769; P:negative regulation of cell proliferation in bone marrow; IDA:RGD.
GO; GO:0045806; P:negative regulation of endocytosis; ISO:RGD.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:2000521; P:negative regulation of immunological synapse formation; ISO:RGD.
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; ISO:RGD.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:RGD.
GO; GO:0014064; P:positive regulation of serotonin secretion; IDA:RGD.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
GO; GO:0070232; P:regulation of T cell apoptotic process; ISO:RGD.
GO; GO:0042129; P:regulation of T cell proliferation; ISO:RGD.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0001501; P:skeletal system development; ISO:RGD.
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.
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:0000269|PubMed:8253805}.
CHAIN 2 262 Galectin-3.
/FTId=PRO_0000076933.
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 98 7; approximate.
REPEAT 99 105 8; approximate.
REPEAT 106 112 9; truncated.
DOMAIN 130 260 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 35 112 9 X 9 AA tandem repeats of Y-P-G-X(3)-P-
[GS]-[AG].
REGION 193 199 Beta-galactoside binding. {ECO:0000250}.
MOTIF 238 253 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:8253805}.
MOD_RES 6 6 Phosphoserine; by CK1.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 200 200 Phosphoserine.
{ECO:0000250|UniProtKB:P17931}.
DISULFID 185 185 Interchain. {ECO:0000250}.
CONFLICT 20 20 Q -> R (in Ref. 1; AAA40828).
{ECO:0000305}.
SEQUENCE 262 AA; 27202 MW; EADB994F5EBD493D CRC64;
MADGFSLNDA LAGSGNPNPQ GWPGAWGNQP GAGGYPGASY PGAYPGQAPP GGYPGQAPPS
AYPGPTGPSA YPGPTAPGAY PGPTAPGAFP GQPGGPGAYP SAPGAYPSAP GAYPATGPFG
APTGPLTVPY DMPLPGGVMP RMLITIIGTV KPNANSITLN FKKGNDIAFH FNPRFNENNR
RVIVCNTKQD NNWGREERQS AFPFESGKPF KIQVLVEADH FKVAVNDVHL LQYNHRMKNL
REISQLGIIG DITLTSASHA MI


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