LEG3_RAT
ID LEG3_RAT Reviewed; 262 AA.
AC P08699;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 178.
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=Laminin-binding protein;
DE AltName: Full=Lectin L-29;
DE AltName: Full=Mac-2 antigen;
GN Name=Lgals3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2958848; DOI=10.1073/pnas.84.19.6859;
RA Albrandt K., Orida N.K., Liu F.-T.;
RT "An IgE-binding protein with a distinctive repetitive sequence and homology
RT with an IgG receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:6859-6863(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 120-145.
RX PubMed=2605254; DOI=10.1021/bi00449a039;
RA Lefler H., Masiarz F.R., Barondes S.H.;
RT "Soluble lactose-binding vertebrate lectins: a growing family.";
RL Biochemistry 28:9222-9229(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 125-262.
RX PubMed=3858867; DOI=10.1073/pnas.82.12.4100;
RA Liu F.-T., Albrandt K., Mendel E., Kulczycki A. Jr., Orida N.K.;
RT "Identification of an IgE-binding protein by molecular cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4100-4104(1985).
RN [5]
RP PROTEIN SEQUENCE OF 164-174 AND 223-236, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [6]
RP PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT ALA-2.
RX PubMed=8253805; DOI=10.1016/s0021-9258(19)74370-1;
RA Herrmann J., Turck C.W., Atchison R.E., Huflejt M.E., Poulter L.,
RA Gitt M.A., Burlingame A.L., Barondes S.H., Leffler H.;
RT "Primary structure of the soluble lactose binding lectin L-29 from rat and
RT dog and interaction of its non-collagenous proline-, glycine-, tyrosine-
RT rich sequence with bacterial and tissue collagenase.";
RL J. Biol. Chem. 268:26704-26711(1993).
RN [7]
RP INTERACTION WITH DMBT1, AND FUNCTION.
RX PubMed=11121438; DOI=10.1083/jcb.151.6.1235;
RA Hikita C., Vijayakumar S., Takito J., Erdjument-Bromage H., Tempst P.,
RA Al-Awqati Q.;
RT "Induction of terminal differentiation in epithelial cells requires
RT polymerization of hensin by galectin 3.";
RL J. Cell Biol. 151:1235-1246(2000).
RN [8]
RP INTERACTION WITH LYPD3.
RX PubMed=15729693; DOI=10.1002/ijc.20977;
RA Paret C., Bourouba M., Beer A., Miyazaki K., Schnoelzer M., Fiedler S.,
RA Zoeller M.;
RT "Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin-3
RT and supports cell migration.";
RL Int. J. Cancer 115:724-733(2005).
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. 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 (By similarity). Together with DMBT1,
CC required for terminal differentiation of columnar epithelial cells
CC during early embryogenesis. {ECO:0000250, ECO:0000269|PubMed:11121438}.
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:P16110,
CC ECO:0000250|UniProtKB:P17931, ECO:0000269|PubMed:11121438,
CC ECO:0000269|PubMed:15729693}.
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}.
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DR EMBL; J02962; AAA40828.1; -; mRNA.
DR EMBL; BC089054; AAH89054.1; -; mRNA.
DR EMBL; M13697; AAA41378.1; -; mRNA.
DR PIR; A54889; A54889.
DR RefSeq; NP_114020.1; NM_031832.1.
DR PDB; 7CXD; X-ray; 1.71 A; A/B/D/E=120-262.
DR PDBsum; 7CXD; -.
DR AlphaFoldDB; P08699; -.
DR SMR; P08699; -.
DR STRING; 10116.ENSRNOP00000014216; -.
DR iPTMnet; P08699; -.
DR PhosphoSitePlus; P08699; -.
DR jPOST; P08699; -.
DR PaxDb; P08699; -.
DR PRIDE; P08699; -.
DR Ensembl; ENSRNOT00000014216; ENSRNOP00000014216; ENSRNOG00000010645.
DR GeneID; 83781; -.
DR KEGG; rno:83781; -.
DR UCSC; RGD:69356; rat.
DR CTD; 3958; -.
DR RGD; 69356; Lgals3.
DR eggNOG; KOG3587; Eukaryota.
DR GeneTree; ENSGT00940000157224; -.
DR InParanoid; P08699; -.
DR OrthoDB; 829777at2759; -.
DR PhylomeDB; P08699; -.
DR TreeFam; TF315551; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:P08699; -.
DR Proteomes; UP000002494; Chromosome 15.
DR Bgee; ENSRNOG00000010645; Expressed in jejunum and 20 other tissues.
DR ExpressionAtlas; P08699; baseline and differential.
DR Genevisible; P08699; RN.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0001533; C:cornified envelope; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0097386; C:glial cell projection; ISO:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0050785; F:advanced glycation end-product receptor activity; IDA:RGD.
DR GO; GO:0042056; F:chemoattractant activity; ISO:RGD.
DR GO; GO:0048030; F:disaccharide binding; IDA:RGD.
DR GO; GO:0034988; F:Fc-gamma receptor I complex binding; IDA:RGD.
DR GO; GO:0019863; F:IgE binding; IDA:RGD.
DR GO; GO:0043236; F:laminin binding; ISO:RGD.
DR GO; GO:0048029; F:monosaccharide binding; IDA:RGD.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048246; P:macrophage chemotaxis; ISO:RGD.
DR GO; GO:0002548; P:monocyte chemotaxis; ISO:RGD.
DR GO; GO:0071674; P:mononuclear cell migration; ISO:RGD.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
DR GO; GO:1903769; P:negative regulation of cell proliferation in bone marrow; IDA:RGD.
DR GO; GO:0045806; P:negative regulation of endocytosis; ISO:RGD.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
DR GO; GO:2000521; P:negative regulation of immunological synapse formation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR GO; GO:0050918; P:positive chemotaxis; ISO:RGD.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0014064; P:positive regulation of serotonin secretion; IDA:RGD.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; ISO:RGD.
DR GO; GO:0042129; P:regulation of T cell proliferation; ISO:RGD.
DR GO; GO:1905235; P:response to quercetin; IEP:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
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:0000269|PubMed:8253805"
FT CHAIN 2..262
FT /note="Galectin-3"
FT /id="PRO_0000076933"
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..98
FT /note="7; approximate"
FT REPEAT 99..105
FT /note="8; approximate"
FT REPEAT 106..112
FT /note="9; truncated"
FT DOMAIN 130..260
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..112
FT /note="9 X 9 AA tandem repeats of Y-P-G-X(3)-P-[GS]-[AG]"
FT MOTIF 238..253
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 47..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 193..199
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:0000269|PubMed:8253805"
FT MOD_RES 6
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17931"
FT DISULFID 185
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 20
FT /note="Q -> R (in Ref. 1; AAA40828)"
FT /evidence="ECO:0000305"
FT STRAND 128..133
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 142..150
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 156..163
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 166..177
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 218..225
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 228..234
FT /evidence="ECO:0007829|PDB:7CXD"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:7CXD"
FT STRAND 245..261
FT /evidence="ECO:0007829|PDB:7CXD"
SQ 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
