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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_CANLF              Reviewed;         296 AA.
P38486;
01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-MAY-2017, entry version 115.
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;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA] OF 12-296, PARTIAL PROTEIN SEQUENCE, AND
ACETYLATION AT ALA-2.
STRAIN=Cocker spaniel; TISSUE=Kidney;
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).
[2]
PHOSPHORYLATION AT SER-6 AND SER-12.
PubMed=8253806;
Huflejt M.E., Turck C.W., Lindstedt R., Barondes S.H., Leffler H.;
"L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6
and serine 12 in vivo and by casein kinase I.";
J. Biol. Chem. 268:26712-26718(1993).
-!- 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}.
-!- PTM: The degree of phosphorylation is higher in the cytoplasmic
form than in the nuclear form. In protein isolated from a canine
kidney cell line, 90% of the phosphate was on Ser-6 and 10% was on
Ser-12. {ECO:0000269|PubMed:8253806}.
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EMBL; L23429; AAA16211.1; -; mRNA.
PIR; A49688; A49688.
UniGene; Cfa.797; -.
ProteinModelPortal; P38486; -.
SMR; P38486; -.
STRING; 9615.ENSCAFP00000022105; -.
iPTMnet; P38486; -.
PaxDb; P38486; -.
PRIDE; P38486; -.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
HOGENOM; HOG000246423; -.
HOVERGEN; HBG006255; -.
InParanoid; P38486; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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.
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 2 296 Galectin-3.
/FTId=PRO_0000076928.
REPEAT 36 44 1.
REPEAT 45 53 2.
REPEAT 54 62 3.
REPEAT 63 71 4.
REPEAT 72 80 5.
REPEAT 81 89 6.
REPEAT 90 98 7.
REPEAT 99 107 8.
REPEAT 108 115 9; approximate.
REPEAT 116 124 10.
REPEAT 125 134 11; approximate.
REPEAT 135 143 12; approximate.
DOMAIN 164 294 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 36 143 12 X 9 AA tandem repeats of Y-P-G-X(3)-P-
G-[GAT].
REGION 227 233 Beta-galactoside binding. {ECO:0000250}.
MOTIF 272 287 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:8253805}.
MOD_RES 6 6 Phosphoserine; by CK1.
{ECO:0000269|PubMed:8253806}.
MOD_RES 12 12 Phosphoserine; by CK1.
{ECO:0000269|PubMed:8253806}.
DISULFID 219 219 Interchain. {ECO:0000250}.
SEQUENCE 296 AA; 30330 MW; FB1DD61EF1444AEE CRC64;
MADSFSLNDA LSGSGNPNPQ GWPGPWGNQP AGAGGYPGAS YPGAYPGQAP PGGYPGQAPP
GGYPGQAPPG GYPGQAPPGG YPGQAPPGGY PGQAPPGGYP GQAPPGTYPG PTAPAYPGPT
APGTQPGQPS GPGAYPPPGQ PSAPGAYPAA GPFGIPAGPL TVPYDLPLPG GVKPRMLITI
LGTVRPSANR LALDFKRGND VAFHFNPRFN EDNKRVIVCN TKLDNIWGKE ERQAAFPFES
GKPFKIQVLV ESDHFKVAVN DAHLLQYNHR MKNLPEISKL GISGDIDLTS ASYAMI


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