LEG3_CANLF
ID LEG3_CANLF Reviewed; 296 AA.
AC P38486;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
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 Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 12-296, PARTIAL PROTEIN SEQUENCE, AND
RP ACETYLATION AT ALA-2.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
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 [2]
RP PHOSPHORYLATION AT SER-6 AND SER-12.
RX PubMed=8253806; DOI=10.1016/s0021-9258(19)74371-3;
RA Huflejt M.E., Turck C.W., Lindstedt R., Barondes S.H., Leffler H.;
RT "L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and
RT serine 12 in vivo and by casein kinase I.";
RL J. Biol. Chem. 268:26712-26718(1993).
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. Together with DMBT1, required for terminal
CC differentiation of columnar epithelial cells during early
CC embryogenesis. 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). {ECO:0000250}.
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 (By similarity). Interacts with TRIM16; this interaction mediates
CC autophagy of damage endomembranes (By similarity).
CC {ECO:0000250|UniProtKB:P08699, ECO:0000250|UniProtKB:P16110,
CC ECO:0000250|UniProtKB:P17931}.
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}.
CC -!- PTM: The degree of phosphorylation is higher in the cytoplasmic form
CC than in the nuclear form. In protein isolated from a canine kidney cell
CC line, 90% of the phosphate was on Ser-6 and 10% was on Ser-12.
CC {ECO:0000269|PubMed:8253806}.
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DR EMBL; L23429; AAA16211.1; -; mRNA.
DR PIR; A49688; A49688.
DR AlphaFoldDB; P38486; -.
DR SMR; P38486; -.
DR STRING; 9615.ENSCAFP00000022105; -.
DR iPTMnet; P38486; -.
DR PaxDb; P38486; -.
DR PRIDE; P38486; -.
DR Ensembl; ENSCAFT00030005060; ENSCAFP00030004495; ENSCAFG00030002726.
DR eggNOG; KOG3587; Eukaryota.
DR InParanoid; P38486; -.
DR Reactome; R-CFA-6798695; Neutrophil degranulation.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0001772; C:immunological synapse; IBA:GO_Central.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042056; F:chemoattractant activity; IEA:Ensembl.
DR GO; GO:0019863; F:IgE binding; IBA:GO_Central.
DR GO; GO:0043236; F:laminin binding; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR GO; GO:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048246; P:macrophage chemotaxis; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0045806; P:negative regulation of endocytosis; IBA:GO_Central.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0050918; P:positive chemotaxis; IBA:GO_Central.
DR GO; GO:0090280; P:positive regulation of calcium ion import; IBA:GO_Central.
DR GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; IEA:Ensembl.
DR GO; GO:0042129; P:regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
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 Acetylation; Cytoplasm; Differentiation; Direct protein sequencing;
KW Disulfide bond; IgE-binding protein; Immunity; Innate immunity; Lectin;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8253805"
FT CHAIN 2..296
FT /note="Galectin-3"
FT /id="PRO_0000076928"
FT REPEAT 36..44
FT /note="1"
FT REPEAT 45..53
FT /note="2"
FT REPEAT 54..62
FT /note="3"
FT REPEAT 63..71
FT /note="4"
FT REPEAT 72..80
FT /note="5"
FT REPEAT 81..89
FT /note="6"
FT REPEAT 90..98
FT /note="7"
FT REPEAT 99..107
FT /note="8"
FT REPEAT 108..115
FT /note="9; approximate"
FT REPEAT 116..124
FT /note="10"
FT REPEAT 125..134
FT /note="11; approximate"
FT REPEAT 135..143
FT /note="12; approximate"
FT DOMAIN 164..294
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 36..143
FT /note="12 X 9 AA tandem repeats of Y-P-G-X(3)-P-G-[GAT]"
FT MOTIF 272..287
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..145
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 227..233
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:0000269|PubMed:8253806"
FT MOD_RES 12
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000269|PubMed:8253806"
FT DISULFID 219
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ 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
