LEG3_RABIT
ID LEG3_RABIT Reviewed; 242 AA.
AC P47845;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 144.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Aorta;
RX PubMed=7590275; DOI=10.1016/0378-1119(95)00388-m;
RA Gaudin J.-C., Monsigny M., Legrand A.;
RT "Cloning of the cDNA encoding rabbit galectin-3.";
RL Gene 163:249-252(1995).
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. {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 Interacts with TRIM16; this interaction mediates autophagy of damage
CC endomembranes (By similarity). {ECO:0000250|UniProtKB:P08699,
CC ECO:0000250|UniProtKB:P16110, 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}.
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DR EMBL; U06470; AAC48491.1; -; mRNA.
DR PIR; JC4300; JC4300.
DR RefSeq; NP_001075807.1; NM_001082338.1.
DR AlphaFoldDB; P47845; -.
DR SMR; P47845; -.
DR STRING; 9986.ENSOCUP00000002537; -.
DR ABCD; P47845; 1 sequenced antibody.
DR GeneID; 100009187; -.
DR KEGG; ocu:100009187; -.
DR CTD; 3958; -.
DR eggNOG; KOG3587; Eukaryota.
DR HOGENOM; CLU_072823_0_0_1; -.
DR InParanoid; P47845; -.
DR OMA; MPRMMIT; -.
DR OrthoDB; 829777at2759; -.
DR TreeFam; TF315551; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0019863; F:IgE binding; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Differentiation; Disulfide bond;
KW IgE-binding protein; Immunity; Innate immunity; Lectin; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Secreted; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT CHAIN 2..242
FT /note="Galectin-3"
FT /id="PRO_0000076932"
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..80
FT /note="5; approximate"
FT REPEAT 81..92
FT /note="6; approximate"
FT REPEAT 93..98
FT /note="7; truncated"
FT DOMAIN 110..240
FT /note="Galectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00639"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..98
FT /note="7 X 9 AA tandem repeats of Y-P-G-X(3)-P-[GS]-A"
FT REGION 55..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 218..233
FT /note="Nuclear export signal"
FT /evidence="ECO:0000250"
FT BINDING 173..181
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:0000250|UniProtKB:P38486"
FT MOD_RES 6
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P38486"
FT DISULFID 165
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ 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
