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Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (Galactoside-binding protein) (GALBP) (IgE-binding protein) (L-31) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen)

 LEG3_HUMAN              Reviewed;         250 AA.
P17931; B2RC38; Q16005; Q6IBA7; Q96J47;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 5.
27-SEP-2017, entry version 204.
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=Galactoside-binding protein;
Short=GALBP;
AltName: Full=IgE-binding protein;
AltName: Full=L-31;
AltName: Full=Laminin-binding protein;
AltName: Full=Lectin L-29;
AltName: Full=Mac-2 antigen;
Name=LGALS3; Synonyms=MAC2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-64 AND PRO-98.
PubMed=2261464; DOI=10.1021/bi00487a015;
Robertson M.W., Albrandt K., Keller D., Liu F.-T.;
"Human IgE-binding protein: a soluble lectin exhibiting a highly
conserved interspecies sequence and differential recognition of IgE
glycoforms.";
Biochemistry 29:8093-8100(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PRO-98.
TISSUE=Carcinoma;
PubMed=2402511; DOI=10.1073/pnas.87.18.7324;
Cherayil B., Chaitovitz S., Wong C., Pillai S.;
"Molecular cloning of a human macrophage lectin specific for
galactose.";
Proc. Natl. Acad. Sci. U.S.A. 87:7324-7328(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-64 AND PRO-98.
PubMed=2022338; DOI=10.1016/0378-1119(91)90139-3;
Oda Y., Leffler H., Sakakura Y., Kasai K., Barondes S.H.;
"Human breast carcinoma cDNA encoding a galactoside-binding lectin
homologous to mouse Mac-2 antigen.";
Gene 99:279-283(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2009535;
Raz A., Carmi P., Raz T., Hogan V., Mohamed A., Wolman S.R.;
"Molecular cloning and chromosomal mapping of a human galactoside-
binding protein.";
Cancer Res. 51:2173-2178(1991).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=7682704; DOI=10.1073/pnas.90.8.3466;
Lotz M.M., Andrews C.W. Jr., Korzelius C.A., Lee E.C.,
Steele G.D. Jr., Clarke A., Mercurio A.M.;
"Decreased expression of Mac-2 (carbohydrate binding protein 35) and
loss of its nuclear localization are associated with the neoplastic
progression of colon carcinoma.";
Proc. Natl. Acad. Sci. U.S.A. 90:3466-3470(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9439577; DOI=10.1006/abbi.1997.0447;
Kadrofske M.M., Openo K.P., Wang J.L.;
"The human LGALS3 (galectin-3) gene: determination of the gene
structure and functional characterization of the promoter.";
Arch. Biochem. Biophys. 349:7-20(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Gastric adenocarcinoma;
Kato S.;
"Human galectin-3 full-length cDNA.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-64 AND
PRO-98.
TISSUE=Skin;
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).
[13]
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).
[14]
INTERACTION WITH LGALS3BP.
PubMed=9501082; DOI=10.1093/emboj/17.6.1606;
Sasaki T., Brakebusch C., Engel J., Timpl R.;
"Mac-2 binding protein is a cell-adhesive protein of the extracellular
matrix which self-assembles into ring-like structures and binds beta1
integrins, collagens and fibronectin.";
EMBO J. 17:1606-1613(1998).
[15]
INTERACTION WITH ITGB1; ITGA3 AND CSPG4, SUBCELLULAR LOCATION, AND
FUNCTION.
PubMed=15181153; DOI=10.1091/mbc.E04-03-0236;
Fukushi J., Makagiansar I.T., Stallcup W.B.;
"NG2 proteoglycan promotes endothelial cell motility and angiogenesis
via engagement of galectin-3 and alpha3beta1 integrin.";
Mol. Biol. Cell 15:3580-3590(2004).
[16]
FUNCTION IN INFLAMMATION.
PubMed=19594635; DOI=10.1111/j.1600-065X.2009.00794.x;
Henderson N.C., Sethi T.;
"The regulation of inflammation by galectin-3.";
Immunol. Rev. 230:160-171(2009).
[17]
TISSUE SPECIFICITY.
PubMed=19497882; DOI=10.1073/pnas.0903568106;
Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y.,
Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J.,
Kim J.S., Haidarian S., Uddin M., Bohn H., Benirschke K.,
Santolaya-Forgas J., Grossman L.I., Erez O., Hassan S.S.,
Zavodszky P., Papp Z., Wildman D.E.;
"A primate subfamily of galectins expressed at the maternal-fetal
interface that promote immune cell death.";
Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009).
[18]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=19616076; DOI=10.1016/j.bbagen.2009.07.005;
Haudek K.C., Spronk K.J., Voss P.G., Patterson R.J., Wang J.L.,
Arnoys E.J.;
"Dynamics of galectin-3 in the nucleus and cytoplasm.";
Biochim. Biophys. Acta 1800:181-189(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
INTERACTION WITH CD6 AND ALCAM.
PubMed=24945728; DOI=10.1016/j.febslet.2014.05.064;
Escoda-Ferran C., Carrasco E., Caballero-Banos M., Miro-Julia C.,
Martinez-Florensa M., Consuegra-Fernandez M., Martinez V.G., Liu F.T.,
Lozano F.;
"Modulation of CD6 function through interaction with galectin-1 and
-3.";
FEBS Lett. 588:2805-2813(2014).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[23]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 114-250.
PubMed=9582341; DOI=10.1074/jbc.273.21.13047;
Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S.H.,
Rini J.M.;
"X-ray crystal structure of the human galectin-3 carbohydrate
recognition domain at 2.1-A resolution.";
J. Biol. Chem. 273:13047-13052(1998).
-!- 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 (By similarity). 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. {ECO:0000250,
ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:19594635,
ECO:0000269|PubMed:19616076}.
-!- SUBUNIT: Probably forms homo- or heterodimers. Interacts with
DMBT1 (By similarity). Interacts with CD6 and ALCAM
(PubMed:24945728). Forms a complex with the ITGA3, ITGB1 and
CSPG4. Interacts with LGALS3BP, LYPD3, CYHR1 and UACA.
{ECO:0000250|UniProtKB:P08699, ECO:0000250|UniProtKB:P16110,
ECO:0000269|PubMed:15181153, ECO:0000269|PubMed:24945728,
ECO:0000269|PubMed:9501082}.
-!- INTERACTION:
P12763:AHSG (xeno); NbExp=2; IntAct=EBI-1170392, EBI-9396660;
Q13740:ALCAM; NbExp=3; IntAct=EBI-1170392, EBI-1188108;
P30203:CD6; NbExp=2; IntAct=EBI-1170392, EBI-2873748;
Q08379:GOLGA2; NbExp=3; IntAct=EBI-1170392, EBI-618309;
Q29983:MICA; NbExp=2; IntAct=EBI-1170392, EBI-1031130;
P09237:MMP7; NbExp=5; IntAct=EBI-1170392, EBI-6595344;
Q13427:PPIG; NbExp=3; IntAct=EBI-1170392, EBI-396072;
Q9NZ81:PRR13; NbExp=3; IntAct=EBI-1170392, EBI-740924;
O75177:SS18L1; NbExp=3; IntAct=EBI-1170392, EBI-744674;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted. Note=Secreted
by a non-classical secretory pathway and associates with the cell
surface.
-!- TISSUE SPECIFICITY: A major expression is found in the colonic
epithelium. It is also abundant in the activated macrophages.
Expressed in fetal membranes. {ECO:0000269|PubMed:19497882}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-3;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00118";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LGALS3ID44396ch14q22.html";
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EMBL; M57710; AAA35607.1; -; mRNA.
EMBL; M35368; AAA88086.1; -; mRNA.
EMBL; M36682; AAA36163.1; -; mRNA.
EMBL; M64303; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S59012; AAB26229.1; -; mRNA.
EMBL; AF031425; AAB86584.1; -; Genomic_DNA.
EMBL; AF031422; AAB86584.1; JOINED; Genomic_DNA.
EMBL; AF031423; AAB86584.1; JOINED; Genomic_DNA.
EMBL; AF031424; AAB86584.1; JOINED; Genomic_DNA.
EMBL; AB006780; BAA22164.1; -; mRNA.
EMBL; AK314929; BAG37435.1; -; mRNA.
EMBL; CR456897; CAG33178.1; -; mRNA.
EMBL; AL139316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW80658.1; -; Genomic_DNA.
EMBL; BC001120; AAH01120.1; -; mRNA.
EMBL; BC053667; AAH53667.1; -; mRNA.
CCDS; CCDS41956.1; -.
PIR; A35820; A35820.
RefSeq; NP_002297.2; NM_002306.3.
UniGene; Hs.531081; -.
PDB; 1A3K; X-ray; 2.10 A; A=114-250.
PDB; 1KJL; X-ray; 1.40 A; A=105-250.
PDB; 1KJR; X-ray; 1.55 A; A=105-250.
PDB; 2NMN; X-ray; 2.45 A; A=113-250.
PDB; 2NMO; X-ray; 1.35 A; A=113-250.
PDB; 2NN8; X-ray; 1.35 A; A=113-250.
PDB; 2XG3; X-ray; 1.20 A; A=114-250.
PDB; 3AYA; X-ray; 2.00 A; A/B=117-250.
PDB; 3AYC; X-ray; 1.80 A; A/B=117-250.
PDB; 3AYD; X-ray; 1.90 A; A=117-250.
PDB; 3AYE; X-ray; 2.00 A; A/B=117-250.
PDB; 3T1L; X-ray; 1.60 A; A=108-250.
PDB; 3T1M; X-ray; 1.55 A; A=108-250.
PDB; 3ZSJ; X-ray; 0.86 A; A=113-250.
PDB; 3ZSK; X-ray; 0.90 A; A=114-250.
PDB; 3ZSL; X-ray; 1.08 A; A=114-250.
PDB; 3ZSM; X-ray; 1.25 A; A=114-250.
PDB; 4BLI; X-ray; 1.08 A; A=114-250.
PDB; 4BLJ; X-ray; 1.20 A; A=114-250.
PDB; 4BM8; X-ray; 0.96 A; A=114-250.
PDB; 4JC1; X-ray; 1.50 A; A=108-250.
PDB; 4JCK; X-ray; 1.15 A; A=108-250.
PDB; 4LBJ; X-ray; 1.80 A; A=114-250.
PDB; 4LBK; X-ray; 1.60 A; A=114-250.
PDB; 4LBL; X-ray; 1.58 A; A=114-250.
PDB; 4LBM; X-ray; 1.55 A; A=112-250.
PDB; 4LBN; X-ray; 1.70 A; A=112-250.
PDB; 4LBO; X-ray; 1.65 A; A=113-250.
PDB; 4R9A; X-ray; 1.20 A; A=111-250.
PDB; 4R9B; X-ray; 1.20 A; A=111-250.
PDB; 4R9C; X-ray; 1.19 A; A=111-250.
PDB; 4R9D; X-ray; 1.24 A; A=111-250.
PDB; 4RL7; X-ray; 2.00 A; A=111-250.
PDB; 4XBN; X-ray; 2.21 A; A=113-250.
PDB; 5E88; X-ray; 1.60 A; A=114-250.
PDB; 5E89; X-ray; 1.50 A; A=114-250.
PDB; 5E8A; X-ray; 1.50 A; A=114-250.
PDB; 5EXO; X-ray; 1.50 A; A=112-250.
PDB; 5H9P; X-ray; 2.04 A; A=113-250.
PDB; 5H9R; X-ray; 1.58 A; A=113-250.
PDB; 5IUQ; X-ray; 1.12 A; A=113-250.
PDB; 5NF7; X-ray; 1.59 A; A=106-250.
PDB; 5NF9; X-ray; 1.87 A; A=106-250.
PDB; 5NFA; X-ray; 1.59 A; A=106-250.
PDB; 5NFB; X-ray; 1.59 A; A=106-250.
PDB; 5NFC; X-ray; 1.59 A; A=106-250.
PDBsum; 1A3K; -.
PDBsum; 1KJL; -.
PDBsum; 1KJR; -.
PDBsum; 2NMN; -.
PDBsum; 2NMO; -.
PDBsum; 2NN8; -.
PDBsum; 2XG3; -.
PDBsum; 3AYA; -.
PDBsum; 3AYC; -.
PDBsum; 3AYD; -.
PDBsum; 3AYE; -.
PDBsum; 3T1L; -.
PDBsum; 3T1M; -.
PDBsum; 3ZSJ; -.
PDBsum; 3ZSK; -.
PDBsum; 3ZSL; -.
PDBsum; 3ZSM; -.
PDBsum; 4BLI; -.
PDBsum; 4BLJ; -.
PDBsum; 4BM8; -.
PDBsum; 4JC1; -.
PDBsum; 4JCK; -.
PDBsum; 4LBJ; -.
PDBsum; 4LBK; -.
PDBsum; 4LBL; -.
PDBsum; 4LBM; -.
PDBsum; 4LBN; -.
PDBsum; 4LBO; -.
PDBsum; 4R9A; -.
PDBsum; 4R9B; -.
PDBsum; 4R9C; -.
PDBsum; 4R9D; -.
PDBsum; 4RL7; -.
PDBsum; 4XBN; -.
PDBsum; 5E88; -.
PDBsum; 5E89; -.
PDBsum; 5E8A; -.
PDBsum; 5EXO; -.
PDBsum; 5H9P; -.
PDBsum; 5H9R; -.
PDBsum; 5IUQ; -.
PDBsum; 5NF7; -.
PDBsum; 5NF9; -.
PDBsum; 5NFA; -.
PDBsum; 5NFB; -.
PDBsum; 5NFC; -.
ProteinModelPortal; P17931; -.
SMR; P17931; -.
BioGrid; 110149; 199.
CORUM; P17931; -.
DIP; DIP-45623N; -.
IntAct; P17931; 57.
STRING; 9606.ENSP00000254301; -.
BindingDB; P17931; -.
ChEMBL; CHEMBL4531; -.
iPTMnet; P17931; -.
PhosphoSitePlus; P17931; -.
BioMuta; LGALS3; -.
DMDM; 215274262; -.
DOSAC-COBS-2DPAGE; P17931; -.
REPRODUCTION-2DPAGE; IPI00465431; -.
UCD-2DPAGE; P17931; -.
EPD; P17931; -.
MaxQB; P17931; -.
PaxDb; P17931; -.
PeptideAtlas; P17931; -.
PRIDE; P17931; -.
DNASU; 3958; -.
Ensembl; ENST00000254301; ENSP00000254301; ENSG00000131981.
GeneID; 3958; -.
KEGG; hsa:3958; -.
UCSC; uc001xbr.4; human.
CTD; 3958; -.
DisGeNET; 3958; -.
EuPathDB; HostDB:ENSG00000131981.15; -.
GeneCards; LGALS3; -.
HGNC; HGNC:6563; LGALS3.
HPA; CAB005191; -.
HPA; HPA003162; -.
MIM; 153619; gene.
neXtProt; NX_P17931; -.
OpenTargets; ENSG00000131981; -.
PharmGKB; PA30340; -.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00760000119105; -.
HOVERGEN; HBG006255; -.
InParanoid; P17931; -.
KO; K06831; -.
OMA; SASHAMI; -.
OrthoDB; EOG091G0WP8; -.
PhylomeDB; P17931; -.
TreeFam; TF315551; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-879415; Advanced glycosylation endproduct receptor signaling.
Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
SIGNOR; P17931; -.
ChiTaRS; LGALS3; human.
EvolutionaryTrace; P17931; -.
GeneWiki; LGALS3; -.
GenomeRNAi; 3958; -.
PMAP-CutDB; Q6IBA7; -.
PRO; PR:P17931; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000131981; -.
CleanEx; HS_LGALS3; -.
ExpressionAtlas; P17931; baseline and differential.
Genevisible; P17931; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0001772; C:immunological synapse; IDA:BHF-UCL.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0044216; C:other organism cell; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc.
GO; GO:0042056; F:chemoattractant activity; IDA:BHF-UCL.
GO; GO:0019863; F:IgE binding; IDA:BHF-UCL.
GO; GO:0043236; F:laminin binding; IDA:BHF-UCL.
GO; GO:0070492; F:oligosaccharide binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0048245; P:eosinophil chemotaxis; IDA:BHF-UCL.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0048246; P:macrophage chemotaxis; IDA:BHF-UCL.
GO; GO:0002548; P:monocyte chemotaxis; IDA:BHF-UCL.
GO; GO:0071674; P:mononuclear cell migration; IDA:BHF-UCL.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0045806; P:negative regulation of endocytosis; IDA:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:2000521; P:negative regulation of immunological synapse formation; ISS:BHF-UCL.
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; ISS:BHF-UCL.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; ISS:BHF-UCL.
GO; GO:0030593; P:neutrophil chemotaxis; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
GO; GO:0090280; P:positive regulation of calcium ion import; IDA:BHF-UCL.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; IDA:BHF-UCL.
GO; GO:1902041; P:regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:BHF-UCL.
GO; GO:0045637; P:regulation of myeloid cell differentiation; TAS:Reactome.
GO; GO:0070232; P:regulation of T cell apoptotic process; IDA:BHF-UCL.
GO; GO:0042129; P:regulation of T cell proliferation; IMP:BHF-UCL.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
CDD; cd00070; GLECT; 1.
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;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Differentiation; Disulfide bond; IgE-binding protein; Immunity;
Innate immunity; Lectin; mRNA processing; mRNA splicing; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Spliceosome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P38486}.
CHAIN 2 250 Galectin-3.
/FTId=PRO_0000076930.
REPEAT 36 44 1.
REPEAT 45 53 2.
REPEAT 54 62 3.
REPEAT 63 69 4; approximate.
REPEAT 70 78 5.
REPEAT 79 88 6; approximate.
REPEAT 89 100 7; approximate.
REPEAT 101 109 8; approximate.
DOMAIN 118 248 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 36 109 8 X 9 AA tandem repeats of Y-P-G-X(3)-P-
G-A.
REGION 181 187 Beta-galactoside binding. {ECO:0000250}.
MOTIF 226 241 Nuclear export signal. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P38486}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000269|PubMed:8253806}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000269|PubMed:8253806}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
DISULFID 173 173 Interchain. {ECO:0000250}.
VARIANT 64 64 P -> H (in dbSNP:rs4644).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2022338,
ECO:0000269|PubMed:2261464}.
/FTId=VAR_012988.
VARIANT 98 98 T -> P (in dbSNP:rs4652).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2022338,
ECO:0000269|PubMed:2261464,
ECO:0000269|PubMed:2402511}.
/FTId=VAR_012989.
VARIANT 183 183 R -> K (in dbSNP:rs10148371).
/FTId=VAR_049768.
CONFLICT 33 52 AGGYPGASYPGAYPGQAPPG -> QGLPRGFLSWGLPRAGT
PR (in Ref. 2). {ECO:0000305}.
CONFLICT 88 88 Missing (in Ref. 2). {ECO:0000305}.
CONFLICT 232 232 S -> R (in Ref. 4; M64303).
{ECO:0000305}.
STRAND 116 121 {ECO:0000244|PDB:3ZSJ}.
STRAND 130 138 {ECO:0000244|PDB:3ZSJ}.
STRAND 144 151 {ECO:0000244|PDB:3ZSJ}.
STRAND 154 165 {ECO:0000244|PDB:3ZSJ}.
STRAND 168 177 {ECO:0000244|PDB:3ZSJ}.
STRAND 185 187 {ECO:0000244|PDB:3ZSJ}.
STRAND 197 204 {ECO:0000244|PDB:3ZSJ}.
STRAND 206 213 {ECO:0000244|PDB:3ZSJ}.
STRAND 216 222 {ECO:0000244|PDB:3ZSJ}.
HELIX 228 230 {ECO:0000244|PDB:3ZSJ}.
STRAND 233 249 {ECO:0000244|PDB:3ZSJ}.
SEQUENCE 250 AA; 26152 MW; C49DDF6D67AE0C88 CRC64;
MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP
GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL
PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN
WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI
DLTSASYTMI


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