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UniProtKB/Swiss-Prot entry P17931


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LEG3_HUMAN
Primary accession number P17931
Secondary accession numbers B2RC38 Q16005 Q96J47
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on November 25, 2008 (Sequence version 5)
Annotations were last modified on    June 16, 2009 (Entry version 118)
Name and origin of the protein
Protein name Galectin-3
Synonyms Galactose-specific lectin 3
Mac-2 antigen
IgE-binding protein
35 kDa lectin
Carbohydrate-binding protein 35
CBP 35
Laminin-binding protein
Lectin L-29
L-31
Galactoside-binding protein
GALBP
Gene name
Name: LGALS3
Synonyms: MAC2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS HIS-64 AND PRO-98.
DOI=10.1021/bi00487a015; PubMed=2261464 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1073/pnas.87.18.7324; PubMed=2402511 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1016/0378-1119(91)90139-3; PubMed=2022338 [NCBI, ExPASy, EBI, Israel, Japan]
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 [NCBI, ExPASy, EBI, Israel, Japan]
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.
DOI=10.1073/pnas.90.8.3466; PubMed=7682704 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/abbi.1997.0447; PubMed=9439577 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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 GENOMIC DNA].
DOI=10.1038/nature01348; PubMed=12508121 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS HIS-64 AND PRO-98.
TISSUE=Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
PHOSPHORYLATION AT SER-6 AND SER-12.
PubMed=8253806 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
INTERACTION WITH LGALS3BP.
DOI=10.1093/emboj/17.6.1606; PubMed=9501082 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
INTERACTION WITH ITGB1; ITGA3 AND CSPG4, SUBCELLULAR LOCATION, AND FUNCTION.
DOI=10.1091/mbc.E04-03-0236; PubMed=15181153 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 114-250.
DOI=10.1074/jbc.273.21.13047; PubMed=9582341 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M57710; AAA35607.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35368; AAA88086.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36682; AAA36163.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M64303; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
S59012; AAB26229.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF031425; AAB86584.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF031422; AAB86584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF031423; AAB86584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF031424; AAB86584.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006780; BAA22164.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK314929; BAG37435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL139316; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC001120; AAH01120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053667; AAH53667.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00465431; -.
PIR A35820; A35820.
RefSeq NP_002297.2; -.
UniGene Hs.531081
3D structure databases
PDB
1A3K; X-ray; 2.10 A; A=114-250.[ExPASy / RCSB / EBI]
1KJL; X-ray; 1.40 A; A=105-249.[ExPASy / RCSB / EBI]
1KJR; X-ray; 1.55 A; A=105-249.[ExPASy / RCSB / EBI]
2NMN; X-ray; 2.45 A; A=113-249.[ExPASy / RCSB / EBI]
2NMO; X-ray; 1.35 A; A=113-249.[ExPASy / RCSB / EBI]
2NN8; X-ray; 1.35 A; A=113-249.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1A3K; -.
1KJL; -.
1KJR; -.
2NMN; -.
2NMO; -.
2NN8; -.
ModBase P17931.
PTM databases
PhosphoSite P17931; -.
Enzyme and pathway databases
Pathway_Interaction_DB hedgehog_glipathway; Hedgehog signaling events mediated by Gli proteins.
2D gel databases
DOSAC-COBS-2DPAGE P17931; -.
REPRODUCTION-2DPAGE IPI00465431; -.
Organism-specific databases
GeneCards GC14P054665; -.
H-InvDB HIX0011683; -.
HGNC HGNC:6563; LGALS3.
GenAtlas LGALS3.
HPA CAB005191; -.
HPA003162; -.
MIM 153619; gene. [NCBI / EBI]
PharmGKB PA30340; -.
Gene expression databases
ArrayExpress P17931; -.
Bgee P17931; -.
CleanEx HS_LGALS3; -.
GermOnline ENSG00000131981; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005634; Cellular component: nucleus (inferred from direct assay from MGI).
GO:0005886; Cellular component: plasma membrane (traceable author statement from ProtInc).
GO:0019863; Molecular function: IgE binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005529; Molecular function: sugar binding (traceable author statement from ProtInc).
GO:0030154; Biological process: cell differentiation (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR013320; ConA-like_subgrp.
IPR015534; Galectin_3.
IPR001079; Galectin_CRD.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.200; ConA_like_subgrp; 1.
PANTHER PTHR11346:SF26; Galectin_3; 1.
PTHR11346; Galectin_bd; 1.
Pfam PF00337; Gal-bind_lectin; 1.
Pfam graphical view of domain structure.
SMART SM00276; GLECT; 1.
SMART graphical view of domain structure.
PROSITE PS51304; GALECTIN; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P17931; -.
Genome annotation databases
Ensembl ENSG00000131981; Homo sapiens. [Contig view]
GeneID 3958; -.
KEGG hsa:3958; -.
Phylogenomic databases
HOVERGEN P17931; -.
OMA P17931; QAPPGAY.
Other
BindingDB P17931; -.
NextBio 15531; -.
PMAP-CutDB P17931; -.
SOURCE LGALS3; Homo sapiens.
ProtoNet P17931.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Differentiation; Disulfide bond; IgE-binding protein; Lectin; Nucleus; Phosphoprotein; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   250  249     Galectin-3. PRO_0000076930
REPEAT   36    44  9     1. 
REPEAT   45    53  9     2. 
REPEAT   54    62  9     3. 
REPEAT   63    69  7     4; approximate. 
REPEAT   70    78  9     5. 
REPEAT   79    88  10     6; approximate. 
REPEAT   89   100  12     7; approximate. 
REPEAT   101   109  9     8; approximate. 
DOMAIN   118   248  131     Galectin. 
REGION   36   109  74     8 X 9 AA tandem repeats of Y-P-G-X(3)-P-G-A. 
REGION   181   187  7     Beta-galactoside binding (By similarity). 
MOD_RES   2     2        N-acetylalanine (By similarity). 
MOD_RES   6     6        Phosphoserine. 
MOD_RES   12    12        Phosphoserine. 
DISULFID   173   173        Interchain (By similarity). 
VARIANT   64    64  1     P -> H (in dbSNP:rs4644 [NCBI]). VAR_012988 
VARIANT   98    98  1     T -> P (in dbSNP:rs4652 [NCBI]). VAR_012989 
VARIANT   183   183  1     R -> K (in dbSNP:rs10148371 [NCBI]). VAR_049768 [3D]
CONFLICT   33    52        AGGYPGASYPGAYPGQAPPG -> QGLPRGFLSWGLPRAGTPR (in Ref. 2). 
CONFLICT   88    88        Missing (in Ref. 2). 
CONFLICT   232   232        S -> R (in Ref. 4; M64303). 
STRAND   116   121  6      
STRAND   130   138  9      
STRAND   144   151  8      
STRAND   154   165  12      
STRAND   168   177  10      
STRAND   185   187  3      
STRAND   197   204  8      
STRAND   206   213  8      
STRAND   216   222  7      
HELIX   228   230  3      
STRAND   233   249  17      
Sequence information
Length: 250 AA [This is the length of the unprocessed precursor] Molecular weight: 26152 Da [This is the MW of the unprocessed precursor] CRC64: C49DDF6D67AE0C88 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADNFSLHDA LSGSGNPNPQ GWPGAWGNQP AGAGGYPGAS YPGAYPGQAP PGAYPGQAPP 

        70         80         90        100        110        120 
GAYPGAPGAY PGAPAPGVYP GPPSGPGAYP SSGQPSATGA YPATGPYGAP AGPLIVPYNL 

       130        140        150        160        170        180 
PLPGGVVPRM LITILGTVKP NANRIALDFQ RGNDVAFHFN PRFNENNRRV IVCNTKLDNN 

       190        200        210        220        230        240 
WGREERQSVF PFESGKPFKI QVLVEPDHFK VAVNDAHLLQ YNHRVKKLNE ISKLGISGDI 

       250 
DLTSASYTMI 

P17931 in FASTA format

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