P17931 (LEG3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Galectin-3
Short name=Gal-3

Alternative name(s):
35 kDa lectin
Carbohydrate-binding protein 35
Short name=CBP 35
Galactose-specific lectin 3
Galactoside-binding protein
Short name=GALBP
IgE-binding protein
L-31
Laminin-binding protein
Lectin L-29
Mac-2 antigen

Gene names

Name:	LGALS3
Synonyms:	MAC2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	250 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.15 Ref.16 Ref.17
Subunit structure	Probably forms homo- or heterodimers. Interacts with DMBT1 By similarity. Forms a complex with the ITGA3, ITGB1 and CSPG4. Interacts with LGALS3BP, LYPD3, CYHR1 and UACA. Ref.14 Ref.15
Subcellular location	Cytoplasm. Nucleus. Secreted. Note: Secreted by a non-classical secretory pathway and associates with the cell surface. Ref.5 Ref.15 Ref.17
Tissue specificity	A major expression is found in the colonic epithelium. It is also abundant in the activated macrophages.
Sequence similarities	Contains 1 galectin domain.

Ontologies

Keywords
Biological process	Differentiation Immunity Innate immunity mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Secreted Spliceosome
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	IgE-binding protein Lectin
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix organization Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW skeletal system development Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrial inner membrane Inferred from direct assay PubMed 19016746. Source: UniProtKB nucleus Inferred from direct assay PubMed 14961764. Source: MGI plasma membrane Traceable author statement PubMed 9162064. Source: ProtInc proteinaceous extracellular matrix Inferred from electronic annotation. Source: Compara spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	carbohydrate binding Traceable author statement PubMed 9162064. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 250

249

Galectin-3

PRO_0000076930

Regions

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

Motif

226 – 241

16

Nuclear export signal By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

6

1

Phosphoserine Ref.13

Modified residue

12

1

Phosphoserine Ref.13

Disulfide bond

173

Interchain By similarity

Natural variations

Natural variant

64

1

P → H. Ref.1 Ref.3 Ref.12
Corresponds to variant rs4644 [ dbSNP | Ensembl ].

VAR_012988

Natural variant

98

1

T → P. Ref.1 Ref.2 Ref.3 Ref.12
Corresponds to variant rs4652 [ dbSNP | Ensembl ].

VAR_012989

Natural variant

183

1

R → K.
Corresponds to variant rs10148371 [ dbSNP | Ensembl ].

VAR_049768

Experimental info

Sequence conflict

33 – 52

20

AGGYP…QAPPG → QGLPRGFLSWGLPRAGTPR Ref.2

Sequence conflict

88

1

Missing Ref.2

Sequence conflict

232

1

S → R in M64303. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

250

Helix Strand Turn

Details...

Beta strand

116 – 121

6

Beta strand

130 – 138

9

Beta strand

144 – 151

8

Beta strand

154 – 165

12

Beta strand

168 – 177

10

Beta strand

185 – 187

3

Beta strand

197 – 204

8

Beta strand

206 – 213

8

Beta strand

216 – 222

7

Helix

228 – 230

3

Beta strand

233 – 249

17

Sequences

	Sequence		Length	Mass (Da)
	P17931 [UniParc]. Last modified November 25, 2008. Version 5. Checksum: C49DDF6D67AE0C88	FASTA	250	26,152
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human IgE-binding protein: a soluble lectin exhibiting a highly conserved interspecies sequence and differential recognition of IgE glycoforms." Robertson M.W., Albrandt K., Keller D., Liu F.-T. Biochemistry 29:8093-8100(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-64 AND PRO-98.
[2]	"Molecular cloning of a human macrophage lectin specific for galactose." Cherayil B., Chaitovitz S., Wong C., Pillai S. Proc. Natl. Acad. Sci. U.S.A. 87:7324-7328(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-98. Tissue: Carcinoma.
[3]	"Human breast carcinoma cDNA encoding a galactoside-binding lectin homologous to mouse Mac-2 antigen." Oda Y., Leffler H., Sakakura Y., Kasai K., Barondes S.H. Gene 99:279-283(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-64 AND PRO-98.
[4]	"Molecular cloning and chromosomal mapping of a human galactoside-binding protein." Raz A., Carmi P., Raz T., Hogan V., Mohamed A., Wolman S.R. Cancer Res. 51:2173-2178(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Decreased expression of Mac-2 (carbohydrate binding protein 35) and loss of its nuclear localization are associated with the neoplastic progression of colon carcinoma." Lotz M.M., Andrews C.W. Jr., Korzelius C.A., Lee E.C., Steele G.D. Jr., Clarke A., Mercurio A.M. Proc. Natl. Acad. Sci. U.S.A. 90:3466-3470(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[6]	"The human LGALS3 (galectin-3) gene: determination of the gene structure and functional characterization of the promoter." Kadrofske M.M., Openo K.P., Wang J.L. Arch. Biochem. Biophys. 349:7-20(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]	"Human galectin-3 full-length cDNA." Kato S. Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Gastric adenocarcinoma.
[8]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thalamus.
[9]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[10]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS HIS-64 AND PRO-98. Tissue: Skin.
[13]	"L-29, a soluble lactose-binding lectin, is phosphorylated on serine 6 and serine 12 in vivo and by casein kinase I." Huflejt M.E., Turck C.W., Lindstedt R., Barondes S.H., Leffler H. J. Biol. Chem. 268:26712-26718(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-6 AND SER-12.
[14]	"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." Sasaki T., Brakebusch C., Engel J., Timpl R. EMBO J. 17:1606-1613(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LGALS3BP.
[15]	"NG2 proteoglycan promotes endothelial cell motility and angiogenesis via engagement of galectin-3 and alpha3beta1 integrin." Fukushi J., Makagiansar I.T., Stallcup W.B. Mol. Biol. Cell 15:3580-3590(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ITGB1; ITGA3 AND CSPG4, SUBCELLULAR LOCATION, FUNCTION.
[16]	"The regulation of inflammation by galectin-3." Henderson N.C., Sethi T. Immunol. Rev. 230:160-171(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN INFLAMMATION.
[17]	"Dynamics of galectin-3 in the nucleus and cytoplasm." Haudek K.C., Spronk K.J., Voss P.G., Patterson R.J., Wang J.L., Arnoys E.J. Biochim. Biophys. Acta 1800:181-189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, FUNCTION.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"X-ray crystal structure of the human galectin-3 carbohydrate recognition domain at 2.1-A resolution." Seetharaman J., Kanigsberg A., Slaaby R., Leffler H., Barondes S.H., Rini J.M. J. Biol. Chem. 273:13047-13052(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 114-250.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - Glycan Binding

Galectin-3

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M57710 mRNA. Translation: AAA35607.1.
M35368 mRNA. Translation: AAA88086.1.
M36682 mRNA. Translation: AAA36163.1.
M64303 mRNA. No translation available.
S59012 mRNA. Translation: AAB26229.1.
AF031425 , AF031422, AF031423, AF031424 Genomic DNA. Translation: AAB86584.1.
AB006780 mRNA. Translation: BAA22164.1.
AK314929 mRNA. Translation: BAG37435.1.
CR456897 mRNA. Translation: CAG33178.1.
AL139316 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80658.1.
BC001120 mRNA. Translation: AAH01120.1.
BC053667 mRNA. Translation: AAH53667.1.

IPI

IPI00465431.

PIR

A35820.

RefSeq

NP_002297.2. NM_002306.3.

UniGene

Hs.531081.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1A3K	X-ray	2.10	A	114-250	[»]
1KJL	X-ray	1.40	A	105-249	[»]
1KJR	X-ray	1.55	A	105-249	[»]
2NMN	X-ray	2.45	A	113-249	[»]
2NMO	X-ray	1.35	A	113-249	[»]
2NN8	X-ray	1.35	A	113-249	[»]
2XG3	X-ray	1.20	A	114-250	[»]
3AYA	X-ray	2.00	A/B	117-250	[»]
3AYC	X-ray	1.80	A/B	117-250	[»]
3AYD	X-ray	1.90	A	117-250	[»]
3AYE	X-ray	2.00	A/B	117-250	[»]
3T1L	X-ray	1.60	A	108-250	[»]
3T1M	X-ray	1.55	A	108-250	[»]
3ZSJ	X-ray	0.86	A	113-250	[»]
3ZSK	X-ray	0.90	A	114-250	[»]
3ZSL	X-ray	1.08	A	114-250	[»]
3ZSM	X-ray	1.25	A	114-250	[»]

ProteinModelPortal

P17931.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-45623N.

IntAct

P17931. 42 interactions.

STRING

9606.ENSP00000254301.

PTM databases

PhosphoSite

P17931.

Polymorphism databases

DMDM

215274262.

2D gel databases

DOSAC-COBS-2DPAGE

P17931.

REPRODUCTION-2DPAGE

IPI00465431.

UCD-2DPAGE

P17931.

Proteomic databases

PaxDb

P17931.

PRIDE

P17931.

Protocols and materials databases

DNASU

3958.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254301; ENSP00000254301; ENSG00000131981.

GeneID

3958.

KEGG

hsa:3958.

UCSC

uc001xbr.3. human.

Organism-specific databases

CTD

3958.

GeneCards

GC14P055595.

HGNC

HGNC:6563. LGALS3.

HPA

CAB005191.
HPA003162.

MIM

153619. gene.

neXtProt

NX_P17931.

PharmGKB

PA30340.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG312075.

HOVERGEN

HBG006255.

InParanoid

P17931.

KO

K06831.

OMA

AYPGPTA.

OrthoDB

EOG4C87TX.

Enzyme and pathway databases

Pathway_Interaction_DB

hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P17931.

Bgee

P17931.

CleanEx

HS_LGALS3.

Genevestigator

P17931.

GermOnline

ENSG00000131981. Homo sapiens.

Family and domain databases

Gene3D

2.60.120.200. 1 hit.

InterPro

IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR015534. Galectin_3.
IPR001079. Galectin_CRD.
[Graphical view]

PANTHER

PTHR11346:SF26. PTHR11346:SF26. 1 hit.

Pfam

PF00337. Gal-bind_lectin. 1 hit.
[Graphical view]

SMART

SM00908. Gal-bind_lectin. 1 hit.
SM00276. GLECT. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS51304. GALECTIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P17931.

ChEMBL

CHEMBL4531.

EvolutionaryTrace

P17931.

GenomeRNAi

3958.

NextBio

15531.

PMAP-CutDB

Q6IBA7.

SOURCE

Search...

Entry information

Entry name

LEG3_HUMAN

Accession

Primary (citable) accession number: P17931
Secondary accession number(s): B2RC38 , Q16005, Q6IBA7, Q96J47

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 25, 2008
Last modified:	May 29, 2013
This is version 160 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.