LGALS3BP

LGALS3BP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1BY2
Identifiers
Aliases	LGALS3BP , 90K, BTBD17B, CyCAP, M2BP, MAC-2-BP, TANGO10B, gp90, galectin 3 binding protein
External IDs	OMIM: 600626 MGI: 99554 HomoloGene: 4067 GeneCards: LGALS3BP
Gene location (Human)
Chr.	Chromosome 17 (human)
End	78,979,947 bp
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)
End	118,292,918 bp
RNA expression pattern
	Top expressed in
	gallbladder; ; right uterine tube; ; Left adrenal gland; ; anterior pituitary; ; stromal cell of endometrium; ; left ventricle; ; canal of the cervix; ; body of stomach; ; upper lobe of left lung; ; left uterine tube;
	Top expressed in
	calvaria; ; gastric mucosa; ; mucous cell of stomach; ; islet of Langerhans; ; Epithelium of stomach; ; duodenum; ; ileum; ; subcutaneous adipose tissue; ; white adipose tissue; ; jejunum;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	scavenger receptor activity ; protein binding ;
Cellular component	extracellular matrix ; extracellular exosome ; blood microparticle ; membrane ; platelet dense granule lumen ; extracellular space ; extracellular region ; collagen-containing extracellular matrix ;
Biological process	cellular defense response ; cell adhesion ; signal transduction ; platelet degranulation ; receptor-mediated endocytosis ; vesicle-mediated transport ; endocytosis ;
	Sources:Amigo / QuickGO
Orthologs
	3959
	19039
	ENSG00000108679
	ENSMUSG00000033880
	Q08380
	Q07797
	NM_005567
	NM_011150
	NP_005558
	NP_035280
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 14, 2022

Galectin-3-binding protein is a protein that in humans is encoded by the LGALS3BP gene.^[5]^[6]^[7]^[8]

Function

The galectins are a family of beta-galactoside-binding proteins implicated in modulating cell–cell and cell–matrix interactions. Using fluorescence in–situ hybridization, the full length 90K cDNA has been localized to chromosome 17q25. The native protein binds specifically to a human macrophage-associated lectin known as Mac-2 and also binds to galectin 1.^[8]

Clinical significance

LGALS3BP has been found elevated in the serum of patients with cancer and in those infected by the human immunodeficiency virus (HIV). It appears to be implicated in immune response associated with natural killer (NK) and lymphokine-activated killer (LAK) cell cytotoxicity.^[8]

Interactions

LGALS3BP has been shown to interact with LGALS3.^[7]^[9]^[10]

Related Research Articles

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Calnexin (CNX) is a 67kDa integral protein of the endoplasmic reticulum (ER). It consists of a large N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short, acidic cytoplasmic tail.

Galectins are a class of proteins that bind specifically to β-galactoside sugars, such as N-acetyllactosamine, which can be bound to proteins by either N-linked or O-linked glycosylation. They are also termed S-type lectins due to their dependency on disulphide bonds for stability and carbohydrate binding. There have been about 15 galectins discovered in mammals, encoded by the LGALS genes, which are numbered in a consecutive manner. Only galectin-1, -2, -3, -4, -7, -7B, -8, -9, -9B, 9C, -10, -12, -13, -14, and -16 have been identified in humans. Galectin-5 and -6 are found in rodents, whereas galectin-11 and -15 are uniquely found in sheep and goats. Members of the galectin family have also been discovered in other mammals, birds, amphibians, fish, nematodes, sponges, and some fungi. Unlike the majority of lectins they are not membrane bound, but soluble proteins with both intra- and extracellular functions. They have distinct but overlapping distributions but found primarily in the cytosol, nucleus, extracellular matrix or in circulation. Although many galectins must be secreted, they do not have a typical signal peptide required for classical secretion. The mechanism and reason for this non-classical secretion pathway is unknown.

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene. CD61 is a cluster of differentiation found on thrombocytes.

Heparin-binding EGF-like growth factor (HB-EGF) is a member of the EGF family of proteins that in humans is encoded by the HBEGF gene.

Galectin-1 is a protein that in humans is encoded by the LGALS1 gene.

Protein ERGIC-53 also known as ER-Golgi intermediate compartment 53 kDa protein or lectin mannose-binding 1 is a protein that in humans is encoded by the LMAN1 gene.

Glycoprotein Ib (platelet), beta polypeptide (GP1BB) also known as CD42c, is a protein that in humans is encoded by the GP1BB gene.

Dentin matrix acidic phosphoprotein 1 is a protein that in humans is encoded by the DMP1 gene.

Galectin-10 is an enzyme that in humans is encoded by the CLC gene.

Galectin-8 is a protein of the galectin family that in humans is encoded by the LGALS8 gene.

Galectin-9 was first isolated from mouse embryonic kidney in 1997 as a 36 kDa beta-galactoside lectin protein. Human galectin-9 is encoded by the LGALS9 gene.

NEDD8-activating enzyme E1 catalytic subunit is a protein that in humans is encoded by the UBA3 gene.

Glycoprotein V (platelet) (GP5) also known as CD42d, is a human gene.

Galectin-2 is a protein that in humans is encoded by the LGALS2 gene.

Sialic acid-binding Ig-like lectin 5 is a protein that in humans is encoded by the SIGLEC5 gene. SIGLEC5 has also been designated CD170.

Galectin-7 is a protein that in humans is encoded by the LGALS7 gene.

Placental protein 13 (PP13) is a protein that in humans is encoded by the LGALS13 gene.

Galectin-4 is a protein that in humans is encoded by the LGALS4 gene.

Galectin-3 is a protein that in humans is encoded by the LGALS3 gene. Galectin-3 is a member of the lectin family, of which 14 mammalian galectins have been identified.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000108679 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033880 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Calabrese G, Sures I, Pompetti F, Natoli G, Palka G, Iacobelli S (May 1995). "The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25". Cytogenet Cell Genet. 69 (3–4): 223–5. doi:10.1159/000133969. PMID 7698018.
↑ Ullrich A, Sures I, D'Egidio M, Jallal B, Powell TJ, Herbst R, Dreps A, Azam M, Rubinstein M, Natoli C, et al. (Aug 1994). "The secreted tumor-associated antigen 90K is a potent immune stimulator". J Biol Chem. 269 (28): 18401–7. doi: 10.1016/S0021-9258(17)32322-0 . PMID 8034587.
1 2 Koths K, Taylor E, Halenbeck R, Casipit C, Wang A (July 1993). "Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain". J. Biol. Chem. 268 (19): 14245–9. doi: 10.1016/S0021-9258(19)85233-X . PMID 8390986.
1 2 3 "Entrez Gene: LGALS3BP lectin, galactoside-binding, soluble, 3 binding protein".
↑ Rosenberg I, Cherayil BJ, Isselbacher KJ, Pillai S (October 1991). "Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin". J. Biol. Chem. 266 (28): 18731–6. doi: 10.1016/S0021-9258(18)55124-3 . PMID 1917996.
↑ Tinari N, Kuwabara I, Huflejt ME, Shen PF, Iacobelli S, Liu FT (January 2001). "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer. 91 (2): 167–72. doi:10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q. PMID 11146440.

Grassadonia A, Tinari N, Iurisci I, et al. (2004). "90K (Mac-2 BP) and galectins in tumor progression and metastasis". Glycoconj. J. 19 (7–9): 551–6. doi:10.1023/B:GLYC.0000014085.00706.d4. PMID 14758079. S2CID 8981436.
Rosenberg I, Cherayil BJ, Isselbacher KJ, Pillai S (1991). "Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin". J. Biol. Chem. 266 (28): 18731–6. doi: 10.1016/S0021-9258(18)55124-3 . PMID 1917996.
Yu B, Wright SD (1995). "LPS-dependent interaction of Mac-2-binding protein with immobilized CD14". J. Inflamm. 45 (2): 115–25. PMID 7583357.
Koths K, Taylor E, Halenbeck R, et al. (1993). "Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain". J. Biol. Chem. 268 (19): 14245–9. doi: 10.1016/S0021-9258(19)85233-X . PMID 8390986.
Inohara H, Akahani S, Koths K, Raz A (1996). "Interactions between galectin-3 and Mac-2-binding protein mediate cell-cell adhesion". Cancer Res. 56 (19): 4530–4. PMID 8813152.
Brakebusch C, Jallal B, Fusco O, et al. (1997). "Expression of the 90K immunostimulator gene is controlled by a promoter with unique features". J. Biol. Chem. 272 (6): 3674–82. doi: 10.1074/jbc.272.6.3674 . PMID 9013622.
Fusco O, Querzoli P, Nenci I, et al. (1998). "90K (MAC-2 BP) gene expression in breast cancer and evidence for the production of 90K by peripheral-blood mononuclear cells". Int. J. Cancer. 79 (1): 23–6. doi: 10.1002/(SICI)1097-0215(19980220)79:1<23::AID-IJC5>3.0.CO;2-Y . PMID 9495353.
Sasaki T, Brakebusch C, Engel J, Timpl R (1998). "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 (6): 1606–13. doi:10.1093/emboj/17.6.1606. PMC 1170508 . PMID 9501082.
Trahey M, Weissman IL (1999). "Cyclophilin C-associated protein: a normal secreted glycoprotein that down-modulates endotoxin and proinflammatory responses in vivo". Proc. Natl. Acad. Sci. U.S.A. 96 (6): 3006–11. Bibcode:1999PNAS...96.3006T. doi: 10.1073/pnas.96.6.3006 . PMC 15885 . PMID 10077627.
Tinari N, Kuwabara I, Huflejt ME, et al. (2001). "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer. 91 (2): 167–72. doi:10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q. PMID 11146440.
Hellstern S, Sasaki T, Fauser C, et al. (2002). "Functional studies on recombinant domains of Mac-2-binding protein". J. Biol. Chem. 277 (18): 15690–6. doi: 10.1074/jbc.M200386200 . PMID 11867635.
Marchetti A, Tinari N, Buttitta F, et al. (2002). "Expression of 90K (Mac-2 BP) correlates with distant metastasis and predicts survival in stage I non-small cell lung cancer patients". Cancer Res. 62 (9): 2535–9. PMID 11980646.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Zhang H, Li XJ, Martin DB, Aebersold R (2003). "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry". Nat. Biotechnol. 21 (6): 660–6. doi:10.1038/nbt827. PMID 12754519. S2CID 581283.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi: 10.1038/ng1285 . PMID 14702039.
Bouwmeester T, Bauch A, Ruffner H, et al. (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
Kristiansen TZ, Bunkenborg J, Gronborg M, et al. (2005). "A proteomic analysis of human bile". Mol. Cell. Proteomics. 3 (7): 715–28. doi: 10.1074/mcp.M400015-MCP200 . PMID 15084671.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000108679 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033880 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid7698018-5] Calabrese G, Sures I, Pompetti F, Natoli G, Palka G, Iacobelli S (May 1995). "The gene (LGALS3BP) encoding the serum protein 90K, associated with cancer and infection by the human immunodeficiency virus, maps at 17q25". Cytogenet Cell Genet. 69 (3–4): 223–5. doi:10.1159/000133969. PMID 7698018.

[pmid8034587-6] Ullrich A, Sures I, D'Egidio M, Jallal B, Powell TJ, Herbst R, Dreps A, Azam M, Rubinstein M, Natoli C, et al. (Aug 1994). "The secreted tumor-associated antigen 90K is a potent immune stimulator". J Biol Chem. 269 (28): 18401–7. doi: 10.1016/S0021-9258(17)32322-0 . PMID 8034587.

[pmid8390986-7] 1 2 Koths K, Taylor E, Halenbeck R, Casipit C, Wang A (July 1993). "Cloning and characterization of a human Mac-2-binding protein, a new member of the superfamily defined by the macrophage scavenger receptor cysteine-rich domain". J. Biol. Chem. 268 (19): 14245–9. doi: 10.1016/S0021-9258(19)85233-X . PMID 8390986.

[entrez-8] 1 2 3 "Entrez Gene: LGALS3BP lectin, galactoside-binding, soluble, 3 binding protein".

[pmid1917996-9] Rosenberg I, Cherayil BJ, Isselbacher KJ, Pillai S (October 1991). "Mac-2-binding glycoproteins. Putative ligands for a cytosolic beta-galactoside lectin". J. Biol. Chem. 266 (28): 18731–6. doi: 10.1016/S0021-9258(18)55124-3 . PMID 1917996.

[pmid11146440-10] Tinari N, Kuwabara I, Huflejt ME, Shen PF, Iacobelli S, Liu FT (January 2001). "Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates galectin-1-induced cell aggregation". Int. J. Cancer. 91 (2): 167–72. doi:10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q. PMID 11146440.

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