DMBT1 (Deleted in malignant brain tumors 1)

Identity

Other names	gp-340 (glycoprotein-340; human)
	SAG (salivary agglutinin; human)
	apactin (mouse)
	CRP-ductin (mouse)
	gp300 (glycoprotein 300; mouse)
	muclin (mouse)
	vomeroglandin (mouse)
	ebnerin (rat)
	hensin (rabbit)
	BGM (bovine gallbladder mucin, cattle)
	H3 (rhesus monkey)
Hugo	DMBT1
Location	10q26.13
Local_order	between D10S1421 and D10S1273E

DNA/RNA

	Genomic organization of DMBT1. Top line: scale in kb. Second line: exon-intron structure of DMBT1 drawn to scale. Exons have the color code of the domains they are coding for. Exon 55 marked in black represents an exon with homology to the mouse and rat homologues, in which it codes for a transmembrane domain. Exon 55 has not yet been identified in a human transcript. Arrows depict regions, in which exon and intron sequences share high homologies. Bottom line: domain organization of the DMBT1 protein predicted from assembly of the first 54 exons. Entries to color codes and abbreviations are depicted in the section describing the protein.
Description	The gene consists of 55 exons distributed over about 80 kb. Scavenger receptor cysteine-rich (SRCR) domains are coded by single exons. Two small exons coding for serine-threonine-proline-rich stretches of 20-24 amino acids in length follow each SRCR exon. To these stretches it has been referred to as SRCR-interspersed domains (SIDs). The only exception is that there is only one of the two SID exons between SRCR4 and SRCR5.
Transcription	Longest transcript identified so far: 7656 bp including 5'-utr, exons 1-16 and exons 18-54. Various alternative transcripts with variable numbers of SRCR and SID exons exist. Exon 55 has not yet been verified to be present in human transcripts.
Pseudogene	No pseudogene known so far.

Protein

	Domain organization of DMBT1. Prototype: protein assembled from the first 54 exons (corresponding transcripts not yet identified). DMBT1/8kb.2: secreted DMBT1 variant encoded by the largest known transcript. DMBT1/6kb.1: secreted DMBT1 variant encoded by the smallest known transcript. Pink triangle: signal peptide putatively required for secretion; blue box repetitive motif of unknown function; red circles: scavenger receptor cysteine-rich (SRCR) domains; orange circles: SRCR-interspersed domains (SIDs); orange circles with TTT and STP: threonine- and serine-threonine-proline-rich domains with limited similarity to SIDs; CUB: C1r/C1s-Uegf-Bmp1 domains; ZP: zona pellucida domain.

Description	The largest known protein variant (DMBT1/8kb.2) comprises 2413 amino acids and has a calculated molecular weight of 265 kDa. Probably due to glycosylation the molecular weight of the purified protein is approximately 340 kDa. The smallest known variant (DMBT1/6kb.1), which lacks several SRCR domains and SIDs, comprises 1785 amino acids with a calculated molecular weight of 196 kDa. Various other protein variants lacking one or more SRCR domains may exist. The protein variants may arise due to genetic polymorphisms and/or alternative splicing. The SRCR domains are involved in ligand interactions. An 11 amino acid motif (GRVEVLYRGSW) present in each of the repeated SRCR domains has been shown to be responsible for the binding of a broad spectrum of Gram-positive and Gram-negative bacteria. The N-terminal SRCR1/SD1 domain has been shown to interact with HIV gp120 and to suppress HIV infection. The functions of the CUB domains and of SRCR14, which shows only limited similarity to the other SRCR domains within DMBT1, have not yet been determined. In other proteins, ZP domains have been shown to function in oligomerization. DMBT1 is also secreted as high molecular weight oligomers. SRCR, CUB, and ZP domains exclusively occur in multicellular animal organisms.
Expression	Main sites of DMBT1 expression are surface epithelial cells and associated glands, in particular in the respiratory and gastrointestinal tract. In most tissues low to moderate DMBT1 levels are expressed under normal conditions. An upregulation has been observed in response to various pathophysiological conditions, such as bacterial infection, inflammation, tumor-flanking tissues, carcinogen exposure, etc. Expression has also been noted in other tissues such as the brain and in immune cells.
Localisation	Extracellular. DMBT1 is either secreted to the mucus and other body fluids or to the extracellular matrix.
Function	DMBT1 exerts at least two distinct functions. As extracellular matrix protein, DMBT1 triggers polarity and terminal differentiation of epithelial cells as well as differentiation of embryonic stem cells to monolayered epithelia, which has been demonstrated by in vitro studies with rodent orthologs of DMBT1. DMBT1 secreted to the luminal side of epithelial surfaces plays a role in defense against bacterial and viral pathogens. This mechanism includes pathogen recognition through a peptide motif present in the SRCR domains and mediation of pathogen aggregation. DMBT1 further has been shown to exert anti-inflammatory effects. In response to activation of the intracellular pattern recognition molecule NOD2 and consecutive NFkB-activation, upregulation of DMBT1 takes place, which in turn hinders bacterial invasion and LPS-induced TLR4-activation. Hindrance of bacterial invasion may abolish NOD2 activation. Thus DMBT1 may act anti-inflammatory via inhibiting both NOD2- and TLR4-mediated NF-kB-activation. As DMBT1 is NF-kB responsive, this presumably builds up an autoregulatory homeostatic loop, by which DMBT1 is able to regulate its own expression as extracellular sensory element. These data point to a function in anti-inflammatory immune exclusion similar to mucosal antibodies (sIgA).
Homology	Homologies exist to other SRCR proteins such as CD5 and CD6, which function in immune defense. However, to date there is no SRCR protein known that additionally contains CUB and ZP domains. At the level of the SRCR domains, DMBT1 further shares some homologies with the sponge aggregation receptor (AR), which initiates the first steps in regeneration of a complete sponge body after dissociation.

Mutations

Germinal

Initial evidence has been gained that the SRCR- and SID-coding exons are subjected to copy number variations.

Somatic

Few point mutations have been identified in cancer so far. There is no hard evidence for an inactivation by biallelic mutation in cancer. Copy number variations of the SRCR- and SID-coding exons have been noted in different cancer types, including brain, lung, breast, gastrointestinal tumors and melanoma. It has not yet been determined to which extent these represent de novo rearrangements or germline mutations/polymorphisms. Underexpression has been observed for lung, colon, gastric, esophageal, breast, and skin cancer. By contrast overexpression was observed for pancreatic and prostate cancer.

Implicated in

Entity	Cancer
Disease	Based on underexpression and on its role in triggering differentiation, a role in tumor suppression of different cancer types, mainly of epithelial origin, has been proposed. A genetic scan in mice identified DMBT1 as candidate genetic modifier, which may determine the penetrance of breast cancer in the presence of p53 mutations. Lower DMBT1 protein levels have been observed in the normal mammary gland epithelium of women, which developed breast cancer versus tissues obtained from healthy donors.
Entity	Crohn's Disease
Disease	Activation of DMBT1 was found to be impaired in the intestinal epithelium of Crohn's disease with predisposing NOD2 mutations.
Entity	Infection
Disease	Based on its broad bacterial binding specificity and inhibitory effects on bacterial and viral (HIV, influenza A viruses) infection in vitro, a role in infectious diseases has been proposed.
Entity	Caries
Disease	DMBT1 alias SAG (salivary agglutinin) has been studied for about two decades as the major caries bacteria agglutinating non-immunoglobulin in the saliva/oral cavity. Based on its capacity to aggregate caries bacteria (e. g. Streptococcus mutans), it was proposed to exert functions in preventing caries. Based on its capacity to mediate bacterial adhesion to enamel-like surfaces, it was proposed to exert functions in promoting caries by other groups.

External links

	Nomenclature
Hugo	DMBT1
GDB	DMBT1
Entrez_Gene	DMBT1  1755  deleted in malignant brain tumors 1
	Cards
Atlas	DMBT1ID309ch10q26
GeneCards	DMBT1
Ensembl	DMBT1 [Search_View]   ENSG00000187908 [Gene_View]
Genatlas	DMBT1
GeneLynx	DMBT1
eGenome	DMBT1
euGene	1755
	Genomic and cartography
GoldenPath	DMBT1  -  10q26.13   chr10:124310171-124393242 +  10q25.3-q26.1   [Description]    (hg18-Mar_2006)
Ensembl	DMBT1 - 10q25.3-q26.1 [CytoView]
NCBI	Mapview
OMIM	Disease map [OMIM]
HomoloGene	DMBT1
	Gene and transcription
Genbank	AB209691 [ ENTREZ ]
Genbank	AF159456 [ ENTREZ ]
Genbank	AJ000342 [ ENTREZ ]
Genbank	AJ243212 [ ENTREZ ]
Genbank	AJ243224 [ ENTREZ ]
RefSeq	NM_004406 [ SRS ]    NM_004406 [ ENTREZ ]
RefSeq	NM_007329 [ SRS ]    NM_007329 [ ENTREZ ]
RefSeq	NM_017579 [ SRS ]    NM_017579 [ ENTREZ ]
RefSeq	AC_000142 [ SRS ]    AC_000142 [ ENTREZ ]
RefSeq	NC_000010 [ SRS ]    NC_000010 [ ENTREZ ]
RefSeq	NT_030059 [ SRS ]    NT_030059 [ ENTREZ ]
RefSeq	NW_001838006 [ SRS ]    NW_001838006 [ ENTREZ ]
AceView	DMBT1 AceView - NCBI
Unigene	Hs.279611 [ SRS ]    Hs.279611 [ NCBI ]     HS279611 [ spliceNest ]
Fast-db	16977 (alternative variants)
	Protein : pattern, domain, 3D structure
HPRD	03575
	Protein Interaction databases
	Polymorphism : SNP, mutations, diseases
OMIM	137800;155255;601969    [ map ]
GENECLINICS	137800;155255;601969
SNP	DMBT1 [dbSNP-NCBI]
SNP	NM_004406 [SNP-NCI]
SNP	NM_007329 [SNP-NCI]
SNP	NM_017579 [SNP-NCI]
SNP	DMBT1 [GeneSNPs - Utah]  DMBT1] [HGBASE - SRS]
HAPMAP	DMBT1 [HAPMAP]
HGMD	DMBT1
	General knowledge
Family Browser	DMBT1 [UCSC Family Browser]
SOURCE	NM_004406
SOURCE	NM_007329
SOURCE	NM_017579
SMD	Hs.279611
SAGE	Hs.279611
GO	scavenger receptor activity [Amigo]  scavenger receptor activity
GO	scavenger receptor activity [Amigo]  scavenger receptor activity
GO	extracellular region [Amigo]  extracellular region
GO	cytoplasm [Amigo]  cytoplasm
GO	pattern recognition receptor activity [Amigo]  pattern recognition receptor activity
GO	membrane [Amigo]  membrane
GO	phagocytic vesicle membrane [Amigo]  phagocytic vesicle membrane
GO	epithelial cell differentiation [Amigo]  epithelial cell differentiation
GO	epithelial cell differentiation [Amigo]  epithelial cell differentiation
GO	induction of bacterial agglutination [Amigo]  induction of bacterial agglutination
GO	innate immune response [Amigo]  innate immune response
GO	negative regulation of cell cycle [Amigo]  negative regulation of cell cycle
GO	calcium-dependent protein binding [Amigo]  calcium-dependent protein binding
PubGene	DMBT1
TreeFam	DMBT1
CTD	1755 [Comparative ToxicoGenomics Database]
	Other databases
Other database	Largest DMBT1 variant (DMBT1/8kb.2)
Other database	Smallest DMBT1 variant (DMBT1/6kb.1)
	Probes
Probe	DMBT1 Related clones (RZPD - Berlin)
	PubMed
PubMed	54 Pubmed reference(s) in LocusLink

Bibliography

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British journal of cancer. 1999 ; 79 (2) : 211-213.

PMID 9888459

Expression of the DMBT1 gene is frequently suppressed in human lung cancer.

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PMID 10551316

Hensin, the polarity reversal protein, is encoded by DMBT1, a gene frequently deleted in malignant gliomas.

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The American journal of physiology. 1999 ; 277 (2 Pt 2) : F277-F289.

PMID 10444583

Hensin remodels the apical cytoskeleton and induces columnarization of intercalated epithelial cells: processes that resemble terminal differentiation.

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The Journal of cell biology. 1999 ; 144 (5) : 1057-1067.

PMID 10085301

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Cancer research. 1999 ; 59 (8) : 1846-1851.

PMID 10213490

Processing of pro-Muclin and divergent trafficking of its products to zymogen granules and the apical plasma membrane of pancreatic acinar cells.

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PMID 11152281

Induction of terminal differentiation in epithelial cells requires polymerization of hensin by galectin 3.

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The Journal of cell biology. 2000 ; 151 (6) : 1235-1246.

PMID 11121438

DMBT1 encodes a protein involved in the immune defense and in epithelial differentiation and is highly unstable in cancer.

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PMID 10749143

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The Journal of biological chemistry. 2000 ; 275 (51) : 39860-39866.

PMID 11007786

Human salivary agglutinin binds to lung surfactant protein-D and is identical with scavenger receptor protein gp-340.

Ligtenberg TJ, Bikker FJ, Groenink J, Tornoe I, Leth-Larsen R, Veerman EC, Nieuw Amerongen AV, Holmskov U

The Biochemical journal. 2001 ; 359 (Pt 1) : 243-248.

PMID 11563989

Deleted in Malignant Brain Tumors 1 is a versatile mucin-like molecule likely to play a differential role in digestive tract cancer.

Mollenhauer J, Herbertz S, Helmke B, Kollender G, Krebs I, Madsen J, Holmskov U, Sorger K, Schmitt L, Wiemann S, Otto HF, Grˆ�ne HJ, Poustka A

Cancer research. 2001 ; 61 (24) : 8880-8886.

PMID 11751412

Identification of the bacteria-binding peptide domain on salivary agglutinin (gp-340/DMBT1), a member of the scavenger receptor cysteine-rich superfamily.

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The Journal of biological chemistry. 2002 ; 277 (35) : 32109-32115.

PMID 12050164

Heterogeneity of ductular reactions in adult rat and human liver revealed by novel expression of deleted in malignant brain tumor 1.

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PMID 12368192

Sequential changes of the DMBT1 expression and location in normal lung tissue and lung carcinomas.

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PMID 12203780

The SRCR/SID region of DMBT1 defines a complex multi-allele system representing the major basis for its variability in cancer.

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PMID 12353266

Rare mutations of the DMBT1 gene in human astrocytic gliomas.

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PMID 12185598

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PMID 11912156

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PMID 12208737

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PMID 14515985

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American journal of physiology. Lung cellular and molecular physiology. 2003 ; 285 (5) : L1066-L1076.

PMID 12871854

DMBT1, a regulator of mucosal homeostasis through the linking of mucosal defense and regeneration?

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PMID 12681477

CRP-ductin, the mouse homologue of gp-340/deleted in malignant brain tumors 1 (DMBT1), binds gram-positive and gram-negative bacteria and interacts with lung surfactant protein D.

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PMID 12689412

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PMID 14511252

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Bikker FJ, Ligtenberg AJ, End C, Renner M, Blaich S, Lyer S, Wittig R, van't Hof W, Veerman EC, Nazmi K, de Blieck-Hogervorst JM, Kioschis P, Nieuw Amerongen AV, Poustka A, Mollenhauer J

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PMID 15355985

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PMID 15477757

Carcinogen inducibility in vivo and down-regulation of DMBT1 during breast carcinogenesis.

Mollenhauer J, Helmke B, Medina D, Bergmann G, Gassler N, Mˆºller H, Lyer S, Diedrichs L, Renner M, Wittig R, Blaich S, Hamann U, Madsen J, Holmskov U, Bikker F, Ligtenberg A, Carlˆ©n A, Olsson J, Otto HF, O'Malley B, Poustka A

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PMID 14732920

Inflammation of the cystic fibrosis mouse small intestine.

Norkina O, Kaur S, Ziemer D, De Lisle RC

American journal of physiology. Gastrointestinal and liver physiology. 2004 ; 286 (6) : G1032-G1041.

PMID 14739145

The Scavenger Receptor Cysteine-Rich (SRCR) domain: an ancient and highly conserved protein module of the innate immune system.

Sarrias MR, Grˆ½nlund J, Padilla O, Madsen J, Holmskov U, Lozano F

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PMID 14995912

Conversion of ES cells to columnar epithelia by hensin and to squamous epithelia by laminin.

Takito J, Al-Awqati Q

The Journal of cell biology. 2004 ; 166 (7) : 1093-1102.

PMID 15452149

gp340 (SAG) binds to the V3 sequence of gp120 important for chemokine receptor interaction.

Wu Z, Golub E, Abrams WR, Malamud D

AIDS research and human retroviruses. 2004 ; 20 (6) : 600-607.

PMID 15242536

Induction of DMBT1 expression by reduced ERK activity during a gastric mucosa differentiation-like process and its association with human gastric cancer.

Kang W, Nielsen O, Fenger C, Leslie G, Holmskov U, Reid KB

Carcinogenesis. 2005 ; 26 (6) : 1129-1137.

PMID 15760920

Respiratory innate immune proteins differentially modulate the neutrophil respiratory burst response to influenza A virus.

White MR, Crouch E, Vesona J, Tacken PJ, Batenburg JJ, Leth-Larsen R, Holmskov U, Hartshorn KL

American journal of physiology. Lung cellular and molecular physiology. 2005 ; 289 (4) : L606-L616.

PMID 15951332

Prostatic intraepithelial neoplasia and adenocarcinoma in mice expressing a probasin-Neu oncogenic transgene.

Li Z, Szabolcs M, Terwilliger JD, Efstratiadis A

Carcinogenesis. 2006 ; 27 (5) : 1054-1067.

PMID 16401639

The N-terminal SRCR-SID domain of gp-340 interacts with HIV type 1 gp120 sequences and inhibits viral infection.

Wu Z, Lee S, Abrams W, Weissman D, Malamud D

AIDS research and human retroviruses. 2006 ; 22 (6) : 508-515.

PMID 16796526

Genetic mapping in mice identifies DMBT1 as a candidate modifier of mammary tumors and breast cancer risk.

Blackburn AC, Hill LZ, Roberts AL, Wang J, Aud D, Jung J, Nikolcheva T, Allard J, Peltz G, Otis CN, Cao QJ, Ricketts RS, Naber SP, Mollenhauer J, Poustka A, Malamud D, Jerry DJ

The American journal of pathology. 2007 ; 170 (6) : 2030-2041.

PMID 17525270

Innate immunity glycoprotein gp-340 variants may modulate human susceptibility to dental caries.

Jonasson A, Eriksson C, Jenkinson HF, Kˆ§llestˆ€l C, Johansson I, Strˆ�mberg N

BMC infectious diseases. 2007 ; 7 : page 57.

PMID 17562017

Regulation of DMBT1 via NOD2 and TLR4 in intestinal epithelial cells modulates bacterial recognition and invasion.

Rosenstiel P, Sina C, End C, Renner M, Lyer S, Till A, Hellmig S, Nikolaus S, Fˆ�lsch UR, Helmke B, Autschbach F, Schirmacher P, Kioschis P, Hafner M, Poustka A, Mollenhauer J, Schreiber S

Journal of immunology (Baltimore, Md. : 1950). 2007 ; 178 (12) : 8203-8211.

PMID 17548659

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Contributor(s)

Written	08-2007	Jan Mollenhauer, Annemarie Poustka
		Division of Molecular Genome Analysis, German Cancer Research Center, Im Neuenheimer, Feld 280, 69120 Heidelberg, Germany

Citation

This paper should be referenced as such :

Mollenhauer J, Poustka A . DMBT1 (Deleted in malignant brain tumors 1). Atlas Genet Cytogenet Oncol Haematol. August 2007 . URL : http://AtlasGeneticsOncology.org/Genes/DMBT1ID309ch10q26.html

© Atlas of Genetics and Cytogenetics in Oncology and Haematology

indexed on : Mon Jul 14 17:43:43 2008