Mucin 7

MUC7
Identifiers
Aliases	MUC7 , MG2, mucin 7, secreted
External IDs	OMIM: 158375 HomoloGene: 133350 GeneCards: MUC7
Gene location (Human)
Chr.	Chromosome 4 (human)
End	70,482,997 bp
RNA expression pattern
	Top expressed in
	trachea; ; parotid gland; ; minor salivary gland; ; palpebral conjunctiva; ; amniotic fluid; ; tongue; ; right lung; ; superior surface of tongue; ; body of tongue; ; skin of abdomen;
	n/a
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	protein binding ;
Cellular component	Golgi lumen ; extracellular region ; extracellular exosome ; plasma membrane ;
Biological process	O-glycan processing ; stimulatory C-type lectin receptor signaling pathway ; antimicrobial humoral immune response mediated by antimicrobial peptide ;
	Sources:Amigo / QuickGO
Orthologs
	4589
	n/a
	ENSG00000171195
	n/a
	Q8TAX7
	n/a
	NM_152291 ; NM_001145006 ; NM_001145007
	n/a
	NP_001138478 ; NP_001138479 ; NP_689504
	n/a
	Wikidata
View/Edit Human

Last updated August 19, 2023

Mucin-7 is a protein that in humans is encoded by the MUC7 gene.^[3]^[4] In animals, the MUC7 gene is found in most placental mammals, but not marsupials.^[5]

Human variations

Humans carry either a five or six tandem repeat version of the gene. In other primates, the number of repeats found is 4-5 for gorillas, 5 for chimpanzees, 6-7 for orangutans, 8-10 for macaques, 10-11 for baboons and 11-12 for green monkeys.^[5]

Related Research Articles

Mucins are a family of high molecular weight, heavily glycosylated proteins (glycoconjugates) produced by epithelial tissues in most animals. Mucins' key characteristic is their ability to form gels; therefore they are a key component in most gel-like secretions, serving functions from lubrication to cell signalling to forming chemical barriers. They often take an inhibitory role. Some mucins are associated with controlling mineralization, including nacre formation in mollusks, calcification in echinoderms and bone formation in vertebrates. They bind to pathogens as part of the immune system. Overexpression of the mucin proteins, especially MUC1, is associated with many types of cancer.

The enzyme UDP-glucose 4-epimerase, also known as UDP-galactose 4-epimerase or GALE, is a homodimeric epimerase found in bacterial, fungal, plant, and mammalian cells. This enzyme performs the final step in the Leloir pathway of galactose metabolism, catalyzing the reversible conversion of UDP-galactose to UDP-glucose. GALE tightly binds nicotinamide adenine dinucleotide (NAD+), a co-factor required for catalytic activity.

Histatin 3, also known as HTN3, is a protein which in humans is encoded by the HTN3 gene.

Statherin is a protein in humans that is encoded by the STATH gene. It prevents the precipitation of calcium phosphate in saliva, maintaining a high calcium level in saliva available for remineralisation of tooth enamel and high phosphate levels for buffering.

Polypeptide N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the GALNT1 gene.

Histatin-1 is a protein that in humans is encoded by the HTN1 gene.

Alpha-(1,3)-fucosyltransferase is an enzyme that in humans is encoded by the FUT9 gene.

Polypeptide N-acetylgalactosaminyltransferase 2 is an enzyme that in humans is encoded by the GALNT2 gene.

Oviduct-specific glycoprotein also known as oviductal glycoprotein(OGP) or estrogen-dependent oviduct protein, oviductin or mucin-9 is a protein that in humans is encoded by the OVGP1 gene.

UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 is an enzyme that in humans is encoded by the B3GNT2 gene.

Beta-1,3-galactosyltransferase 5 is an enzyme that in humans is encoded by the B3GALT5 gene.

Polypeptide N-acetylgalactosaminyltransferase 6 is an enzyme that in humans is encoded by the GALNT6 gene.

Polypeptide N-acetylgalactosaminyltransferase 13 is an enzyme that in humans is encoded by the GALNT13 gene.

Chondroitin sulfate N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the CSGALNACT1 gene.

Polypeptide N-acetylgalactosaminyltransferase 14 is an enzyme that in humans is encoded by the GALNT14 gene.

Core 1 synthase, glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase, 1, also known as C1GALT1, is an enzyme which in humans is encoded by the C1GALT1 gene.

Histatins are histidine-rich (cationic) antimicrobial proteins found in saliva. Histatin's involvement in antimicrobial activities makes histatin part of the innate immune system.

(N-acetylneuraminyl)-galactosylglucosylceramide N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:1-O-(O- - -O-beta-D-galactopyranosyl- -beta-D-glucopyranosyl)-ceramide 4-beta-N-acetyl-D-galactosaminyltransferase. This enzyme catalyses the following chemical reaction

N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase is an enzyme with systematic name UDP-N-acetyl-D-galactosamine:N-acetyl-beta-D-glucosaminyl-group 4-beta-N-acetylgalactosaminyltransferase. This enzyme catalyses the following chemical reaction

Proline-rich protein HaeIII subfamily 2 is a protein that in humans is encoded by the PRH2 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000171195 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Bobek LA, Liu J, Sait SN, Shows TB, Bobek YA, Levine MJ (February 1996). "Structure and chromosomal localization of the human salivary mucin gene, MUC7". Genomics. 31 (3): 277–82. doi:10.1006/geno.1996.0049. PMID 8838308.
↑ "Entrez Gene: MUC7 mucin 7, secreted".
1 2 Xu D, Pavlidis P, Thamadilok S, Redwood E, Fox S, Blekhman R, Ruhl S, Gokcumen O (August 2016). "Recent evolution of the salivary mucin MUC7". Scientific Reports. 6: 31791. Bibcode:2016NatSR...631791X. doi:10.1038/srep31791. PMC 4997351 . PMID 27558399. This article contains quotations from this source, which is available under the Creative Commons Attribution 4.0 International (CC BY 4.0) license.

Zalewska A, Zwierz K, Zółkowski K, Gindzieński A (2002). "Structure and biosynthesis of human salivary mucins". Acta Biochimica Polonica. 47 (4): 1067–79. doi: 10.18388/abp.2000_3960 . PMID 11996097.
Bobek LA, Tsai H, Biesbrock AR, Levine MJ (September 1993). "Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7)". The Journal of Biological Chemistry. 268 (27): 20563–9. doi: 10.1016/S0021-9258(20)80762-5 . PMID 7690757.
Troxler RF, Iontcheva I, Oppenheim FG, Nunes DP, Offner GD (October 1997). "Molecular characterization of a major high molecular weight mucin from human sublingual gland". Glycobiology. 7 (7): 965–73. doi: 10.1093/glycob/7.7.965 . PMID 9363439.
Prakobphol A, Thomsson KA, Hansson GC, Rosen SD, Singer MS, Phillips NJ, Medzihradszky KF, Burlingame AL, Leffler H, Fisher SJ (April 1998). "Human low-molecular-weight salivary mucin expresses the sialyl lewisx determinant and has L-selectin ligand activity". Biochemistry. 37 (14): 4916–27. doi:10.1021/bi972612a. PMID 9538010.
Kirkbride HJ, Bolscher JG, Nazmi K, Vinall LE, Nash MW, Moss FM, Mitchell DM, Swallow DM (May 2001). "Genetic polymorphism of MUC7: allele frequencies and association with asthma". European Journal of Human Genetics. 9 (5): 347–54. doi: 10.1038/sj.ejhg.5200642 . PMID 11378823.
Guo JM, Zhang Y, Cheng L, Iwasaki H, Wang H, Kubota T, Tachibana K, Narimatsu H (July 2002). "Molecular cloning and characterization of a novel member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, pp-GalNAc-T12". FEBS Letters. 524 (1–3): 211–8. doi: 10.1016/S0014-5793(02)03007-7 . PMID 12135769. S2CID 84453381.
Cheng L, Tachibana K, Zhang Y, Guo J, Kahori Tachibana K, Kameyama A, Wang H, Hiruma T, Iwasaki H, Togayachi A, Kudo T, Narimatsu H (November 2002). "Characterization of a novel human UDP-GalNAc transferase, pp-GalNAc-T10". FEBS Letters. 531 (2): 115–21. doi:10.1016/S0014-5793(02)03399-9. PMID 12417297. S2CID 221288147.
Banderas-Tarabay JA, Zacarías-D'Oleire IG, Garduño-Estrada R, Aceves-Luna E, González-Begné M (2003). "Electrophoretic analysis of whole saliva and prevalence of dental caries. A study in Mexican dental students". Archives of Medical Research. 33 (5): 499–505. doi:10.1016/S0188-4409(02)00395-8. PMID 12459324.
Wang H, Tachibana K, Zhang Y, Iwasaki H, Kameyama A, Cheng L, Guo J, Hiruma T, Togayachi A, Kudo T, Kikuchi N, Narimatsu H (January 2003). "Cloning and characterization of a novel UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, pp-GalNAc-T14". Biochemical and Biophysical Research Communications. 300 (3): 738–44. doi:10.1016/S0006-291X(02)02908-X. PMID 12507512.
Soares RV, Siqueira CC, Bruno LS, Oppenheim FG, Offner GD, Troxler RF (June 2003). "MG2 and lactoferrin form a heterotypic complex in salivary secretions". Journal of Dental Research. 82 (6): 471–5. doi:10.1177/154405910308200613. PMID 12766201. S2CID 23276142.
Ge J, Catt DM, Gregory RL (November 2004). "Streptococcus mutans surface alpha-enolase binds salivary mucin MG2 and human plasminogen". Infection and Immunity. 72 (11): 6748–52. doi:10.1128/IAI.72.11.6748-6752.2004. PMC 523000 . PMID 15501816.
Grys TE, Siegel MB, Lathem WW, Welch RA (March 2005). "The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to host cells". Infection and Immunity. 73 (3): 1295–303. doi:10.1128/IAI.73.3.1295-1303.2005. PMC 1064933 . PMID 15731026.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Bruno LS, Li X, Wang L, Soares RV, Siqueira CC, Oppenheim FG, Troxler RF, Offner GD (October 2005). "Two-hybrid analysis of human salivary mucin MUC7 interactions". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1746 (1): 65–72. doi:10.1016/j.bbamcr.2005.08.007. PMID 16203048.
Li S, Intini G, Bobek LA (July 2006). "Modulation of MUC7 mucin expression by exogenous factors in airway cells in vitro and in vivo". American Journal of Respiratory Cell and Molecular Biology. 35 (1): 95–102. doi:10.1165/rcmb.2005-0305OC. PMC 2658701 . PMID 16514118.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000171195 - Ensembl, May 2017

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

[pmid8838308-3] Bobek LA, Liu J, Sait SN, Shows TB, Bobek YA, Levine MJ (February 1996). "Structure and chromosomal localization of the human salivary mucin gene, MUC7". Genomics. 31 (3): 277–82. doi:10.1006/geno.1996.0049. PMID 8838308.

[entrez-4] "Entrez Gene: MUC7 mucin 7, secreted".

[Xu_Pavlidis_Thamadilok_Redwood_2016-5] 1 2 Xu D, Pavlidis P, Thamadilok S, Redwood E, Fox S, Blekhman R, Ruhl S, Gokcumen O (August 2016). "Recent evolution of the salivary mucin MUC7". Scientific Reports. 6: 31791. Bibcode:2016NatSR...631791X. doi:10.1038/srep31791. PMC 4997351 . PMID 27558399. This article contains quotations from this source, which is available under the Creative Commons Attribution 4.0 International (CC BY 4.0) license.

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Mucin 7

Contents

Human variations

Related Research Articles

References

Further reading