DEFB103A

DEFB103B
Available structures
PDB	Human UniProt search: PDBe RCSB
List of PDB id codes
	1KJ6
Identifiers
Aliases	DEFB103B , BD-3, DEFB-3, DEFB103, DEFB3, HBD-3, HBD3, HBP-3, HBP3, defensin beta 103B
External IDs	OMIM: 606611 HomoloGene: 10256 GeneCards: DEFB103B
Gene location (Human)
Chr.	Chromosome 8 (human)
End	7,430,348 bp
RNA expression pattern
	Top expressed in
	cell; ; thymus; ; monocyte; ; blood; ; cervix; ; exocrine gland; ; fundus; ; head; ; salivary gland; ; canal of the cervix;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	CCR6 chemokine receptor binding ; chemoattractant activity ;
Cellular component	Golgi lumen ; extracellular region ; extracellular space ;
Biological process	defense response ; defense response to bacterium ; antimicrobial humoral response ; defense response to Gram-negative bacterium ; antimicrobial humoral immune response mediated by antimicrobial peptide ; defense response to Gram-positive bacterium ; chemotaxis ; positive chemotaxis ; cell chemotaxis ;
	Sources:Amigo / QuickGO
Orthologs
	55894
	n/a
	ENSG00000177243 ; ENSG00000273641
	n/a
	P81534
	n/a
	NM_018661
	n/a
	NP_001075020
	n/a
	Wikidata
View/Edit Human

Last updated August 20, 2023

Beta-defensin 103 is a protein that in humans is encoded by the DEFB103A gene.^[3]^[4]^[5]

Function

Defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Members of the defensin family are highly similar in protein sequence. This gene encodes defensin, beta 103B, which has broad spectrum antimicrobial activity and may play an important role in innate epithelial defense.^[5]

In dogs, the product of the same genetic locus, β-Defensin 103, also plays a role in pigmentation, being an agonist of the melanocortin 1 receptor.^[6]

Related Research Articles

Defensins are small cysteine-rich cationic proteins across cellular life, including vertebrate and invertebrate animals, plants, and fungi. They are host defense peptides, with members displaying either direct antimicrobial activity, immune signaling activities, or both. They are variously active against bacteria, fungi and many enveloped and nonenveloped viruses. They are typically 18-45 amino acids in length, with three or four highly conserved disulphide bonds.

Antimicrobial peptides (AMPs), also called host defence peptides (HDPs) are part of the innate immune response found among all classes of life. Fundamental differences exist between prokaryotic and eukaryotic cells that may represent targets for antimicrobial peptides. These peptides are potent, broad spectrum antimicrobials which demonstrate potential as novel therapeutic agents. Antimicrobial peptides have been demonstrated to kill Gram negative and Gram positive bacteria, enveloped viruses, fungi and even transformed or cancerous cells. Unlike the majority of conventional antibiotics it appears that antimicrobial peptides frequently destabilize biological membranes, can form transmembrane channels, and may also have the ability to enhance immunity by functioning as immunomodulators.

Dermcidin is a protein with 110 amino acids that in humans is encoded by the DCD gene. The full-length protein produces derived peptides as proteolysis-inducing factor (PIF) and other anti-microbial peptides, secreted by human eccrine sweat glands onto the skin as a part of the innate host defense of the immune system. PIF is involved in muscular proteolysis.

Chemokine ligand 20 (CCL20) or liver activation regulated chemokine (LARC) or Macrophage Inflammatory Protein-3 (MIP3A) is a small cytokine belonging to the CC chemokine family. It is strongly chemotactic for lymphocytes and weakly attracts neutrophils. CCL20 is implicated in the formation and function of mucosal lymphoid tissues via chemoattraction of lymphocytes and dendritic cells towards the epithelial cells surrounding these tissues. CCL20 elicits its effects on its target cells by binding and activating the chemokine receptor CCR6.

Cathelicidin antimicrobial peptide (CAMP) is a polypeptide that is primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs); in humans, the CAMP gene encodes the peptide precursor CAP-18, which is processed by proteinase 3-mediated extracellular cleavage into the active form LL-37. LL-37 is the only peptide in the Cathelicidin family found in the human body.

Beta-defensin 2 (BD-2) also known as skin-antimicrobial peptide 1 (SAP1) is a peptide that in humans is encoded by the DEFB4 gene.

Alpha defensins are a family of mammalian defensin peptides of the alpha subfamily. In mammals they are also known as cryptdins and are produced within the small bowel. Cryptdin is a portmanteau of crypt and defensin.

<span class="mw-page-title-main">Beta defensin</span>

Beta defensins are a family of vertebrate defensins. The beta defensins are antimicrobial peptides implicated in the resistance of epithelial surfaces to microbial colonization.

Defensin, alpha 1 also known as human alpha defensin 1, human neutrophil peptide 1 (HNP-1) or neutrophil defensin 1 is a human protein that is encoded by the DEFA1 gene. Human alpha defensin 1 belongs to the alpha defensin family of antimicrobial peptides.

Beta-defensin 1 is a protein that in humans is encoded by the DEFB1 gene.

Trefoil factor 3 is a protein that in humans is encoded by the TFF3 gene.

Arthropod defensins are a family defensin proteins found in mollusks, insects, and arachnids. These cysteine-rich antibacterial peptides are primarily active against Gram-positive bacteria and fungi in vitro. However Drosophila fruit flies mutant for the fly defensin were more susceptible to infection by the Gram-negative bacteria Providencia burhodogranariea, and resisted infection against Gram-positive bacteria like wild-type flies. It remains to be seen how in vitro activity relates to in vivo function. Mutants for the defensin-like antimicrobial peptide Drosomycin were more susceptible to fungi, validating a role for defensin-like peptides in anti-fungal defence.

Defensin, alpha 5 (DEFA5) also known as human alpha defensin 5 (HD5) is a protein that in humans is encoded by the DEFA5 gene. DEFA5 is expressed in the Paneth cells of the ileum.

Beta-defensin 106 is a protein that in humans is encoded by the DEFB106A gene.

Beta-defensin 105 is a protein that is encoded by the DEFB105A gene in humans.

Beta-defensin 119 is a protein that in humans is encoded by the DEFB119 gene.

The ocular immune system protects the eye from infection and regulates healing processes following injuries. The interior of the eye lacks lymph vessels but is highly vascularized, and many immune cells reside in the uvea, including mostly macrophages, dendritic cells, and mast cells. These cells fight off intraocular infections, and intraocular inflammation can manifest as uveitis or retinitis. The cornea of the eye is immunologically a very special tissue. Its constant exposure to the exterior world means that it is vulnerable to a wide range of microorganisms while its moist mucosal surface makes the cornea particularly susceptible to attack. At the same time, its lack of vasculature and relative immune separation from the rest of the body makes immune defense difficult. Lastly, the cornea is a multifunctional tissue. It provides a large part of the eye's refractive power, meaning it has to maintain remarkable transparency, but must also serve as a barrier to keep pathogens from reaching the rest of the eye, similar to function of the dermis and epidermis in keeping underlying tissues protected. Immune reactions within the cornea come from surrounding vascularized tissues as well as innate immune responsive cells that reside within the cornea.

Defensin, alpha 6 (DEFA6) also known as human alpha defensin 6 (HD6) is a human protein that is encoded by the DEFA6 gene. DEFA6 is expressed in the Paneth cells of the ileum.

Defensin, alpha 4 (DEFA4), also known as neutrophil defensin 4 or HNP4, is a human defensin peptide that is encoded by the DEFA4 gene. HNP4 is expressed in the granules of the neutrophil where it defends the host against bacteria and viruses.

Beta-defensin 3 is a protein that in humans is encoded by the DEFB3 gene.

References

1 2 3 ENSG00000273641 GRCh38: Ensembl release 89: ENSG00000177243, ENSG00000273641 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Jia HP, Schutte BC, Schudy A, Linzmeier R, Guthmiller JM, Johnson GK, Tack BF, Mitros JP, Rosenthal A, Ganz T, McCray PB Jr (Mar 2001). "Discovery of new human beta-defensins using a genomics-based approach". Gene. 263 (1–2): 211–8. doi:10.1016/S0378-1119(00)00569-2. PMID 11223260.
↑ Harder J, Bartels J, Christophers E, Schroder JM (Feb 2001). "Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic". J Biol Chem. 276 (8): 5707–13. doi: 10.1074/jbc.M008557200 . PMID 11085990.
1 2 "Entrez Gene: DEFB103A defensin, beta 103A".
↑ Candille SI, Kaelin CB, Cattanach BM, Yu B, Thompson DA, Nix MA, Kerns JA, Schmutz SM, Millhauser GL, Barsh GS (November 2007). "A -defensin mutation causes black coat color in domestic dogs". Science. 318 (5855): 1418–23. doi:10.1126/science.1147880. PMC 2906624 . PMID 17947548.

Hartley JL, Temple GF, Brasch MA (2001). "DNA cloning using in vitro site-specific recombination". Genome Res. 10 (11): 1788–95. doi:10.1101/gr.143000. PMC 310948 . PMID 11076863.
Tomita T, Nagase T (2001). "[Defensins as a mechanism of host defense and innate immunity]". Nippon Ronen Igakkai Zasshi. Japanese Journal of Geriatrics. 38 (4): 440–3. doi: 10.3143/geriatrics.38.440 . PMID 11523142.
García JR, Jaumann F, Schulz S, et al. (2002). "Identification of a novel, multifunctional beta-defensin (human beta-defensin 3) with specific antimicrobial activity. Its interaction with plasma membranes of Xenopus oocytes and the induction of macrophage chemoattraction". Cell Tissue Res. 306 (2): 257–64. doi:10.1007/s004410100433. PMID 11702237. S2CID 27786343.
Biragyn A, Surenhu M, Yang D, et al. (2002). "Mediators of innate immunity that target immature, but not mature, dendritic cells induce antitumor immunity when genetically fused with nonimmunogenic tumor antigens". J. Immunol. 167 (11): 6644–53. doi: 10.4049/jimmunol.167.11.6644 . PMID 11714836.
Schibli DJ, Hunter HN, Aseyev V, et al. (2002). "The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus". J. Biol. Chem. 277 (10): 8279–89. doi: 10.1074/jbc.M108830200 . PMID 11741980.
Dunsche A, Açil Y, Dommisch H, et al. (2002). "The novel human beta-defensin-3 is widely expressed in oral tissues". Eur. J. Oral Sci. 110 (2): 121–4. doi:10.1034/j.1600-0722.2002.11186.x. PMID 12013554.
Paulsen F, Pufe T, Conradi L, et al. (2003). "Antimicrobial peptides are expressed and produced in healthy and inflamed human synovial membranes". J. Pathol. 198 (3): 369–77. doi:10.1002/path.1224. PMID 12375270. S2CID 20348830.
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.
Abiko Y, Nishimura M, Kusano K, et al. (2004). "Upregulated expression of human beta defensin-1 and -3 mRNA during differentiation of keratinocyte immortalized cell lines, HaCaT and PHK16-0b". J. Dermatol. Sci. 31 (3): 225–8. doi:10.1016/S0923-1811(03)00007-0. PMID 12727027.
Nishimura M, Abiko Y, Kusano K, et al. (2003). "Localization of human beta-defensin 3 mRNA in normal oral epithelium, leukoplakia, and lichen planus: an in situ hybridization study". Medical Electron Microscopy. 36 (2): 94–7. doi:10.1007/s00795-002-0206-8. PMID 12825122. S2CID 1543924.
Wu Z, Hoover DM, Yang D, et al. (2003). "Engineering disulfide bridges to dissect antimicrobial and chemotactic activities of human beta-defensin 3". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 8880–5. doi: 10.1073/pnas.1533186100 . PMC 166407 . PMID 12840147.
King AE, Fleming DC, Critchley HO, Kelly RW (2004). "Differential expression of the natural antimicrobials, beta-defensins 3 and 4, in human endometrium". J. Reprod. Immunol. 59 (1): 1–16. doi:10.1016/S0165-0378(02)00083-9. PMID 12892899.
Chadebech P, Goidin D, Jacquet C, et al. (2004). "Use of human reconstructed epidermis to analyze the regulation of beta-defensin hBD-1, hBD-2, and hBD-3 expression in response to LPS". Cell Biol. Toxicol. 19 (5): 313–24. doi:10.1023/B:CBTO.0000004975.36521.c8. PMID 14703118. S2CID 20166061.
Pernet I, Reymermier C, Guezennec A, et al. (2004). "Calcium triggers beta-defensin (hBD-2 and hBD-3) and chemokine macrophage inflammatory protein-3 alpha (MIP-3alpha/CCL20) expression in monolayers of activated human keratinocytes". Exp. Dermatol. 12 (6): 755–60. doi:10.1111/j.0906-6705.2003.00086.x. PMID 14714554. S2CID 84942825.
Yoshimoto T, Yamaai T, Mizukawa N, et al. (2004). "Different expression patterns of beta-defensins in human squamous cell carcinomas". Anticancer Res. 23 (6C): 4629–33. PMID 14981906.
Joly S, Organ CC, Johnson GK, et al. (2005). "Correlation between beta-defensin expression and induction profiles in gingival keratinocytes". Mol. Immunol. 42 (9): 1073–84. doi:10.1016/j.molimm.2004.11.001. PMID 15829297.
Varoga D, Pufe T, Harder J, et al. (2005). "Human beta-defensin 3 mediates tissue remodeling processes in articular cartilage by increasing levels of metalloproteinases and reducing levels of their endogenous inhibitors". Arthritis Rheum. 52 (6): 1736–45. doi: 10.1002/art.21090 . PMID 15934078.
Niyonsaba F, Ushio H, Nagaoka I, et al. (2005). "The human beta-defensins (-1, -2, -3, -4) and cathelicidin LL-37 induce IL-18 secretion through p38 and ERK MAPK activation in primary human keratinocytes". J. Immunol. 175 (3): 1776–84. doi: 10.4049/jimmunol.175.3.1776 . PMID 16034119.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000273641 GRCh38: Ensembl release 89: ENSG00000177243, ENSG00000273641 - Ensembl, May 2017

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

[pmid11223260-3] Jia HP, Schutte BC, Schudy A, Linzmeier R, Guthmiller JM, Johnson GK, Tack BF, Mitros JP, Rosenthal A, Ganz T, McCray PB Jr (Mar 2001). "Discovery of new human beta-defensins using a genomics-based approach". Gene. 263 (1–2): 211–8. doi:10.1016/S0378-1119(00)00569-2. PMID 11223260.

[pmid11085990-4] Harder J, Bartels J, Christophers E, Schroder JM (Feb 2001). "Isolation and characterization of human beta -defensin-3, a novel human inducible peptide antibiotic". J Biol Chem. 276 (8): 5707–13. doi: 10.1074/jbc.M008557200 . PMID 11085990.

[entrez-5] 1 2 "Entrez Gene: DEFB103A defensin, beta 103A".

[pmid17947548-6] Candille SI, Kaelin CB, Cattanach BM, Yu B, Thompson DA, Nix MA, Kerns JA, Schmutz SM, Millhauser GL, Barsh GS (November 2007). "A -defensin mutation causes black coat color in domestic dogs". Science. 318 (5855): 1418–23. doi:10.1126/science.1147880. PMC 2906624 . PMID 17947548.

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[2]

[3]

[4]

[5]

[6]

DEFB103A

Contents

Function

Related Research Articles

References

Further reading