Histatin 3

HTN3
Identifiers
Aliases	HTN3 , HIS2, HTN2, HTN5, histatin 3, PB
External IDs	OMIM: 142702 HomoloGene: 133553 GeneCards: HTN3
Gene location (Human)
Chr.	Chromosome 4 (human)
End	70,036,538 bp
RNA expression pattern
	Top expressed in
	placenta; ; thymus; ; bone marrow; ; anterior pituitary; ; skeletal muscle tissue; ; salivary gland; ; ganglionic eminence; ; urinary bladder; ; rectum; ; gastrocnemius muscle;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	protein binding ; metal ion binding ;
Cellular component	extracellular region ; extracellular space ;
Biological process	biomineral tissue development ; defense response to bacterium ; defense response to fungus ; antimicrobial humoral response ; killing of cells of other organism ; antimicrobial humoral immune response mediated by antimicrobial peptide ;
	Sources:Amigo / QuickGO
Orthologs
	3347
	n/a
	ENSG00000205649 ; ENSG00000282967
	n/a
	P15516
	n/a
	NM_000200
	n/a
	NP_000191
	n/a
	Wikidata
View/Edit Human

Last updated March 28, 2024

Histatin 3, also known as HTN3, is a protein which in humans is encoded by the HTN3 gene.^[3]^[4]

Function

The primary protein encoded by HTN3 is histatin 3. Histatins are a family of small, histidine-rich, salivary proteins, encoded by at least two loci (HTN3 and HTN1). Post-translational proteolytic processing results in many histatins: e.g., histatins 4-6 are derived from histatin 3 by proteolysis. Histatins 1 and 3 are primary products of HIS1(1) and HIS2(1) alleles, respectively. Histatins are believed to have important non-immunological, anti-microbial function in the oral cavity.^[3] Histatin 1 and histatin 2 are major wound-closing factors in human saliva.^[5]

allele	gene	protein
HIS1	HTN1	histatin 1
HIS2	HTN3	histatin 3 → histatins 4-6

Related Research Articles

The salivary glands in many vertebrates including mammals are exocrine glands that produce saliva through a system of ducts. Humans have three paired major salivary glands, as well as hundreds of minor salivary glands. Salivary glands can be classified as serous, mucous, or seromucous (mixed).

Candida albicans is an opportunistic pathogenic yeast that is a common member of the human gut flora. It can also survive outside the human body. It is detected in the gastrointestinal tract and mouth in 40–60% of healthy adults. It is usually a commensal organism, but it can become pathogenic in immunocompromised individuals under a variety of conditions. It is one of the few species of the genus Candida that cause the human infection candidiasis, which results from an overgrowth of the fungus. Candidiasis is, for example, often observed in HIV-infected patients. C. albicans is the most common fungal species isolated from biofilms either formed on (permanent) implanted medical devices or on human tissue. C. albicans, C. tropicalis, C. parapsilosis, and C. glabrata are together responsible for 50–90% of all cases of candidiasis in humans. A mortality rate of 40% has been reported for patients with systemic candidiasis due to C. albicans. By one estimate, invasive candidiasis contracted in a hospital causes 2,800 to 11,200 deaths yearly in the US. Nevertheless, these numbers may not truly reflect the true extent of damage this organism causes, given new studies indicating that C. albicans can cross the blood–brain barrier in mice.

Histidine ammonia-lyase is an enzyme that in humans is encoded by the HAL gene. It converts histidine into ammonia and urocanic acid. Its systematic name is L-histidine ammonia-lyase (urocanate-forming).

<span class="mw-page-title-main">Histidine kinase</span>

Histidine kinases (HK) are multifunctional, and in non-animal kingdoms, typically transmembrane, proteins of the transferase class of enzymes that play a role in signal transduction across the cellular membrane. The vast majority of HKs are homodimers that exhibit autokinase, phosphotransfer, and phosphatase activity. HKs can act as cellular receptors for signaling molecules in a way analogous to tyrosine kinase receptors (RTK). Multifunctional receptor molecules such as HKs and RTKs typically have portions on the outside of the cell that bind to hormone- or growth factor-like molecules, portions that span the cell membrane, and portions within the cell that contain the enzymatic activity. In addition to kinase activity, the intracellular domains typically have regions that bind to a secondary effector molecule or complex of molecules that further propagate signal transduction within the cell. Distinct from other classes of protein kinases, HKs are usually parts of a two-component signal transduction mechanisms in which HK transfers a phosphate group from ATP to a histidine residue within the kinase, and then to an aspartate residue on the receiver domain of a response regulator protein. More recently, the widespread existence of protein histidine phosphorylation distinct from that of two-component histidine kinases has been recognised in human cells. In marked contrast to Ser, Thr and Tyr phosphorylation, the analysis of phosphorylated Histidine using standard biochemical and mass spectrometric approaches is much more challenging, and special procedures and separation techniques are required for their preservation alongside classical Ser, Thr and Tyr phosphorylation on proteins isolated from human cells.

Alpha-amylase 1 is an enzyme that in humans is encoded by the AMY1A gene. This gene is found in many organisms.

Cystatin-S is a protein that in humans is encoded by the CST4 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.

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

Cystatin-SN is a protein that in humans is encoded by the CST1 gene.

Cystatin-SA is a protein that in humans is encoded by the CST2 gene.

Basic salivary proline-rich protein 1 is a protein that in humans is encoded by the PRB1 gene.

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

Aquaporin-5 (AQP-5) is a protein that in humans is encoded by the AQP5 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.

Basic salivary proline-rich protein 4 is a protein that in humans is encoded by the PRB4 gene.

Basic salivary proline-rich protein 3 is a protein that in humans is encoded by the PRB3 gene.

28S ribosomal protein S26, mitochondrial is a protein that in humans is encoded by the MRPS26 gene.

Salivary acidic proline-rich phosphoprotein 1/2 is a protein that in humans is encoded by the PRH1 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.

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

References

1 2 3 ENSG00000282967 GRCh38: Ensembl release 89: ENSG00000205649, ENSG00000282967 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: HTN3 histatin 3".
↑ Sabatini LM, Azen EA (April 1989). "Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2)". Biochem. Biophys. Res. Commun. 160 (2): 495–502. doi:10.1016/0006-291X(89)92460-1. PMID 2719677.
↑ Oudhoff MJ, Bolscher JG, Nazmi K, Kalay H, van 't Hof W, Amerongen AV, Veerman EC (November 2008). "Histatins are the major wound-closure stimulating factors in human saliva as identified in a cell culture assay". FASEB J. 22 (11): 3805–12. doi: 10.1096/fj.08-112003 . PMID 18650243. S2CID 19797007.

Troxler RF, Offner GD, Xu T, et al. (1990). "Structural relationship between human salivary histatins". J. Dent. Res. 69 (1): 2–6. CiteSeerX 10.1.1.503.4988 . doi:10.1177/00220345900690010101. PMID 2303595. S2CID 21092156.
vanderSpek JC, Offner GD, Troxler RF, Oppenheim FG (1990). "Molecular cloning of human submandibular histatins". Arch. Oral Biol. 35 (2): 137–43. doi:10.1016/0003-9969(90)90175-A. PMID 2344289.
Sugiyama K, Ogino T, Ogata K (1990). "Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva". Arch. Oral Biol. 35 (6): 415–9. doi:10.1016/0003-9969(90)90202-L. PMID 2372245.
Sabatini LM, Azen EA (1989). "Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2)". Biochem. Biophys. Res. Commun. 160 (2): 495–502. doi:10.1016/0006-291X(89)92460-1. PMID 2719677.
vanderSpek JC, Wyandt HE, Skare JC, et al. (1989). "Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs". Am. J. Hum. Genet. 45 (3): 381–7. PMC 1683406 . PMID 2773933.
Oppenheim FG, Xu T, McMillian FM, et al. (1988). "Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans". J. Biol. Chem. 263 (16): 7472–7. doi: 10.1016/S0021-9258(18)68522-9 . PMID 3286634.
Dickinson DP, Ridall AL, Levine MJ (1988). "Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence". Biochem. Biophys. Res. Commun. 149 (2): 784–90. doi:10.1016/0006-291X(87)90436-0. PMID 3426601.
Sabatini LM, Azen EA (1994). "Two coding change mutations in the HIS2(2) allele characterize the salivary histatin 3-2 protein variant". Hum. Mutat. 4 (1): 12–9. doi: 10.1002/humu.1380040103 . PMID 7951254. S2CID 25236047.
Sabatini LM, Ota T, Azen EA (1993). "Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family". Mol. Biol. Evol. 10 (3): 497–511. doi: 10.1093/oxfordjournals.molbev.a040022 . PMID 8336540.
Tsai H, Raj PA, Bobek LA (1997). "Candidacidal activity of recombinant human salivary histatin-5 and variants". Infect. Immun. 64 (12): 5000–7. doi:10.1128/IAI.64.12.5000-5007.1996. PMC 174480 . PMID 8945538.
Iontcheva I, Oppenheim FG, Offner GD, Troxler RF (2000). "Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system". J. Dent. Res. 79 (2): 732–9. doi:10.1177/00220345000790020601. PMID 10728974. S2CID 27558675.
Naurato N, Wong P, Lu Y, et al. (2000). "Interaction of tannin with human salivary histatins". J. Agric. Food Chem. 47 (6): 2229–34. doi:10.1021/jf981044i. PMID 10794615.
Gusman H, Travis J, Helmerhorst EJ, et al. (2001). "Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease". Infect. Immun. 69 (3): 1402–8. doi:10.1128/IAI.69.3.1402-1408.2001. PMC 98034 . PMID 11179305.
Grogan J, McKnight CJ, Troxler RF, Oppenheim FG (2001). "Zinc and copper bind to unique sites of histatin 5". FEBS Lett. 491 (1–2): 76–80. doi: 10.1016/S0014-5793(01)02157-3 . PMID 11226423. S2CID 29850611.
Gyurko C, Lendenmann U, Helmerhorst EJ, et al. (2002). "Killing of Candida albicans by histatin 5: cellular uptake and energy requirement". Antonie van Leeuwenhoek. 79 (3–4): 297–309. doi:10.1023/A:1012070600340. PMID 11816973. S2CID 32933751.
Baev D, Li XS, Dong J, et al. (2002). "Human salivary histatin 5 causes disordered volume regulation and cell cycle arrest in Candida albicans". Infect. Immun. 70 (9): 4777–84. doi:10.1128/IAI.70.9.4777-4784.2002. PMC 128240 . PMID 12183519.
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.
Li XS, Reddy MS, Baev D, Edgerton M (2003). "Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5". J. Biol. Chem. 278 (31): 28553–61. doi: 10.1074/jbc.M300680200 . PMID 12761219.
Ahmad M, Piludu M, Oppenheim FG, et al. (2004). "Immunocytochemical localization of histatins in human salivary glands". J. Histochem. Cytochem. 52 (3): 361–70. doi: 10.1177/002215540405200307 . PMID 14966203.
Castagnola M, Inzitari R, Rossetti DV, et al. (2004). "A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway". J. Biol. Chem. 279 (40): 41436–43. doi: 10.1074/jbc.M404322200 . PMID 15272024.

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[refGRCh38Ensembl-1] 1 2 3 ENSG00000282967 GRCh38: Ensembl release 89: ENSG00000205649, ENSG00000282967 - Ensembl, May 2017

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

[entrez-3] 1 2 "Entrez Gene: HTN3 histatin 3".

[pmid2719677-4] Sabatini LM, Azen EA (April 1989). "Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2)". Biochem. Biophys. Res. Commun. 160 (2): 495–502. doi:10.1016/0006-291X(89)92460-1. PMID 2719677.

[pmid18650243-5] Oudhoff MJ, Bolscher JG, Nazmi K, Kalay H, van 't Hof W, Amerongen AV, Veerman EC (November 2008). "Histatins are the major wound-closure stimulating factors in human saliva as identified in a cell culture assay". FASEB J. 22 (11): 3805–12. doi: 10.1096/fj.08-112003 . PMID 18650243. S2CID 19797007.

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[2]

[3]

[4]

[5]

v t e Pore-forming toxins (TC 1C)
Antimicrobial cationic peptides	Cathelicidin Defensin Dermcidin Histatin (HTN1, HTN3)
Other, human	Perforin
Other, nonhuman	Cecropin Diphtheria toxin Dermaseptin Latarcin Magainin Melittin Nisin Pneumolysin

Histatin 3

Contents

Function

Related Research Articles

References

Further reading