HTN3

Histatin 3

Identifiers

HTN3 ; HIS2; HTN2; HTN5

External IDs

OMIM: 142702 HomoloGene: 133553 GeneCards: HTN3 Gene

Gene ontology
Molecular function	• protein binding • metal ion binding
Cellular component	• extracellular region
Biological process	• biomineral tissue development • killing of cells of other organism • defense response to bacterium • defense response to fungus
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

n/a

n/a

n/a

RefSeq (mRNA)

NM_000200

n/a

RefSeq (protein)

NP_000191

n/a

Location (UCSC)

Chr 4:
70.89 – 70.9 Mb

n/a

PubMed search

n/a

Histatin 3, also known as HTN3, is a protein which in humans is encoded by the HTN3 gene.^[1]^[2]

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.^[1] Histatin 1 and histatin 2 are major wound-closing factors in human saliva.^[3]

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

References

↑ 1.0 1.1 "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.

Troxler RF, Offner GD, Xu T et al. (1990). "Structural relationship between human salivary histatins.". J. Dent. Res. 69 (1): 2–6. doi:10.1177/00220345900690010101. PMID 2303595.
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. 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.
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. 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. 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.
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.
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.
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. 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.

Pore-forming toxins (TC 1C)

Antimicrobial cationic peptides

Other, human

Perforin

Other, nonhuman

Index of cells

Description	Structure nucleus chromosome genetics Organelles peroxisome cytoskeleton centrosome epithelia cilia mitochondria Membranes proteins cell adhesions Membrane transport ion channels vesicular transport solute carrier ABC transporters ATPase oxidoreduction-driven

Disease	Structural peroxisome cytoskeleton cilia mitochondria nucleus scleroprotein Membrane channelopathy solute carrier ATPase ABC transporters other extracellular ligands cell surface receptors intracellular signalling Vesicular transport Pore-forming toxins

HTN3

Function

References

Further reading