HTN3: Difference between revisions

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{{Infobox_gene}}
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'''Histatin 3''', also known as '''HTN3''', is a [[protein]] which in humans is encoded by the ''HTN3'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HTN3 histatin 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3347| accessdate = }}</ref><ref name="pmid2719677">{{cite journal |vauthors=Sabatini LM, Azen EA | title = Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2) | journal = Biochem. Biophys. Res. Commun. | volume = 160 | issue = 2 | pages = 495–502 |date=April 1989 | pmid = 2719677 | doi = 10.1016/0006-291X(89)92460-1| url = http://linkinghub.elsevier.com/retrieve/pii/0006-291X(89)92460-1 }}</ref>
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== Function ==
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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 [[Proteolysis|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.<ref name="entrez"/> Histatin 1 and histatin 2 are major wound-closing factors in human saliva.<ref name="pmid18650243">{{cite journal |vauthors=Oudhoff MJ, Bolscher JG, Nazmi K, Kalay H, van 't Hof W, Amerongen AV, Veerman EC | title = Histatins are the major wound-closure stimulating factors in human saliva as identified in a cell culture assay | journal = FASEB J. | volume = 22 | issue = 11 | pages = 3805–12 |date=November 2008 | pmid = 18650243 | doi = 10.1096/fj.08-112003 | url =  }}</ref>
{{GNF_Protein_box
| image = 
| image_source = 
| PDB =
| Name = Histatin 3
| HGNCid = 5284
| Symbol = HTN3
| AltSymbols =; HIS2; HTN2; HTN5
| OMIM = 142702
| ECnumber = 
| Homologene = 
| MGIid = 
| GeneAtlas_image1 = PBB_GE_HTN3_206786_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0001503 |text = ossification}} {{GNF_GO|id=GO:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0050832 |text = defense response to fungus}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3347
    | Hs_Ensembl = ENSG00000205649
    | Hs_RefseqProtein = NP_000191
    | Hs_RefseqmRNA = NM_000200
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 70928761
    | Hs_GenLoc_end = 70936834
    | Hs_Uniprot = P15516
    | Mm_EntrezGene = 
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = 
    | Mm_RefseqProtein = 
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Histatin 3''', also known as '''HTN3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HTN3 histatin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3347| accessdate = }}</ref>


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{| class="wikitable" border="1" style="text-align:center"
{{PBB_Summary
|-
| section_title =
! allele
| summary_text = 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 proteolyitic processing results in many histatins: e.g., histatins 4-6 are derived from histatin 3 by proteolysis.  Histatins are believed to have important non-immunological, anti-microbial function in the oral cavity.<ref name="entrez">{{cite web | title = Entrez Gene: HTN3 histatin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3347| accessdate = }}</ref>
! gene
}}
! protein
|-
| HIS1
| [[HTN1]]
| histatin 1
|-
| HIS2
| HTN3
| histatin 3 → histatins 4-6
|}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Troxler RF, Offner GD, Xu T, ''et al.'' |title=Structural relationship between human salivary histatins. |journal=J. Dent. Res. |volume=69 |issue= 1 |pages= 2-6 |year= 1990 |pmid= 2303595 |doi=  }}
*{{cite journal   |vauthors=Troxler RF, Offner GD, Xu T, etal |title=Structural relationship between human salivary histatins. |journal=J. Dent. Res. |volume=69 |issue= 1 |pages= 2–6 |year= 1990 |pmid= 2303595 |doi=  10.1177/00220345900690010101}}
*{{cite journal  | author=vanderSpek JC, Offner GD, Troxler RF, Oppenheim FG |title=Molecular cloning of human submandibular histatins. |journal=Arch. Oral Biol. |volume=35 |issue= 2 |pages= 137-43 |year= 1990 |pmid= 2344289 |doi=  }}
*{{cite journal  |vauthors=vanderSpek JC, Offner GD, Troxler RF, Oppenheim FG |title=Molecular cloning of human submandibular histatins. |journal=Arch. Oral Biol. |volume=35 |issue= 2 |pages= 137–43 |year= 1990 |pmid= 2344289 |doi=10.1016/0003-9969(90)90175-A }}
*{{cite journal  | author=Sugiyama K, Ogino T, Ogata K |title=Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva. |journal=Arch. Oral Biol. |volume=35 |issue= 6 |pages= 415-9 |year= 1990 |pmid= 2372245 |doi= }}
*{{cite journal  |vauthors=Sugiyama K, Ogino T, Ogata K |title=Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva. |journal=Arch. Oral Biol. |volume=35 |issue= 6 |pages= 415–9 |year= 1990 |pmid= 2372245 |doi=10.1016/0003-9969(90)90202-L  }}
*{{cite journal  | author=Sabatini LM, Azen EA |title=Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2). |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 2 |pages= 495-502 |year= 1989 |pmid= 2719677 |doi=  }}
*{{cite journal  |vauthors=Sabatini LM, Azen EA |title=Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2). |journal=Biochem. Biophys. Res. Commun. |volume=160 |issue= 2 |pages= 495–502 |year= 1989 |pmid= 2719677 |doi=10.1016/0006-291X(89)92460-1 }}
*{{cite journal | author=vanderSpek JC, Wyandt HE, Skare JC, ''et al.'' |title=Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs. |journal=Am. J. Hum. Genet. |volume=45 |issue= 3 |pages= 381-7 |year= 1989 |pmid= 2773933 |doi=  }}
*{{cite journal   |vauthors=vanderSpek JC, Wyandt HE, Skare JC, etal |title=Localization of the genes for histatins to human chromosome 4q13 and tissue distribution of the mRNAs. |journal=Am. J. Hum. Genet. |volume=45 |issue= 3 |pages= 381–7 |year= 1989 |pmid= 2773933 |doi= | pmc=1683406 }}
*{{cite journal | author=Oppenheim FG, Xu T, McMillian FM, ''et al.'' |title=Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. |journal=J. Biol. Chem. |volume=263 |issue= 16 |pages= 7472-7 |year= 1988 |pmid= 3286634 |doi=  }}
*{{cite journal   |vauthors=Oppenheim FG, Xu T, McMillian FM, etal |title=Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans. |journal=J. Biol. Chem. |volume=263 |issue= 16 |pages= 7472–7 |year= 1988 |pmid= 3286634 |doi=  }}
*{{cite journal  | author=Dickinson DP, Ridall AL, Levine MJ |title=Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence. |journal=Biochem. Biophys. Res. Commun. |volume=149 |issue= 2 |pages= 784-90 |year= 1988 |pmid= 3426601 |doi=  }}
*{{cite journal  |vauthors=Dickinson DP, Ridall AL, Levine MJ |title=Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence. |journal=Biochem. Biophys. Res. Commun. |volume=149 |issue= 2 |pages= 784–90 |year= 1988 |pmid= 3426601 |doi=10.1016/0006-291X(87)90436-0 }}
*{{cite journal  | author=Sabatini LM, Azen EA |title=Two coding change mutations in the HIS2(2) allele characterize the salivary histatin 3-2 protein variant. |journal=Hum. Mutat. |volume=4 |issue= 1 |pages= 12-9 |year= 1994 |pmid= 7951254 |doi= 10.1002/humu.1380040103 }}
*{{cite journal  |vauthors=Sabatini LM, Azen EA |title=Two coding change mutations in the HIS2(2) allele characterize the salivary histatin 3-2 protein variant. |journal=Hum. Mutat. |volume=4 |issue= 1 |pages= 12–9 |year= 1994 |pmid= 7951254 |doi= 10.1002/humu.1380040103 }}
*{{cite journal  | author=Sabatini LM, Ota T, Azen EA |title=Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family. |journal=Mol. Biol. Evol. |volume=10 |issue= 3 |pages= 497-511 |year= 1993 |pmid= 8336540 |doi=  }}
*{{cite journal  |vauthors=Sabatini LM, Ota T, Azen EA |title=Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family. |journal=Mol. Biol. Evol. |volume=10 |issue= 3 |pages= 497–511 |year= 1993 |pmid= 8336540 |doi=  }}
*{{cite journal  | author=Tsai H, Raj PA, Bobek LA |title=Candidacidal activity of recombinant human salivary histatin-5 and variants. |journal=Infect. Immun. |volume=64 |issue= 12 |pages= 5000-7 |year= 1997 |pmid= 8945538 |doi=  }}
*{{cite journal  |vauthors=Tsai H, Raj PA, Bobek LA |title=Candidacidal activity of recombinant human salivary histatin-5 and variants. |journal=Infect. Immun. |volume=64 |issue= 12 |pages= 5000–7 |year= 1997 |pmid= 8945538 |doi= | pmc=174480 }}
*{{cite journal  | author=Iontcheva I, Oppenheim FG, Offner GD, Troxler RF |title=Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. |journal=J. Dent. Res. |volume=79 |issue= 2 |pages= 732-9 |year= 2000 |pmid= 10728974 |doi= }}
*{{cite journal  |vauthors=Iontcheva I, Oppenheim FG, Offner GD, Troxler RF |title=Molecular mapping of statherin- and histatin-binding domains in human salivary mucin MG1 (MUC5B) by the yeast two-hybrid system. |journal=J. Dent. Res. |volume=79 |issue= 2 |pages= 732–9 |year= 2000 |pmid= 10728974 |doi=10.1177/00220345000790020601  }}
*{{cite journal | author=Naurato N, Wong P, Lu Y, ''et al.'' |title=Interaction of tannin with human salivary histatins. |journal=J. Agric. Food Chem. |volume=47 |issue= 6 |pages= 2229-34 |year= 2000 |pmid= 10794615 |doi=  }}
*{{cite journal   |vauthors=Naurato N, Wong P, Lu Y, etal |title=Interaction of tannin with human salivary histatins. |journal=J. Agric. Food Chem. |volume=47 |issue= 6 |pages= 2229–34 |year= 2000 |pmid= 10794615 |doi=10.1021/jf981044i }}
*{{cite journal | author=Gusman H, Travis J, Helmerhorst EJ, ''et al.'' |title=Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease. |journal=Infect. Immun. |volume=69 |issue= 3 |pages= 1402-8 |year= 2001 |pmid= 11179305 |doi= 10.1128/IAI.69.3.1402-1408.2001 }}
*{{cite journal   |vauthors=Gusman H, Travis J, Helmerhorst EJ, etal |title=Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease. |journal=Infect. Immun. |volume=69 |issue= 3 |pages= 1402–8 |year= 2001 |pmid= 11179305 |doi= 10.1128/IAI.69.3.1402-1408.2001 | pmc=98034 }}
*{{cite journal  | author=Grogan J, McKnight CJ, Troxler RF, Oppenheim FG |title=Zinc and copper bind to unique sites of histatin 5. |journal=FEBS Lett. |volume=491 |issue= 1-2 |pages= 76-80 |year= 2001 |pmid= 11226423 |doi=  }}
*{{cite journal  |vauthors=Grogan J, McKnight CJ, Troxler RF, Oppenheim FG |title=Zinc and copper bind to unique sites of histatin 5. |journal=FEBS Lett. |volume=491 |issue= 1–2 |pages= 76–80 |year= 2001 |pmid= 11226423 |doi=10.1016/S0014-5793(01)02157-3 }}
*{{cite journal | author=Gyurko C, Lendenmann U, Helmerhorst EJ, ''et al.'' |title=Killing of Candida albicans by histatin 5: cellular uptake and energy requirement. |journal=Antonie Van Leeuwenhoek |volume=79 |issue= 3-4 |pages= 297-309 |year= 2002 |pmid= 11816973 |doi=  }}
*{{cite journal   |vauthors=Gyurko C, Lendenmann U, Helmerhorst EJ, etal |title=Killing of Candida albicans by histatin 5: cellular uptake and energy requirement |journal=Antonie Van Leeuwenhoek |volume=79 |issue= 3–4 |pages= 297–309 |year= 2002 |pmid= 11816973 |doi=10.1023/A:1012070600340 }}
*{{cite journal | author=Baev D, Li XS, Dong J, ''et al.'' |title=Human salivary histatin 5 causes disordered volume regulation and cell cycle arrest in Candida albicans. |journal=Infect. Immun. |volume=70 |issue= 9 |pages= 4777-84 |year= 2002 |pmid= 12183519 |doi=  }}
*{{cite journal   |vauthors=Baev D, Li XS, Dong J, etal |title=Human salivary histatin 5 causes disordered volume regulation and cell cycle arrest in Candida albicans |journal=Infect. Immun. |volume=70 |issue= 9 |pages= 4777–84 |year= 2002 |pmid= 12183519 |doi=10.1128/IAI.70.9.4777-4784.2002  | pmc=128240 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal  | author=Li XS, Reddy MS, Baev D, Edgerton M |title=Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28553-61 |year= 2003 |pmid= 12761219 |doi= 10.1074/jbc.M300680200 }}
*{{cite journal  |vauthors=Li XS, Reddy MS, Baev D, Edgerton M |title=Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5 |journal=J. Biol. Chem. |volume=278 |issue= 31 |pages= 28553–61 |year= 2003 |pmid= 12761219 |doi= 10.1074/jbc.M300680200 }}
*{{cite journal | author=Ahmad M, Piludu M, Oppenheim FG, ''et al.'' |title=Immunocytochemical localization of histatins in human salivary glands. |journal=J. Histochem. Cytochem. |volume=52 |issue= 3 |pages= 361-70 |year= 2004 |pmid= 14966203 |doi=  }}
*{{cite journal   |vauthors=Ahmad M, Piludu M, Oppenheim FG, etal |title=Immunocytochemical localization of histatins in human salivary glands |journal=J. Histochem. Cytochem. |volume=52 |issue= 3 |pages= 361–70 |year= 2004 |pmid= 14966203 |doi=  10.1177/002215540405200307}}
*{{cite journal | author=Castagnola M, Inzitari R, Rossetti DV, ''et al.'' |title=A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway. |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41436-43 |year= 2004 |pmid= 15272024 |doi= 10.1074/jbc.M404322200 }}
*{{cite journal   |vauthors=Castagnola M, Inzitari R, Rossetti DV, etal |title=A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway |journal=J. Biol. Chem. |volume=279 |issue= 40 |pages= 41436–43 |year= 2004 |pmid= 15272024 |doi= 10.1074/jbc.M404322200 }}
}}
}}
{{refend}}
{{refend}}


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Latest revision as of 14:10, 31 August 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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. ↑ 1.0 1.1 "Entrez Gene: HTN3 histatin 3".
  2. ↑ 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.
  3. ↑ 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.

Further reading



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