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1.C.79.1.1
Histatin 3 precursor of 51 aas and 1 N-terminal TMS.  Histatins are salivary proteins that are major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C. albicans and C. neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P. gingivalis (Gusman et al. 2001; Tsai et al. 1996). The His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9. It may kill cells by volume dysregulation and ion imbalance triggered by osmotic stress (Puri and Edgerton 2014). Histatins also promote wound healing (Torres et al. 2018).

Accession Number:P15516
Protein Name:Histatin-3
Length:51
Molecular Weight:6149.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Secreted1
Substrate ATP

Cross database links:

RefSeq: NP_000191.1   
Entrez Gene ID: 3347   
OMIM: 142702  gene
KEGG: hsa:3347   

Gene Ontology

GO:0005576 C:extracellular region
GO:0046872 F:metal ion binding
GO:0005515 F:protein binding
GO:0031214 P:biomineral formation
GO:0042742 P:defense response to bacterium
GO:0050832 P:defense response to fungus
GO:0031640 P:killing of cells of another organism

References (15)

[1] “Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2).”  Sabatini L.M.et.al.   2719677
[2] “Human submandibular gland statherin and basic histidine-rich peptide are encoded by highly abundant mRNA's derived from a common ancestral sequence.”  Dickinson D.P.et.al.   3426601
[3] “Molecular cloning of human submandibular histatins.”  Vanderspek J.C.et.al.   2344289
[4] “Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family.”  Chen Z.W.et.al.   8336540
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Two coding change mutations in the HIS2(2) allele characterize the salivary histatin 3-2 protein variant.”  Sabatini L.M.et.al.   7951254
[7] “Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.”  Oppenheim F.G.et.al.   3286634
[8] “Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva.”  Sugiyama K.et.al.   2372245
[9] “A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway.”  Castagnola M.et.al.   15272024
[10] “Candidacidal activity of recombinant human salivary histatin-5 and variants.”  Tsai H.et.al.   8945538
[11] “Zinc and copper bind to unique sites of histatin 5.”  Grogan J.et.al.   11226423
[12] “Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease.”  Gusman H.et.al.   11179305
[13] “Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5.”  Li X.S.et.al.   12761219
[14] “Immunocytochemical localization of histatins in human salivary glands.”  Ahmad M.et.al.   14966203
[15] “Tyrosine polysulfation of human salivary histatin 1. A post-translational modification specific of the submandibular gland.”  Cabras T.et.al.   17503797

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FASTA formatted sequence 
1:	MKFFVFALIL ALMLSMTGAD SHAKRHHGYK RKFHEKHHSH RGYRSNYLYD N