AMPDB_165 | Histatin-3

1 General Description

AMPDB ID: AMPDB_165

Protein Names: Histatin-3 (Basic histidine-rich protein) (Hst) (Histidine-rich protein 3) (PB) [Cleaved into: Histatin-3; His3-(20-44)-peptide (His3 20 44) (His3-(1-25)-peptide) (His3 1 25) (Histatin-3 1 25) (Histatin-6); His3-(20-43)-peptide (His3 20 43) (His3-(1-24)-peptide) (His3 1 24) (Histatin-3 1 24) (Histatin-5); His3-(20-32)-peptide (His3 20 32) (His3-(1-13)-peptide) (His3 1 13) (Histatin-3 1 13); His3-(20-31)-peptide (His3 20 31) (His3-(1-12)-peptide) (His3 1 12) (Histatin-3 1 12); His3-(20-30)-peptide (His3 20 30) (His3-(1-11)-peptide) (His3 1 11) (Histatin-3 1 11); His3-(24-32)-peptide (His3 24 32) (His3-(5-13)-peptide) (His3 5 13) (Histatin-3 5 13); His3-(24-31)-peptide (His3 24 31) (His3-(5-12)-peptide) (His3 5 12) (Histatin-11) (Histatin-3 5 12); His3-(24-30)-peptide (His3 24 30) (His3-(5-11)-peptide) (His3 5 11) (Histatin-12) (Histatin-3 5 11); His3-(25-32)-peptide (His3 25 32) (His3-(6-13)-peptide) (His3 6 13) (Histatin-3 6 13); His3-(25-30)-peptide (His3 25 30) (His3-(6-11)-peptide) (His3 6 11) (Histatin-3 6 11); His3-(26-32)-peptide (His3 26 32) (His3-(7-13)-peptide) (His3 7 13) (Histatin-3 7 13); His3-(26-31)-peptide (His3 26 31) (His3-(7-12)-peptide) (His3 7 12) (Histatin-3 7 12); His3-(26-30)-peptide (His3 26 30) (His3-(7-11)-peptide) (His3 7 11) (Histatin-3 7 11); His3-(31-51)-peptide (His3 31 51) (His3-(12-32)-peptide) (His3 12 32) (Histatin-3 12 32) (Histatin-4); His3-(31-44)-peptide (His3 31 44) (His3-(12-25)-peptide) (His3 12 25) (Histatin-3 12 25) (Histatin-9); His3-(31-43)-peptide (His3 31 43) (His3-(12-24)-peptide) (His3 12 24) (Histatin-3 12 24) (Histatin-7); His3-(32-44)-peptide (His3 32 44) (His3-(13-25)-peptide) (His3 13 25) (Histatin-10) (Histatin-3 13 25); His3-(32-43)-peptide (His3 32-43) (His3-(13-24)-peptide) (His3 13 24) (Histatin-3 13 24) (Histatin-8); His3-(33-44)-peptide (His3 33 44) (His3-(14-25)-peptide) (His3 14 25) (Histatin-3 14 25); His3-(33-43)-peptide (His3 33 43) (His3-(14-24)-peptide) (His3 14 24) (Histatin-3 14 24); His3-(34-44)-peptide (His3 34 44) (His3-(15-25)-peptide) (His3 15 25) (Histatin-3 15 25); His3-(34-43)-peptide (His3 34 43) (His3-(15-24)-peptide) (His3 15 24) (Histatin-3 15 24); His3-(45-51)-peptide (His3 45 51) (His3-(26-32)-peptide) (His3 26 32) (Histatin-3 26 32); His3-(47-51)-peptide (His3 47 51) (His3-(28-32)-peptide) (His3 28 32) (Histatin-3 28 32); His3-(48-51)-peptide (His3 48 51) (His3-(29-32)-peptide) (His3 29 32) (Histatin-3 29 32)]

Protein Family: Histatin statherin family

Gene Name: HTN3 HIS2

Source Organism: Homo sapiens (Human)

Protein Length: 51 AA

Protein Existence: Evidence at protein level

2 Protein Sequence & Composition

MKFFVFALILALMLSMTGADSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN

FASTA format

Counts of Amino Acids

'A': 4, 'R': 4, 'N': 2, 'D': 2, 'C': 0, 'Q': 0, 'E': 1, 'G': 3, 'H': 7, 'I': 1, 'L': 5, 'K': 5, 'M': 3, 'F': 4, 'P': 0, 'S': 4, 'T': 1, 'W': 0, 'Y': 4, 'V': 1

Frequencies of Amino Acids

'A': 7.84%, 'R': 7.84%, 'N': 3.92%, 'D': 3.92%, 'C': 0%, 'Q': 0%, 'E': 1.96%, 'G': 5.88%, 'H': 13.73%, 'I': 1.96%, 'L': 9.8%, 'K': 9.8%, 'M': 5.88%, 'F': 7.84%, 'P': 0%, 'S': 7.84%, 'T': 1.96%, 'W': 0%, 'Y': 7.84%, 'V': 1.96%

Missing Amino Acid(s)

C, P, Q, W

Most Occurring Amino Acid(s)

Less Occurring Amino Acid(s)

E, I, T, V

Hydrophobic Amino Acid(s) Count

Hydrophilic Amino Acid(s) Count

Basic Amino Acid(s) Count

Acidic Amino Acid(s) Count

Modified Amino Acid(s) Count

Modified Amino Acid(s) Frequencies

Computed by biopython (version 1.79) & proteinAnalysis (version 1)

3 Physicochemical Properties

Sl. No.	Properties	Values	Reference
1.	Molecular Mass	6149.09 Da	Computed by ProtParam module (biopython 1.79)
2.	Aliphatic Index	59.412	Computed by ProtParam module (biopython 1.79)
3.	Instability Index (Half Life)	31.275	Computed by ProtParam module (biopython 1.79)
4.	Hydrophobicity (GRAVY)	-0.704	Computed by ProtParam module (biopython 1.79)
5.	Hydrophobic Moment	0.411	Computed by ProtParam module (biopython 1.79)
6.	Isoelectric Point	10.597	Computed by ProtParam module (biopython 1.79)
7.	Charge (at pH 7)	6.632	Computed by ProtParam module (biopython 1.79)
8.	Secondary Structure Fraction	0.294, 0.176, 0.255 [Helix, Turn, Sheet]	Computed by ProtParam module (biopython 1.79)
9.	Aromaticity	0.157	Computed by ProtParam module (biopython 1.79)
10.	Molar Extinction Coefficient (cysteine\|cystine)	5960, 5960	Computed by ProtParam module (biopython 1.79)

4.1 Target Organism(s)

C.albicans, C.neoformans

4.2 Antimicrobial Activity

Antibiotic, Antimicrobial, Fungicide, Anti-candida

4.3 Enzymatic Activity

4.4 Inhibitory Effect

4.5 Other Biological Activity

Non-hemolytic, Non-ribosomal

Activity data manually curated from Literature and UniProt

5 Database Cross-references

5.1 Literature Database

Citation 1: Sabatini LM, Azen EA, Azen EA. Histatins, a family of salivary histidine-rich proteins, are encoded by at least two loci (HIS1 and HIS2). Biochem Biophys Res Commun. 1989;160(2):495-502. Published 1989 Apr 28. doi:10.1016/0006-291x(89)92460-1

PMID: 2719677

Citation 2: Dickinson DP, Ridall AL, Levine MJ, et al. 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. 1987;149(2):784-90. Published 1987 Dec 16. doi:10.1016/0006-291x(87)90436-0

PMID: 3426601

Citation 3: vanderSpek JC, Offner GD, Troxler RF, et al. Molecular cloning of human submandibular histatins. Arch Oral Biol. 1990;35(2):137-43. Published 1990. doi:10.1016/0003-9969(90)90175-a

PMID: 2344289

Citation 4: Sabatini LM, Ota T, Azen EA, et al. Nucleotide sequence analysis of the human salivary protein genes HIS1 and HIS2, and evolution of the STATH/HIS gene family. Mol Biol Evol. 1993;10(3):497-511. Published 1993 May. doi:10.1093/oxfordjournals.molbev.a040022

PMID: 8336540

Citation 5: Gerhard DS, Wagner L, Feingold EA, et al. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004;14(10B):2121-7. Published 2004 Oct. doi:10.1101/gr.2596504

PMID: 15489334

Citation 6: Sabatini LM, Azen EA, Azen EA. Two coding change mutations in the HIS2(2) allele characterize the salivary histatin 3-2 protein variant. Hum Mutat. 1994;4(1):12-9. Published 1994. doi:10.1002/humu.1380040103

PMID: 7951254

Citation 7: Oppenheim FG, Xu T, McMillian FM, et al. 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. 1988;263(16):7472-7. Published 1988 Jun 5. doi:

PMID: 3286634

Citation 8: Sugiyama K, Ogino T, Ogata K, et al. Rapid purification and characterization of histatins (histidine-rich polypeptides) from human whole saliva. Arch Oral Biol. 1990;35(6):415-9. Published 1990. doi:10.1016/0003-9969(90)90202-l

PMID: 2372245

Citation 9: Castagnola M, Inzitari R, Rossetti DV, et al. A cascade of 24 histatins (histatin 3 fragments) in human saliva. Suggestions for a pre-secretory sequential cleavage pathway. J Biol Chem. 2004;279(40):41436-43. Published 2004 Oct 1. doi:10.1074/jbc.M404322200

PMID: 15272024

Citation 10: Tsai H, Raj PA, Bobek LA, et al. Candidacidal activity of recombinant human salivary histatin-5 and variants. Infect Immun. 1996;64(12):5000-7. Published 1996 Dec. doi:10.1128/iai.64.12.5000-5007.1996

PMID: 8945538

Citation 11: Grogan J, McKnight CJ, Troxler RF, et al. Zinc and copper bind to unique sites of histatin 5. FEBS Lett. 2001;491(1-2):76-80. Published 2001 Feb 23. doi:10.1016/s0014-5793(01)02157-3

PMID: 11226423

Citation 12: Gusman H, Travis J, Helmerhorst EJ, et al. Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease. Infect Immun. 2001;69(3):1402-8. Published 2001 Mar. doi:10.1128/IAI.69.3.1402-1408.2001

PMID: 11179305

Citation 13: Li XS, Reddy MS, Baev D, et al. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J Biol Chem. 2003;278(31):28553-61. Published 2003 Aug 1. doi:10.1074/jbc.M300680200

PMID: 12761219

Citation 14: Ahmad M, Piludu M, Oppenheim FG, et al. Immunocytochemical localization of histatins in human salivary glands. J Histochem Cytochem. 2004;52(3):361-70. Published 2004 Mar. doi:10.1177/002215540405200307

PMID: 14966203

Citation 15: Cabras T, Fanali C, Monteiro JA, et al. Tyrosine polysulfation of human salivary histatin 1. A post-translational modification specific of the submandibular gland. J Proteome Res. 2007;6(7):2472-80. Published 2007 Jul. doi:10.1021/pr0700706

PMID: 17503797

Citation 16: Amado F, Lobo MJ, Domingues P, et al. Salivary peptidomics. Expert Rev Proteomics. 2010;7(5):709-21. Published 2010 Oct. doi:10.1586/epr.10.48

PMID: 20973643

5.2 Protein Sequence Databases

5.3 3D Structure Databases

AlphaFoldDB: P15516

5.4 Nucleotide Sequence Databases

Sl. no.	Accession(s)	Access Link(s)
1.	M26665	GenBank \|\| EMBL
2.	M18372	GenBank \|\| EMBL
3.	L05514	GenBank \|\| EMBL
4.	L05513	GenBank \|\| EMBL
5.	BC009791	GenBank \|\| EMBL
6.	BC095438	GenBank \|\| EMBL
7.	S74382	GenBank \|\| EMBL