HIS3_HUMAN
ID HIS3_HUMAN Reviewed; 51 AA.
AC P15516; Q16243; Q502Z1;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Histatin-3;
DE AltName: Full=Basic histidine-rich protein;
DE Short=Hst;
DE AltName: Full=Histidine-rich protein 3;
DE AltName: Full=PB;
DE Contains:
DE RecName: Full=Histatin-3;
DE Contains:
DE RecName: Full=His3-(20-44)-peptide;
DE Short=His3 20/44;
DE AltName: Full=His3-(1-25)-peptide;
DE Short=His3 1/25;
DE AltName: Full=Histatin-3 1/25;
DE AltName: Full=Histatin-6;
DE Contains:
DE RecName: Full=His3-(20-43)-peptide;
DE Short=His3 20/43;
DE AltName: Full=His3-(1-24)-peptide;
DE Short=His3 1/24;
DE AltName: Full=Histatin-3 1/24;
DE AltName: Full=Histatin-5;
DE Contains:
DE RecName: Full=His3-(20-32)-peptide;
DE Short=His3 20/32;
DE AltName: Full=His3-(1-13)-peptide;
DE Short=His3 1/13;
DE AltName: Full=Histatin-3 1/13;
DE Contains:
DE RecName: Full=His3-(20-31)-peptide;
DE Short=His3 20/31;
DE AltName: Full=His3-(1-12)-peptide;
DE Short=His3 1/12;
DE AltName: Full=Histatin-3 1/12;
DE Contains:
DE RecName: Full=His3-(20-30)-peptide;
DE Short=His3 20/30;
DE AltName: Full=His3-(1-11)-peptide;
DE Short=His3 1/11;
DE AltName: Full=Histatin-3 1/11;
DE Contains:
DE RecName: Full=His3-(24-32)-peptide;
DE Short=His3 24/32;
DE AltName: Full=His3-(5-13)-peptide;
DE Short=His3 5/13;
DE AltName: Full=Histatin-3 5/13;
DE Contains:
DE RecName: Full=His3-(24-31)-peptide;
DE Short=His3 24/31;
DE AltName: Full=His3-(5-12)-peptide;
DE Short=His3 5/12;
DE AltName: Full=Histatin-11;
DE AltName: Full=Histatin-3 5/12;
DE Contains:
DE RecName: Full=His3-(24-30)-peptide;
DE Short=His3 24/30;
DE AltName: Full=His3-(5-11)-peptide;
DE Short=His3 5/11;
DE AltName: Full=Histatin-12;
DE AltName: Full=Histatin-3 5/11;
DE Contains:
DE RecName: Full=His3-(25-32)-peptide;
DE Short=His3 25/32;
DE AltName: Full=His3-(6-13)-peptide;
DE Short=His3 6/13;
DE AltName: Full=Histatin-3 6/13;
DE Contains:
DE RecName: Full=His3-(25-30)-peptide;
DE Short=His3 25/30;
DE AltName: Full=His3-(6-11)-peptide;
DE Short=His3 6/11;
DE AltName: Full=Histatin-3 6/11;
DE Contains:
DE RecName: Full=His3-(26-32)-peptide;
DE Short=His3 26/32;
DE AltName: Full=His3-(7-13)-peptide;
DE Short=His3 7/13;
DE AltName: Full=Histatin-3 7/13;
DE Contains:
DE RecName: Full=His3-(26-31)-peptide;
DE Short=His3 26/31;
DE AltName: Full=His3-(7-12)-peptide;
DE Short=His3 7/12;
DE AltName: Full=Histatin-3 7/12;
DE Contains:
DE RecName: Full=His3-(26-30)-peptide;
DE Short=His3 26/30;
DE AltName: Full=His3-(7-11)-peptide;
DE Short=His3 7/11;
DE AltName: Full=Histatin-3 7/11;
DE Contains:
DE RecName: Full=His3-(31-51)-peptide;
DE Short=His3 31/51;
DE AltName: Full=His3-(12-32)-peptide;
DE Short=His3 12/32;
DE AltName: Full=Histatin-3 12/32;
DE AltName: Full=Histatin-4;
DE Contains:
DE RecName: Full=His3-(31-44)-peptide;
DE Short=His3 31/44;
DE AltName: Full=His3-(12-25)-peptide;
DE Short=His3 12/25;
DE AltName: Full=Histatin-3 12/25;
DE AltName: Full=Histatin-9;
DE Contains:
DE RecName: Full=His3-(31-43)-peptide;
DE Short=His3 31/43;
DE AltName: Full=His3-(12-24)-peptide;
DE Short=His3 12/24;
DE AltName: Full=Histatin-3 12/24;
DE AltName: Full=Histatin-7;
DE Contains:
DE RecName: Full=His3-(32-44)-peptide;
DE Short=His3 32/44;
DE AltName: Full=His3-(13-25)-peptide;
DE Short=His3 13/25;
DE AltName: Full=Histatin-10;
DE AltName: Full=Histatin-3 13/25;
DE Contains:
DE RecName: Full=His3-(32-43)-peptide;
DE Short=His3 32-43;
DE AltName: Full=His3-(13-24)-peptide;
DE Short=His3 13/24;
DE AltName: Full=Histatin-3 13/24;
DE AltName: Full=Histatin-8;
DE Contains:
DE RecName: Full=His3-(33-44)-peptide;
DE Short=His3 33/44;
DE AltName: Full=His3-(14-25)-peptide;
DE Short=His3 14/25;
DE AltName: Full=Histatin-3 14/25;
DE Contains:
DE RecName: Full=His3-(33-43)-peptide;
DE Short=His3 33/43;
DE AltName: Full=His3-(14-24)-peptide;
DE Short=His3 14/24;
DE AltName: Full=Histatin-3 14/24;
DE Contains:
DE RecName: Full=His3-(34-44)-peptide;
DE Short=His3 34/44;
DE AltName: Full=His3-(15-25)-peptide;
DE Short=His3 15/25;
DE AltName: Full=Histatin-3 15/25;
DE Contains:
DE RecName: Full=His3-(34-43)-peptide;
DE Short=His3 34/43;
DE AltName: Full=His3-(15-24)-peptide;
DE Short=His3 15/24;
DE AltName: Full=Histatin-3 15/24;
DE Contains:
DE RecName: Full=His3-(45-51)-peptide;
DE Short=His3 45/51;
DE AltName: Full=His3-(26-32)-peptide;
DE Short=His3 26/32;
DE AltName: Full=Histatin-3 26/32;
DE Contains:
DE RecName: Full=His3-(47-51)-peptide;
DE Short=His3 47/51;
DE AltName: Full=His3-(28-32)-peptide;
DE Short=His3 28/32;
DE AltName: Full=Histatin-3 28/32;
DE Contains:
DE RecName: Full=His3-(48-51)-peptide;
DE Short=His3 48/51;
DE AltName: Full=His3-(29-32)-peptide;
DE Short=His3 29/32;
DE AltName: Full=Histatin-3 29/32;
DE Flags: Precursor;
GN Name=HTN3; Synonyms=HIS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2719677; DOI=10.1016/0006-291x(89)92460-1;
RA Sabatini L.M., Azen E.A.;
RT "Histatins, a family of salivary histidine-rich proteins, are encoded by at
RT least two loci (HIS1 and HIS2).";
RL Biochem. Biophys. Res. Commun. 160:495-502(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3426601; DOI=10.1016/0006-291x(87)90436-0;
RA Dickinson D.P., Ridall A.L., Levine M.J.;
RT "Human submandibular gland statherin and basic histidine-rich peptide are
RT encoded by highly abundant mRNA's derived from a common ancestral
RT sequence.";
RL Biochem. Biophys. Res. Commun. 149:784-790(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2344289; DOI=10.1016/0003-9969(90)90175-a;
RA Vanderspek J.C., Offner G.D., Troxler R.F., Oppenheim F.G.;
RT "Molecular cloning of human submandibular histatins.";
RL Arch. Oral Biol. 35:137-143(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8336540; DOI=10.1093/oxfordjournals.molbev.a040022;
RA Chen Z.W.;
RT "Nucleotide sequence analysis of the human salivary protein genes HIS1 and
RT HIS2, and evolution of the STATH/HIS gene family.";
RL Mol. Biol. Evol. 10:497-511(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle, and Thyroid;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-51, VARIANTS HISTATIN-3-2 GLN-41
RP AND 47-TYR--ASN-51 DEL, AND POLYMORPHISM.
RC TISSUE=Saliva;
RX PubMed=7951254; DOI=10.1002/humu.1380040103;
RA Sabatini L.M., Azen E.A.;
RT "Two coding change mutations in the HIS2(2) allele characterize the
RT salivary histatin 3-2 protein variant.";
RL Hum. Mutat. 4:12-19(1994).
RN [7]
RP PROTEIN SEQUENCE OF 20-51.
RC TISSUE=Parotid gland;
RX PubMed=3286634; DOI=10.1016/s0021-9258(18)68522-9;
RA Oppenheim F.G., Xu T., McMillian F.M., Levitz S.M., Diamond R.D.,
RA Offner G.D., Troxler R.F.;
RT "Histatins, a novel family of histidine-rich proteins in human parotid
RT secretion. Isolation, characterization, primary structure, and fungistatic
RT effects on Candida albicans.";
RL J. Biol. Chem. 263:7472-7477(1988).
RN [8]
RP PROTEIN SEQUENCE OF 20-42.
RC TISSUE=Saliva;
RX PubMed=2372245; DOI=10.1016/0003-9969(90)90202-l;
RA Sugiyama K., Ogino T., Ogata K.;
RT "Rapid purification and characterization of histatins (histidine-rich
RT polypeptides) from human whole saliva.";
RL Arch. Oral Biol. 35:415-419(1990).
RN [9]
RP PROTEIN SEQUENCE OF 20-32, AND IDENTIFICATION BY MASS SPECTROMETRY OF 24
RP PEPTIDE FRAGMENTS.
RC TISSUE=Saliva;
RX PubMed=15272024; DOI=10.1074/jbc.m404322200;
RA Castagnola M., Inzitari R., Rossetti D.V., Olmi C., Cabras T., Piras V.,
RA Nicolussi P., Sanna M.T., Pellegrini M., Giardina B., Messana I.;
RT "A cascade of 24 histatins (histatin 3 fragments) in human saliva.
RT Suggestions for a pre-secretory sequential cleavage pathway.";
RL J. Biol. Chem. 279:41436-41443(2004).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ARG-31; LYS-32; LYS-36; HIS-38; HIS-40 AND
RP ARG-41.
RX PubMed=8945538; DOI=10.1128/iai.64.12.5000-5007.1996;
RA Tsai H., Raj P.A., Bobek L.A.;
RT "Candidacidal activity of recombinant human salivary histatin-5 and
RT variants.";
RL Infect. Immun. 64:5000-5007(1996).
RN [11]
RP ZINC-BINDING SITE.
RX PubMed=11226423; DOI=10.1016/s0014-5793(01)02157-3;
RA Grogan J., McKnight C.J., Troxler R.F., Oppenheim F.G.;
RT "Zinc and copper bind to unique sites of histatin 5.";
RL FEBS Lett. 491:76-80(2001).
RN [12]
RP FUNCTION.
RX PubMed=11179305; DOI=10.1128/iai.69.3.1402-1408.2001;
RA Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F.,
RA Oppenheim F.G.;
RT "Salivary histatin 5 is an inhibitor of both host and bacterial enzymes
RT implicated in periodontal disease.";
RL Infect. Immun. 69:1402-1408(2001).
RN [13]
RP INTERACTION WITH SSA1 AND SSA2.
RX PubMed=12761219; DOI=10.1074/jbc.m300680200;
RA Li X.S., Reddy M.S., Baev D., Edgerton M.;
RT "Candida albicans Ssa1/2p is the cell envelope binding protein for human
RT salivary histatin 5.";
RL J. Biol. Chem. 278:28553-28561(2003).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=14966203; DOI=10.1177/002215540405200307;
RA Ahmad M., Piludu M., Oppenheim F.G., Helmerhorst E.J., Hand A.R.;
RT "Immunocytochemical localization of histatins in human salivary glands.";
RL J. Histochem. Cytochem. 52:361-370(2004).
RN [15]
RP LACK OF SULFATION AT TYR-43; TYR-47 AND TYR-49, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17503797; DOI=10.1021/pr0700706;
RA Cabras T., Fanali C., Monteiro J.A., Amado F., Inzitari R., Desiderio C.,
RA Scarano E., Giardina B., Castagnola M., Messana I.;
RT "Tyrosine polysulfation of human salivary histatin 1. A post-translational
RT modification specific of the submandibular gland.";
RL J. Proteome Res. 6:2472-2480(2007).
RN [16]
RP PEPTIDE NOMENCLATURE.
RX PubMed=20973643; DOI=10.1586/epr.10.48;
RA Amado F., Lobo M.J., Domingues P., Duarte J.A., Vitorino R.;
RT "Salivary peptidomics.";
RL Expert Rev. Proteomics 7:709-721(2010).
CC -!- FUNCTION: Histatins are salivary proteins that are considered to be
CC major precursors of the protective proteinaceous structure on tooth
CC surfaces (enamel pellicle). In addition, histatins exhibit
CC antibacterial and antifungal activities. His3-(20-43)-peptide
CC (histatin-5) is especially effective against C.albicans and
CC C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from
CC P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor
CC of metalloproteinases MMP2 and MMP9. {ECO:0000269|PubMed:11179305,
CC ECO:0000269|PubMed:8945538}.
CC -!- SUBUNIT: His3-(20-43)-peptide is a homodimer. Histatin-3 and His3-(20-
CC 43)-peptide interact with yeast SSA1 and SSA2 proteins.
CC -!- INTERACTION:
CC P15516; Q9UBS4: DNAJB11; NbExp=3; IntAct=EBI-738783, EBI-713113;
CC P15516; P95493: rgpB; Xeno; NbExp=7; IntAct=EBI-738783, EBI-8505881;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14966203}.
CC Note=Secreted by serous acinar and demilune cells.
CC -!- PTM: 24 proteolytic products are found in saliva.
CC -!- POLYMORPHISM: There are two alleles of HTN3, HIS2(1) (shown here) and
CC HIS2(2) that codes for the variant histatin-3-2 found primarily and in
CC high frequencies in black populations. {ECO:0000269|PubMed:7951254}.
CC -!- MISCELLANEOUS: The recommended nomenclature of salivary peptides
CC follows published guidelines (PubMed:20973643). In agreement with the
CC authors, it has been decided to indicate the boundaries of the peptides
CC according to the positions within the precursor, and not in the mature
CC protein, as has formerly been proposed. {ECO:0000305|PubMed:20973643}.
CC -!- SIMILARITY: Belongs to the histatin/statherin family. {ECO:0000305}.
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DR EMBL; M26665; AAA58646.1; -; mRNA.
DR EMBL; M18372; AAA51830.1; -; mRNA.
DR EMBL; L05514; AAA02746.1; -; Genomic_DNA.
DR EMBL; L05513; AAA02746.1; JOINED; Genomic_DNA.
DR EMBL; BC009791; AAH09791.1; -; mRNA.
DR EMBL; BC095438; AAH95438.1; -; mRNA.
DR EMBL; S74382; AAB32411.1; -; Genomic_DNA.
DR CCDS; CCDS33999.1; -.
DR PIR; B32541; B32541.
DR RefSeq; NP_000191.1; NM_000200.2.
DR AlphaFoldDB; P15516; -.
DR SASBDB; P15516; -.
DR BioGRID; 109579; 32.
DR IntAct; P15516; 4.
DR MINT; P15516; -.
DR STRING; 9606.ENSP00000432561; -.
DR TCDB; 1.C.79.1.1; the channel-forming histatin antimicrobial peptide (histatin) family.
DR BioMuta; HTN3; -.
DR MassIVE; P15516; -.
DR PaxDb; P15516; -.
DR PeptideAtlas; P15516; -.
DR PRIDE; P15516; -.
DR ProteomicsDB; 53166; -.
DR Antibodypedia; 24280; 16 antibodies from 9 providers.
DR DNASU; 3347; -.
DR Ensembl; ENST00000530128.5; ENSP00000432561.1; ENSG00000205649.9.
DR Ensembl; ENST00000635585.1; ENSP00000489520.1; ENSG00000282967.4.
DR Ensembl; ENST00000672568.1; ENSP00000500810.1; ENSG00000282967.4.
DR Ensembl; ENST00000673563.1; ENSP00000500623.1; ENSG00000205649.9.
DR Ensembl; ENST00000677679.1; ENSP00000504141.1; ENSG00000282967.4.
DR GeneID; 3347; -.
DR KEGG; hsa:3347; -.
DR MANE-Select; ENST00000673563.1; ENSP00000500623.1; NM_000200.3; NP_000191.1.
DR UCSC; uc003hew.2; human.
DR CTD; 3347; -.
DR DisGeNET; 3347; -.
DR GeneCards; HTN3; -.
DR HGNC; HGNC:5284; HTN3.
DR HPA; ENSG00000205649; Tissue enriched (salivary).
DR MIM; 142702; gene.
DR neXtProt; NX_P15516; -.
DR OpenTargets; ENSG00000205649; -.
DR PharmGKB; PA29547; -.
DR VEuPathDB; HostDB:ENSG00000205649; -.
DR eggNOG; ENOG502TEIC; Eukaryota.
DR GeneTree; ENSGT00940000164572; -.
DR InParanoid; P15516; -.
DR OMA; DSHEEKH; -.
DR OrthoDB; 1623335at2759; -.
DR PhylomeDB; P15516; -.
DR TreeFam; TF341637; -.
DR PathwayCommons; P15516; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; P15516; -.
DR BioGRID-ORCS; 3347; 5 hits in 517 CRISPR screens.
DR ChiTaRS; HTN3; human.
DR GeneWiki; HTN3; -.
DR GenomeRNAi; 3347; -.
DR Pharos; P15516; Tbio.
DR PRO; PR:P15516; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P15516; protein.
DR Bgee; ENSG00000205649; Expressed in placenta and 46 other tissues.
DR ExpressionAtlas; P15516; baseline and differential.
DR Genevisible; P15516; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; NAS:UniProtKB.
DR GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR DisProt; DP02206; -.
DR InterPro; IPR030774; Histatin-3.
DR InterPro; IPR030773; Histatin/statherin.
DR PANTHER; PTHR15057; PTHR15057; 1.
DR PANTHER; PTHR15057:SF1; PTHR15057:SF1; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Biomineralization;
KW Cleavage on pair of basic residues; Direct protein sequencing; Fungicide;
KW Metal-binding; Reference proteome; Secreted; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:15272024,
FT ECO:0000269|PubMed:2372245, ECO:0000269|PubMed:3286634"
FT CHAIN 20..51
FT /note="Histatin-3"
FT /id="PRO_0000021418"
FT PEPTIDE 20..44
FT /note="His3-(20-44)-peptide"
FT /id="PRO_0000021419"
FT PEPTIDE 20..43
FT /note="His3-(20-43)-peptide"
FT /id="PRO_0000021420"
FT PEPTIDE 20..32
FT /note="His3-(20-32)-peptide"
FT /id="PRO_0000021421"
FT PEPTIDE 20..31
FT /note="His3-(20-31)-peptide"
FT /id="PRO_0000021422"
FT PEPTIDE 20..30
FT /note="His3-(20-30)-peptide"
FT /id="PRO_0000021423"
FT PEPTIDE 24..32
FT /note="His3-(24-32)-peptide"
FT /id="PRO_0000021424"
FT PEPTIDE 24..31
FT /note="His3-(24-31)-peptide"
FT /id="PRO_0000021425"
FT PEPTIDE 24..30
FT /note="His3-(24-30)-peptide"
FT /id="PRO_0000021426"
FT PEPTIDE 25..32
FT /note="His3-(25-32)-peptide"
FT /id="PRO_0000021427"
FT PEPTIDE 25..30
FT /note="His3-(25-30)-peptide"
FT /id="PRO_0000021428"
FT PEPTIDE 26..32
FT /note="His3-(26-32)-peptide"
FT /id="PRO_0000021429"
FT PEPTIDE 26..31
FT /note="His3-(26-31)-peptide"
FT /id="PRO_0000021430"
FT PEPTIDE 26..30
FT /note="His3-(26-30)-peptide"
FT /id="PRO_0000021431"
FT PEPTIDE 31..51
FT /note="His3-(31-51)-peptide"
FT /id="PRO_0000021432"
FT PEPTIDE 31..44
FT /note="His3-(31-44)-peptide"
FT /id="PRO_0000021433"
FT PEPTIDE 31..43
FT /note="His3-(31-43)-peptide"
FT /id="PRO_0000021434"
FT PEPTIDE 32..44
FT /note="His3-(32-44)-peptide"
FT /id="PRO_0000021435"
FT PEPTIDE 32..43
FT /note="His3-(32-43)-peptide"
FT /id="PRO_0000021436"
FT PEPTIDE 33..44
FT /note="His3-(33-44)-peptide"
FT /id="PRO_0000021437"
FT PEPTIDE 33..43
FT /note="His3-(33-43)-peptide"
FT /id="PRO_0000021438"
FT PEPTIDE 34..44
FT /note="His3-(34-44)-peptide"
FT /id="PRO_0000021439"
FT PEPTIDE 34..43
FT /note="His3-(34-43)-peptide"
FT /id="PRO_0000021440"
FT PEPTIDE 45..51
FT /note="His3-(45-51)-peptide"
FT /id="PRO_0000021441"
FT PEPTIDE 47..51
FT /note="His3-(47-51)-peptide"
FT /id="PRO_0000021442"
FT PEPTIDE 48..51
FT /note="His3-(48-51)-peptide"
FT /id="PRO_0000021443"
FT REGION 27..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT SITE 32
FT /note="Important for candidacidal activity"
FT SITE 41
FT /note="Important for candidacidal activity"
FT SITE 43
FT /note="Not sulfated"
FT /evidence="ECO:0000269|PubMed:17503797"
FT SITE 47
FT /note="Not sulfated"
FT /evidence="ECO:0000269|PubMed:17503797"
FT SITE 49
FT /note="Not sulfated"
FT /evidence="ECO:0000269|PubMed:17503797"
FT VARIANT 41
FT /note="R -> Q (in histatin-3-2; loss of the proteolytic
FT cleavage site; dbSNP:rs1136511)"
FT /evidence="ECO:0000269|PubMed:7951254"
FT /id="VAR_005288"
FT VARIANT 47..51
FT /note="Missing (in histatin-3-2; dbSNP:rs17147990)"
FT /evidence="ECO:0000269|PubMed:7951254"
FT /id="VAR_005289"
FT MUTAGEN 31
FT /note="R->I: No effect on candidacidal activity of His3-
FT (20-43)-peptide."
FT /evidence="ECO:0000269|PubMed:8945538"
FT MUTAGEN 32
FT /note="K->T,E: 3-fold reduction in candidacidal activity of
FT His3-(20-43)-peptide."
FT /evidence="ECO:0000269|PubMed:8945538"
FT MUTAGEN 36
FT /note="K->N: No effect on candidacidal activity of His3-
FT (20-43)-peptide."
FT /evidence="ECO:0000269|PubMed:8945538"
FT MUTAGEN 38
FT /note="H->P: No effect on candidacidal activity of His3-
FT (20-43)-peptide."
FT /evidence="ECO:0000269|PubMed:8945538"
FT MUTAGEN 40
FT /note="H->L,R: No effect on candidacidal activity of His3-
FT (20-43)-peptide."
FT /evidence="ECO:0000269|PubMed:8945538"
FT MUTAGEN 41
FT /note="R->G: 10-fold reduction in candidacidal activity of
FT His3-(20-43)-peptide; when associated with E-32."
FT /evidence="ECO:0000269|PubMed:8945538"
SQ SEQUENCE 51 AA; 6149 MW; AFCCB4B32083FD65 CRC64;
MKFFVFALIL ALMLSMTGAD SHAKRHHGYK RKFHEKHHSH RGYRSNYLYD N
