HIS1_HUMAN
ID HIS1_HUMAN Reviewed; 57 AA.
AC P15515;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Histatin-1;
DE AltName: Full=Histidine-rich protein 1;
DE AltName: Full=Post-PB protein;
DE Short=PPB;
DE Contains:
DE RecName: Full=His1-(31-57)-peptide;
DE Short=His1 31/57;
DE AltName: Full=His1-(12-38)-peptide;
DE Short=His1 12/38;
DE AltName: Full=Histatin-2;
DE Flags: Precursor;
GN Name=HTN1; Synonyms=HIS1;
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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 [4]
RP PROTEIN SEQUENCE OF 20-57, AND PHOSPHORYLATION AT SER-21.
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 [5]
RP PROTEIN SEQUENCE OF 20-57.
RC TISSUE=Parotid gland;
RX PubMed=3944083; DOI=10.1016/s0021-9258(17)36072-6;
RA Oppenheim F.G., Yang Y.C., Diamond R.D., Hyslop D., Offner G.D.,
RA Troxler R.F.;
RT "The primary structure and functional characterization of the neutral
RT histidine-rich polypeptide from human parotid secretion.";
RL J. Biol. Chem. 261:1177-1182(1986).
RN [6]
RP PROTEIN SEQUENCE OF 20-57.
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 14-57.
RX PubMed=2773933;
RA Vanderspek J.C., Wyandt H.E., Skare J.C., Milunsky A., Oppenheim F.G.,
RA Troxler R.F.;
RT "Localization of the genes for histatins to human chromosome 4q13 and
RT tissue distribution of the mRNAs.";
RL Am. J. Hum. Genet. 45:381-387(1989).
RN [8]
RP PHOSPHORYLATION, SULFATION AT TYR-46; TYR-49; TYR-53 AND TYR-55, TISSUE
RP SPECIFICITY, AND MASS 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 [9]
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.
CC -!- INTERACTION:
CC P15515; Q8TAX7: MUC7; NbExp=2; IntAct=EBI-738638, EBI-738582;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Submandibular and parotid glands.
CC {ECO:0000269|PubMed:17503797}.
CC -!- PTM: Depending on the authors, the form called histatin-2 is
CC alternatively a proteolytic product, or the non-phosphorylated form of
CC histatin-1. {ECO:0000269|PubMed:17503797, ECO:0000269|PubMed:3286634}.
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=4848.2; Mass_error=0.5;
CC Method=Electrospray; Note=Not post-translationally modified.;
CC Evidence={ECO:0000269|PubMed:17503797};
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=4928.2; Mass_error=0.5;
CC Method=Electrospray; Note=with 1 phosphate group.;
CC Evidence={ECO:0000269|PubMed:17503797};
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=5008.6; Mass_error=0.5;
CC Method=Electrospray; Note=with 1 phosphate group and 1 sulfate group.;
CC Evidence={ECO:0000269|PubMed:17503797};
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=5088.4; Mass_error=0.5;
CC Method=Electrospray; Note=with 1 phosphate group and 2 sulfate groups.;
CC Evidence={ECO:0000269|PubMed:17503797};
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=5168.2; Mass_error=0.5;
CC Method=Electrospray; Note=with 1 phosphate group and 3 sulfate groups.;
CC Evidence={ECO:0000269|PubMed:17503797};
CC -!- MASS SPECTROMETRY: [Histatin-1]: Mass=5247.7; Mass_error=0.5;
CC Method=Electrospray; Note=with 1 phosphate group and 4 sulfate groups.;
CC Evidence={ECO:0000269|PubMed:17503797};
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; M26664; AAA58645.1; -; mRNA.
DR EMBL; L04132; AAA02745.1; -; Genomic_DNA.
DR EMBL; BC017835; AAH17835.1; -; mRNA.
DR CCDS; CCDS3534.1; -.
DR PIR; I57425; A32541.
DR RefSeq; NP_002150.1; NM_002159.3.
DR AlphaFoldDB; P15515; -.
DR BioGRID; 109578; 2.
DR IntAct; P15515; 1.
DR STRING; 9606.ENSP00000424501; -.
DR TCDB; 1.C.79.1.3; the channel-forming histatin antimicrobial peptide (histatin) family.
DR iPTMnet; P15515; -.
DR PhosphoSitePlus; P15515; -.
DR BioMuta; HTN1; -.
DR MassIVE; P15515; -.
DR PaxDb; P15515; -.
DR PeptideAtlas; P15515; -.
DR PRIDE; P15515; -.
DR ProteomicsDB; 53165; -.
DR TopDownProteomics; P15515; -.
DR Antibodypedia; 24284; 58 antibodies from 10 providers.
DR DNASU; 3346; -.
DR Ensembl; ENST00000246896.8; ENSP00000246896.3; ENSG00000126550.10.
DR Ensembl; ENST00000511674.5; ENSP00000424501.1; ENSG00000126550.10.
DR Ensembl; ENST00000635327.2; ENSP00000489349.1; ENSG00000283046.4.
DR Ensembl; ENST00000635569.1; ENSP00000489198.1; ENSG00000283046.4.
DR Ensembl; ENST00000678229.1; ENSP00000504066.1; ENSG00000283046.4.
DR GeneID; 3346; -.
DR KEGG; hsa:3346; -.
DR MANE-Select; ENST00000246896.8; ENSP00000246896.3; NM_002159.4; NP_002150.1.
DR UCSC; uc003hex.4; human.
DR CTD; 3346; -.
DR DisGeNET; 3346; -.
DR GeneCards; HTN1; -.
DR HGNC; HGNC:5283; HTN1.
DR HPA; ENSG00000126550; Tissue enriched (salivary).
DR MIM; 142701; gene.
DR neXtProt; NX_P15515; -.
DR OpenTargets; ENSG00000126550; -.
DR PharmGKB; PA29546; -.
DR VEuPathDB; HostDB:ENSG00000126550; -.
DR eggNOG; ENOG502TEIH; Eukaryota.
DR GeneTree; ENSGT00940000164572; -.
DR HOGENOM; CLU_208169_1_0_1; -.
DR InParanoid; P15515; -.
DR OrthoDB; 1623335at2759; -.
DR PhylomeDB; P15515; -.
DR TreeFam; TF341637; -.
DR PathwayCommons; P15515; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR SignaLink; P15515; -.
DR BioGRID-ORCS; 3346; 6 hits in 562 CRISPR screens.
DR ChiTaRS; HTN1; human.
DR GeneWiki; HTN1; -.
DR GenomeRNAi; 3346; -.
DR Pharos; P15515; Tbio.
DR PRO; PR:P15515; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P15515; protein.
DR Bgee; ENSG00000126550; Expressed in olfactory segment of nasal mucosa and 33 other tissues.
DR Genevisible; P15515; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
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 InterPro; IPR030774; Histatin-3.
DR InterPro; IPR030773; Histatin/statherin.
DR PANTHER; PTHR15057; PTHR15057; 1.
DR PANTHER; PTHR15057:SF2; PTHR15057:SF2; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Biomineralization; Direct protein sequencing;
KW Fungicide; Phosphoprotein; Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:2372245,
FT ECO:0000269|PubMed:3286634, ECO:0000269|PubMed:3944083"
FT PEPTIDE 20..57
FT /note="Histatin-1"
FT /id="PRO_0000021416"
FT PEPTIDE 31..57
FT /note="His1-(31-57)-peptide"
FT /id="PRO_0000021417"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:3286634,
FT ECO:0000269|PubMed:3944083"
FT MOD_RES 46
FT /note="Sulfotyrosine; in submandibular gland form"
FT /evidence="ECO:0000269|PubMed:17503797"
FT MOD_RES 49
FT /note="Sulfotyrosine; in submandibular gland form"
FT /evidence="ECO:0000269|PubMed:17503797"
FT MOD_RES 53
FT /note="Sulfotyrosine; in submandibular gland form"
FT /evidence="ECO:0000269|PubMed:17503797"
FT MOD_RES 55
FT /note="Sulfotyrosine; in submandibular gland form"
FT /evidence="ECO:0000269|PubMed:17503797"
SQ SEQUENCE 57 AA; 6963 MW; F3532BD1DCE23D83 CRC64;
MKFFVFALVL ALMISMISAD SHEKRHHGYR RKFHEKHHSH REFPFYGDYG SNYLYDN
