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   27-MAR-2024, entry version 171.
DE   RecName: Full=Histatin-1;
DE            Short=Hst1 {ECO:0000303|PubMed:35970844};
DE   AltName: Full=Histidine-rich protein 1 {ECO:0000303|PubMed:3286634};
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 {ECO:0000303|PubMed:20973643};
DE              Short=His1 12/38 {ECO:0000303|PubMed:20973643};
DE     AltName: Full=Histatin 2 {ECO:0000303|PubMed:20973643};
DE              Short=Hst2 {ECO:0000303|PubMed:35970844};
DE     AltName: Full=Histatin-2;
DE   Flags: Precursor;
GN   Name=HTN1 {ECO:0000312|HGNC:HGNC:5283}; 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 [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   [3]
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   [4]
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   [5]
RP   PROTEIN SEQUENCE OF 20-57, AND FUNCTION.
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, PHOSPHORYLATION AT SER-21, AND FUNCTION.
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   [7]
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   [8]
RP   PHOSPHORYLATION, SULFATION AT TYR-46; TYR-49; TYR-53 AND TYR-55, TISSUE
RP   SPECIFICITY, MASS SPECTROMETRY, AND CAUTION.
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   FUNCTION, DOMAIN, AND CAUTION.
RX   PubMed=18650243; DOI=10.1096/fj.08-112003;
RA   Oudhoff M.J., Bolscher J.G., Nazmi K., Kalay H., van 't Hof W.,
RA   Amerongen A.V., Veerman E.C.;
RT   "Histatins are the major wound-closure stimulating factors in human saliva
RT   as identified in a cell culture assay.";
RL   FASEB J. 22:3805-3812(2008).
RN   [10]
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).
RN   [11]
RP   FUNCTION, PHOSPHORYLATION, AND CAUTION.
RX   PubMed=25903106; DOI=10.1096/fj.14-266825;
RA   van Dijk I.A., Nazmi K., Bolscher J.G., Veerman E.C., Stap J.;
RT   "Histatin-1, a histidine-rich peptide in human saliva, promotes cell-
RT   substrate and cell-cell adhesion.";
RL   FASEB J. 29:3124-3132(2015).
RN   [12]
RP   FUNCTION, AND CAUTION.
RX   PubMed=28751526; DOI=10.1096/fj.201700085r;
RA   Torres P., Diaz J., Arce M., Silva P., Mendoza P., Lois P.,
RA   Molina-Berrios A., Owen G.I., Palma V., Torres V.A.;
RT   "The salivary peptide histatin-1 promotes endothelial cell adhesion,
RT   migration, and angiogenesis.";
RL   FASEB J. 31:4946-4958(2017).
RN   [13]
RP   FUNCTION, AND CAUTION.
RX   PubMed=28542418; DOI=10.1371/journal.pone.0178030;
RA   Shah D., Ali M., Shukla D., Jain S., Aakalu V.K.;
RT   "Effects of histatin-1 peptide on human corneal epithelial cells.";
RL   PLoS ONE 12:e0178030-e0178030(2017).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, AND CAUTION.
RX   PubMed=32225006; DOI=10.3390/cells9040795;
RA   Ma D., Sun W., Nazmi K., Veerman E.C.I., Bikker F.J., Jaspers R.T.,
RA   Bolscher J.G.M., Wu G.;
RT   "Salivary Histatin 1 and 2 Are Targeted to Mitochondria and Endoplasmic
RT   Reticulum in Human Cells.";
RL   Cells 9:0-0(2020).
RN   [15]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH TMEM97.
RX   PubMed=34233061; DOI=10.1111/febs.16108;
RA   Son K.N., Lee H., Shah D., Kalmodia S., Miller R.C., Ali M.,
RA   Balasubramaniam A., Cologna S.M., Kong H., Shukla D., Aakalu V.K.;
RT   "Histatin-1 is an endogenous ligand of the sigma-2 receptor.";
RL   FEBS J. 288:6815-6827(2021).
RN   [16]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=35970844; DOI=10.1038/s41368-022-00181-5;
RA   Ma D., Sun W., Fu C., Nazmi K., Veerman E.C.I., Jaspers R.T.,
RA   Bolscher J.G.M., Bikker F.J., Wu G.;
RT   "GPCR/endocytosis/ERK signaling/S2R is involved in the regulation of the
RT   internalization, mitochondria-targeting and -activating properties of human
RT   salivary histatin 1.";
RL   Int. J. Oral Sci. 14:42-42(2022).
CC   -!- FUNCTION: Histatins (Hsts) are cationic and histidine-rich secreted
CC       peptides mainly synthesized by saliva glands of humans and higher
CC       primates (PubMed:3944083, PubMed:3286634). Hsts are considered to be
CC       major precursors of the protective proteinaceous structure on tooth
CC       surfaces (enamel pellicle). Hsts can be divided into two major groups
CC       according to their biological functions: antimicrobial Hsts (e.g. Hst
CC       5/HTN3) and cell-activating Hsts (e.g. Hst 1/HTN1 and Hst 2/HTN1)
CC       (PubMed:32225006). Hst 1/HTN1 and Hst 2/HTN1 act in different cell
CC       types (epithelium, fibroblasts and endothelium) in oral and non-oral
CC       mucosa (PubMed:25903106, PubMed:28751526, PubMed:28542418,
CC       PubMed:32225006). {ECO:0000269|PubMed:25903106,
CC       ECO:0000269|PubMed:28542418, ECO:0000269|PubMed:28751526,
CC       ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:3286634,
CC       ECO:0000269|PubMed:3944083}.
CC   -!- FUNCTION: [Histatin-1]: Hst 1 functions primarily as a wound healing
CC       factor by activating cell-surface and cell-cell adhesions, cell
CC       spreading and migration and it can also stimulate cellular metabolic
CC       activity (PubMed:18650243, PubMed:25903106, PubMed:28751526,
CC       PubMed:28542418, PubMed:32225006, PubMed:35970844). Hst 1 is
CC       internalized in host cells in a stereospecific and energy-dependent
CC       process, which is partially mediated by the G protein-coupled receptors
CC       (GPCR)-activated endocytosis (PubMed:35970844). Internalized Hst 1 is
CC       targeted and released via early endosomes trafficking to the
CC       mitochondria, where it significantly enhances mitochondrial energy
CC       metabolism (PubMed:32225006, PubMed:35970844). At the mitochondria, Hst
CC       1 increases mitochondria-ER contacts through binding with ER receptor
CC       TMEM97, which also stimulates metabolic activity and cell migration and
CC       may as well regulate calcium homeostasis of the cell (PubMed:32225006,
CC       PubMed:34233061, PubMed:35970844). Also activates the ERK1/2 signaling
CC       pathway to promote cell migration, possibly upon interaction with GPRCs
CC       at the plasma membrane (PubMed:28751526). Also triggers the
CC       RIN2/Rab5/Rac1 signaling cascade which activates endothelial cell
CC       adhesion, spreading and migration required for angiogenesis in the oral
CC       wound healing process, however the receptor that transduces Hst 1
CC       signal has not yet been identified (PubMed:28751526). Also displays
CC       antimicrobial functions against pathogenic yeast Candida albicans,
CC       although with less effectiveness than Hst 5 (PubMed:3944083,
CC       PubMed:3286634, PubMed:28751526). {ECO:0000269|PubMed:18650243,
CC       ECO:0000269|PubMed:25903106, ECO:0000269|PubMed:28542418,
CC       ECO:0000269|PubMed:28751526, ECO:0000269|PubMed:32225006,
CC       ECO:0000269|PubMed:3286634, ECO:0000269|PubMed:34233061,
CC       ECO:0000269|PubMed:35970844, ECO:0000269|PubMed:3944083}.
CC   -!- FUNCTION: [His1-(31-57)-peptide]: Hst 2 consists of the fragment
CC       sequence 12-28 of Hst 1. Similar to Hst 1, actively and
CC       stereospecifically internalized in host cells and targeted to the
CC       mitochondria and the ER and promotes cell metabolic activity
CC       (PubMed:18650243, PubMed:32225006). Also activates the ERK1/2 signaling
CC       pathway to promote cell migration and wound closure (PubMed:18650243).
CC       In contrast with Hst 1, not able to promote cell-substrate and cell-
CC       cell adhesion (PubMed:25903106). {ECO:0000269|PubMed:18650243,
CC       ECO:0000269|PubMed:25903106, ECO:0000269|PubMed:32225006}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC   -!- SUBUNIT: [Histatin-1]: Interacts with TMEM97; the interaction induces
CC       Hst1-stimulating wound healing. {ECO:0000269|PubMed:34233061}.
CC   -!- INTERACTION:
CC       P15515; Q8TAX7: MUC7; NbExp=2; IntAct=EBI-738638, EBI-738582;
CC   -!- SUBCELLULAR LOCATION: [Histatin-1]: Secreted. Mitochondrion
CC       {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:35970844}. Endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:32225006,
CC       ECO:0000269|PubMed:34233061, ECO:0000269|PubMed:35970844}. Note=Hst 1
CC       co-localized with mitochondria as well as the endoplasmic reticulum
CC       (ER) after internalization in host cells. {ECO:0000269|PubMed:32225006,
CC       ECO:0000269|PubMed:34233061, ECO:0000269|PubMed:35970844}.
CC   -!- SUBCELLULAR LOCATION: [His1-(31-57)-peptide]: Secreted. Mitochondrion
CC       {ECO:0000269|PubMed:32225006}. Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:32225006}. Note=Hst 2 co-localized with
CC       mitochondria as well as the endoplasmic reticulum (ER) after
CC       internalization in host cells. {ECO:0000269|PubMed:32225006}.
CC   -!- TISSUE SPECIFICITY: [Histatin-1]: Submandibular and parotid glands.
CC       {ECO:0000269|PubMed:17503797}.
CC   -!- DOMAIN: The wound healing domain in C-terminus may promote cell
CC       migration and proliferation. {ECO:0000269|PubMed:18650243}.
CC   -!- PTM: [Histatin-1]: Phosphorylated. {ECO:0000269|PubMed:17503797,
CC       ECO:0000269|PubMed:25903106, 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. In agreement with the authors, it has
CC       been decided to indicate the boundaries of the peptides according to
CC       the positions within the precursor, and not in the mature protein, as
CC       has formerly been proposed (Probable). Histatin 1, histatin 3 and
CC       histatin 5 constitute more than 80% of the total histatin concentration
CC       (Probable). {ECO:0000305|PubMed:20973643, ECO:0000305|PubMed:3286634}.
CC   -!- SIMILARITY: Belongs to the histatin/statherin family. {ECO:0000305}.
CC   -!- CAUTION: [Histatin-1]: Has been reported to promote cell proliferation
CC       (PubMed:18650243). However other studies were unable to demonstrate any
CC       cell proliferation activity (PubMed:25903106, PubMed:28751526,
CC       PubMed:28542418, PubMed:32225006). The peptide named histatin 2 was
CC       mistakenly described as the non-phosphorylated form of histatin 1 by
CC       some authors (PubMed:17503797). {ECO:0000269|PubMed:17503797,
CC       ECO:0000269|PubMed:18650243, ECO:0000269|PubMed:25903106,
CC       ECO:0000269|PubMed:28542418, ECO:0000269|PubMed:28751526,
CC       ECO:0000269|PubMed:32225006}.
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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; 3.
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; 9606-ENSP00000424501; -.
DR   PeptideAtlas; P15515; -.
DR   ProteomicsDB; 53165; -.
DR   TopDownProteomics; P15515; -.
DR   Antibodypedia; 24284; 72 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   AGR; HGNC:5283; -.
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; 4682135at2759; -.
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 615 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 male germ line stem cell (sensu Vertebrata) in testis and 33 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; 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; IEA:UniProtKB-KW.
DR   GO; GO:0022409; P:positive regulation of cell-cell adhesion; IDA:UniProtKB.
DR   GO; GO:0009893; P:positive regulation of metabolic process; IDA:UniProtKB.
DR   GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR   GO; GO:0035470; P:positive regulation of vascular wound healing; IDA:UniProtKB.
DR   GO; GO:0090303; P:positive regulation of wound healing; IDA:UniProtKB.
DR   GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IDA:UniProtKB.
DR   InterPro; IPR030773; Histatin/statherin.
DR   PANTHER; PTHR15057:SF2; HISTATIN-1; 1.
DR   PANTHER; PTHR15057; STATHERIN; 1.
DR   Genevisible; P15515; HS.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Biomineralization; Direct protein sequencing;
KW   Endoplasmic reticulum; Fungicide; Membrane; Mitochondrion; Phosphoprotein;
KW   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   REGION          51..56
FT                   /note="Involved in wound healing"
FT                   /evidence="ECO:0000269|PubMed:18650243"
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
//