A0A2L1DGG0 · HSTX1_HAESL
- ProteinPeptide HSTX-I
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Leech salivary gland peptide with unknown function (PubMed:32524995).
It was originally described as exhibiting analgesic function by specifically inhibiting rodent Nav1.8/SCN10A and Nav1.9/SCN11A voltage-gated sodium channels, as well as showing analgesic activities in several mouse models (PubMed:29559913).
In a second study, the synthetic peptide has been shown as having very weak activity on Nav1.8/SCN10A at the highest concentration tested (90 uM) and as being only very modestly active at hNav1.9/SCN11A, with a modest peak current size reduction (~19%) at high concentrations (10 uM) (PubMed:32524995).
In addition, this second study reports no analgesic activity in a mouse model of inflammatory pain (PubMed:32524995).
It was originally described as exhibiting analgesic function by specifically inhibiting rodent Nav1.8/SCN10A and Nav1.9/SCN11A voltage-gated sodium channels, as well as showing analgesic activities in several mouse models (PubMed:29559913).
In a second study, the synthetic peptide has been shown as having very weak activity on Nav1.8/SCN10A at the highest concentration tested (90 uM) and as being only very modestly active at hNav1.9/SCN11A, with a modest peak current size reduction (~19%) at high concentrations (10 uM) (PubMed:32524995).
In addition, this second study reports no analgesic activity in a mouse model of inflammatory pain (PubMed:32524995).
Miscellaneous
Does not show effect on voltage-gated calcium channels, potassium channels, and tetrodotoxin-sensitive sodium channels (PubMed:29559913).
Does not show activity on Nav1.7/SCN9A, and shows very weak activity on cation channel TRPA1 (PubMed:32524995).
Does not show activity on Nav1.7/SCN9A, and shows very weak activity on cation channel TRPA1 (PubMed:32524995).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region |
Names & Taxonomy
Protein names
- Recommended namePeptide HSTX-I
Organism names
- Taxonomic lineageEukaryota > Metazoa > Spiralia > Lophotrochozoa > Annelida > Clitellata > Hirudinea > Hirudinida > Hirudiniformes > Haemadipsidae > Haemadipsa
Accessions
- Primary accessionA0A2L1DGG0
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, peptide, disulfide bond, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MRTLLVFLLLAIFVAVLIGNV | ||||||
Propeptide | PRO_0000452215 | 22-28 | ||||
Sequence: QVEAACK | ||||||
Peptide | PRO_5014992413 | 26-48 | Peptide HSTX-I | |||
Sequence: ACKEYWECGAFLFCIEGICVPMI | ||||||
Disulfide bond | 27↔39 | |||||
Sequence: CKEYWECGAFLFC | ||||||
Disulfide bond | 33↔44 | |||||
Sequence: CGAFLFCIEGIC | ||||||
Modified residue | 48 | Isoleucine amide | ||||
Sequence: I |
Keywords
- PTM
Expression
Tissue specificity
Expressed in salivary glands. Highly expressed in the head, body and tail with a 2-3-fold higher expression in the head.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length49
- Mass (Da)5,409
- Last updated2021-04-07 v2
- Checksum38DF53B293A9C102
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 8 | in Ref. 1; AVC68883 | ||||
Sequence: L → LVFL |
Mass Spectrometry
Keywords
- Technical term