HSTX2_HAESL
ID HSTX2_HAESL Reviewed; 47 AA.
AC P0DUG5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 1.
DT 25-MAY-2022, entry version 3.
DE RecName: Full=Peptide HSTX-II {ECO:0000303|PubMed:29559913};
DE Flags: Precursor;
OS Haemadipsa sylvestris (Indian leech).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC Hirudinea; Hirudinida; Hirudiniformes; Haemadipsidae; Haemadipsa.
OX NCBI_TaxID=13555;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Salivary gland;
RX PubMed=29559913; DOI=10.3389/fphar.2018.00186;
RA Wang G., Long C., Liu W., Xu C., Zhang M., Li Q., Lu Q., Meng P., Li D.,
RA Rong M., Sun Z., Luo X., Lai R.;
RT "Novel sodium channel inhibitor from leeches.";
RL Front. Pharmacol. 9:186-186(2018).
CC -!- FUNCTION: Leech salivary gland peptide with unknown function.
CC {ECO:0000250|UniProtKB:A0A2L1DGG0}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A2L1DGG0}.
CC -!- TISSUE SPECIFICITY: Expressed in salivary glands. Highly expressed in
CC the head, body and tail with a 2-3-fold higher expression in the head.
CC {ECO:0000250|UniProtKB:A0A2L1DGG0}.
CC -!- MISCELLANEOUS: Does not show effect on voltage-gated calcium channels,
CC potassium channels, and tetrodotoxin-sensitive sodium channels. Does
CC not show activity on Nav1.7/SCN9A, and shows very weak activity on
CC cation channel TRPA1. {ECO:0000250|UniProtKB:A0A2L1DGG0}.
CC -!- SIMILARITY: Belongs to the annelide toxin family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; P0DUG5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE 3: Inferred from homology;
KW Amidation; Disulfide bond; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..27
FT /evidence="ECO:0000250|UniProtKB:A0A2L1DGG0"
FT /id="PRO_0000452216"
FT PEPTIDE 28..46
FT /note="Peptide HSTX-II"
FT /evidence="ECO:0000250|UniProtKB:A0A2L1DGG0"
FT /id="PRO_0000452217"
FT MOD_RES 46
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000250|UniProtKB:A0A2L1DGG0"
FT DISULFID 26..37
FT /evidence="ECO:0000250|UniProtKB:A0A2L1DGG0"
FT DISULFID 32..42
FT /evidence="ECO:0000250|UniProtKB:A0A2L1DGG0"
SQ SEQUENCE 47 AA; 5015 MW; 4D8E6F7BECDD1436 CRC64;
MKTLLVFLLL AILVAVFIGN AQVEACKNHT DCLSGICLKG FCMPAFG