HM1B_PHLSP
ID HM1B_PHLSP Reviewed; 90 AA.
AC P0DL58;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2015, sequence version 1.
DT 25-MAY-2022, entry version 12.
DE RecName: Full=Mu-theraphotoxin-Phlo1b {ECO:0000303|PubMed:26134258};
DE Short=Mu-TRTX-Phlo1b {ECO:0000303|PubMed:26134258};
DE Flags: Precursor;
OS Phlogius sp. (Tarantula spider).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC Mygalomorphae; Theraphosidae; Phlogius; unclassified Phlogius.
OX NCBI_TaxID=1690075;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 59-71, FUNCTION, MASS
RP SPECTROMETRY, AMIDATION AT PHE-85, AND SUBCELLULAR LOCATION.
RC TISSUE=Venom, and Venom gland;
RX PubMed=26134258; DOI=10.3390/toxins7072494;
RA Chow C.Y., Cristofori-Armstrong B., Undheim E.A., King G.F., Rash L.D.;
RT "Three peptide modulators of the human voltage-gated sodium channel 1.7, an
RT important analgesic target, from the venom of an Australian tarantula.";
RL Toxins 7:2494-2513(2015).
CC -!- FUNCTION: Gating-modifier toxin that inhibits voltage-gated sodium
CC channel Nav by shifting the threshold for channel activation to more
CC positive potentials. This toxin moderately inhibits human Nav1.7/SCN9A
CC (IC(50)=360 nM) and weakly inhibits hNav1.2/SCN2A (37% inhibition at 1
CC uM peptide) and hNav1.5/SCN5A (<20% inhibition at 1 uM peptide).
CC Inhibition of Nav1.7 is voltage-dependent, with lower inhibition at
CC more positive test pulses. {ECO:0000269|PubMed:26134258}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26134258}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000305|PubMed:26134258}.
CC -!- DOMAIN: The presence of a 'disulfide through disulfide knot'
CC structurally defines this protein as a knottin.
CC {ECO:0000305|PubMed:26134258}.
CC -!- MASS SPECTROMETRY: Mass=4138.76; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:26134258};
CC -!- SIMILARITY: Belongs to the neurotoxin 10 (Hwtx-1) family. 39 (Jztx-34)
CC subfamily. {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; P0DL58; -.
DR SMR; P0DL58; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR011696; Huwentoxin-1.
DR Pfam; PF07740; Toxin_12; 1.
PE 1: Evidence at protein level;
KW Amidation; Cardiotoxin; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Neurotoxin; Secreted; Signal; Toxin;
KW Voltage-gated sodium channel impairing toxin.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..50
FT /evidence="ECO:0000305"
FT /id="PRO_0000434303"
FT CHAIN 51..85
FT /note="Mu-theraphotoxin-Phlo1b"
FT /evidence="ECO:0000269|PubMed:26134258"
FT /id="PRO_0000434304"
FT PROPEP 86..90
FT /evidence="ECO:0000305"
FT /id="PRO_0000434305"
FT MOD_RES 85
FT /note="Phenylalanine amide"
FT /evidence="ECO:0000269|PubMed:26134258"
FT DISULFID 52..66
FT /evidence="ECO:0000250|UniProtKB:P0C247"
FT DISULFID 59..71
FT /evidence="ECO:0000250|UniProtKB:P0C247"
FT DISULFID 65..79
FT /evidence="ECO:0000250|UniProtKB:P0C247"
SQ SEQUENCE 90 AA; 10207 MW; C421A71E70AC2871 CRC64;
MKVSVLITLA VLGVMFVWTS AAEQEDHGSD RRDSPALLKS LGRVFQSEER ACRELLGGCS
KDSDCCAHLE CRKKWPYHCV WDWTFGNEKS
