BDS5C_HETCR
ID BDS5C_HETCR Reviewed; 41 AA.
AC C0HL53;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 18-JUL-2018, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=Pi-stichotoxin-Hcr5c {ECO:0000303|PubMed:29684594};
DE Short=Pi-SHTX-Hcr5c {ECO:0000305|PubMed:29684594};
DE AltName: Full=APETx-like peptide {ECO:0000303|PubMed:32326130};
DE AltName: Full=Pi-AnmTX Hcr 1b-3 {ECO:0000303|PubMed:29684594};
DE Short=Hcr 1b-3 {ECO:0000303|PubMed:32326130};
OS Heteractis crispa (Leathery sea anemone) (Radianthus macrodactylus).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Stichodactylidae; Heteractis.
OX NCBI_TaxID=175771;
RN [1]
RP PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=29684594; DOI=10.1016/j.peptides.2018.04.013;
RA Kalina R., Gladkikh I., Dmitrenok P., Chernikov O., Koshelev S.,
RA Kvetkina A., Kozlov S., Kozlovskaya E., Monastyrnaya M.;
RT "New APETx-like peptides from sea anemone Heteractis crispa modulate ASIC1a
RT channels.";
RL Peptides 104:41-49(2018).
RN [2]
RP FUNCTION.
RX PubMed=32326130; DOI=10.3390/toxins12040266;
RA Kalina R.S., Koshelev S.G., Zelepuga E.A., Kim N.Y., Kozlov S.A.,
RA Kozlovskaya E.P., Monastyrnaya M.M., Gladkikh I.N.;
RT "APETx-Like peptides from the sea anemone Heteractis crispa, diverse in
RT their effect on ASIC1a and ASIC3 ion channels.";
RL Toxins 12:0-0(2020).
CC -!- FUNCTION: Weakly and reversibly inhibits rat homomeric ASIC1 (isoform
CC ASIC1a) (IC(50)=4.95 uM), and ASIC3 (IC(50)=17 uM) (PubMed:29684594,
CC PubMed:32326130). ASIC1a current inhibition and ASIC3 transient current
CC inhibition are not complete, and reach a maximum of 70% inhibition and
CC 80%, respectively (PubMed:32326130). {ECO:0000269|PubMed:29684594,
CC ECO:0000269|PubMed:32326130}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Nematocyst {ECO:0000305}.
CC -!- MASS SPECTROMETRY: Mass=4519.9; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:29684594};
CC -!- SIMILARITY: Belongs to the sea anemone type 3 (BDS) potassium channel
CC toxin family. {ECO:0000305}.
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DR AlphaFoldDB; C0HL53; -.
DR SMR; C0HL53; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0008200; F:ion channel inhibitor activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR Gene3D; 2.20.20.10; -; 1.
DR InterPro; IPR012414; BDS_K_chnl_tox.
DR InterPro; IPR023355; Myo_ane_neurotoxin_sf.
DR Pfam; PF07936; Defensin_4; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Ion channel impairing toxin;
KW Nematocyst; Proton-gated sodium channel impairing toxin; Secreted; Toxin.
FT PEPTIDE 1..41
FT /note="Pi-stichotoxin-Hcr5c"
FT /evidence="ECO:0000269|PubMed:29684594"
FT /id="PRO_0000444938"
FT DISULFID 4..37
FT /evidence="ECO:0000250|UniProtKB:P61541"
FT DISULFID 6..30
FT /evidence="ECO:0000250|UniProtKB:P61541"
FT DISULFID 20..38
FT /evidence="ECO:0000250|UniProtKB:P61541"
SQ SEQUENCE 41 AA; 4529 MW; 93599A7EC5079829 CRC64;
GTPCKCHGYI GVYWFMLAGC PDGYGYNLSC PYFLGICCVK K