KPHAB_ACTTE
ID KPHAB_ACTTE Reviewed; 17 AA.
AC P0DM22; A0A452CSQ6;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 13.
DE RecName: Full=Kappa-actitoxin-Ate1a {ECO:0000303|PubMed:30109357};
DE Short=Ate1a {ECO:0000303|PubMed:30109357};
OS Actinia tenebrosa (Australian red waratah sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Actinia.
OX NCBI_TaxID=6105;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE, SYNTHESIS, MASS SPECTROMETRY,
RP STRUCTURE BY NMR, FUNCTION, BIOASSAY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AMIDATION AT GLY-17, AND DISULFIDE BOND.
RC TISSUE=Tentacle;
RX PubMed=30109357; DOI=10.1007/s00018-018-2897-6;
RA Madio B., Peigneur S., Chin Y.K.Y., Hamilton B.R., Henriques S.T.,
RA Smith J.J., Cristofori-Armstrong B., Dekan Z., Boughton B.A., Alewood P.F.,
RA Tytgat J., King G.F., Undheim E.A.B.;
RT "PHAB toxins: a unique family of predatory sea anemone toxins evolving via
RT intra-gene concerted evolution defines a new peptide fold.";
RL Cell. Mol. Life Sci. 75:4511-4524(2018).
CC -!- FUNCTION: Voltage-gated potassium channel inhibitor that is certainly
CC used for prey capture (PubMed:30109357). It inhibits several potassium
CC channels, but not all (Kv1.1/KCNA1 (IC(50)=353 nM), Kv1.2/KCNA2
CC (IC(50)=146 nM), Kv1.3/KCNA3 (IC(50)=3051 nM), Kv1.6/KCNA6 (IC(50)=191
CC nM), and Shaker IR (23% inhibition at 3 uM)) (PubMed:30109357). In
CC vivo, injection of this toxin into amphipods results in impaired
CC swimming followed by contractile paralysis (PubMed:30109357).
CC {ECO:0000269|PubMed:30109357}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30109357}.
CC Nematocyst {ECO:0000305|PubMed:30109357}.
CC -!- TISSUE SPECIFICITY: Expressed by tentacle.
CC {ECO:0000269|PubMed:30109357}.
CC -!- DOMAIN: Adopts the three-dimensional structure 'proline-hinged
CC asymmetric beta-hairpin-like' (PHAB) fold.
CC {ECO:0000305|PubMed:30109357}.
CC -!- DOMAIN: The prepropeptide contains 10 domains separated by dibasic
CC cleavage sites: a signal peptide, three cysteine-containing propeptide
CC domains (CysPro), three cysteine-free propeptide domains (LinearPro)
CC and three Kappa-actitoxin-Ate1a (PHAB) domains. The sequence 'CysPro-
CC LinearPro-PHAB' is repeated three times. {ECO:0000305|PubMed:30109357}.
CC -!- MASS SPECTROMETRY: Mass=1887.93; Method=MALDI; Note=Monoisotopic mass.;
CC Evidence={ECO:0000269|PubMed:30109357};
CC -!- MISCELLANEOUS: Does not show antimicrobial activity (when 256 ug/mL are
CC tested on E.coli, K.pneumoniae, A.baumannii, P.aeruginosa, and
CC S.aureus, as well as on fungi C.albicans and C.neoformans)
CC (PubMed:30109357). Is not cytotoxic or cytolytic against cultured human
CC cancer cell lines and erythrocytes (PubMed:30109357). It shows only a
CC weak affinity for lipid membranes (PubMed:30109357). It has no effect
CC on Kv1.4/KCNA4, Kv1.5/KCNA5, Kv2.1/KCNB1, Kv3.1/KCNC1, Kv4.2/KCND2,
CC Kv7.2/KCNQ2, and Kv11.1/KCNH2/ERG1 (PubMed:30109357).
CC {ECO:0000269|PubMed:30109357}.
CC -!- SIMILARITY: Belongs to the sea anemonne PHAB family. {ECO:0000305}.
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DR PDB; 6AZA; NMR; -; A=1-17.
DR PDBsum; 6AZA; -.
DR AlphaFoldDB; P0DM22; -.
DR BMRB; P0DM22; -.
DR SMR; P0DM22; -.
DR Proteomes; UP000515163; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0015459; F:potassium channel regulator activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW 3D-structure; Amidation; Direct protein sequencing; Disulfide bond;
KW Ion channel impairing toxin; Nematocyst; Neurotoxin;
KW Potassium channel impairing toxin; Reference proteome; Secreted; Toxin;
KW Voltage-gated potassium channel impairing toxin.
FT PEPTIDE 1..17
FT /note="Kappa-actitoxin-Ate1a"
FT /evidence="ECO:0000269|PubMed:30109357"
FT /id="PRO_0000445681"
FT MOD_RES 17
FT /note="Glycine amide"
FT /evidence="ECO:0000269|PubMed:30109357"
FT DISULFID 2..16
FT /evidence="ECO:0000269|PubMed:30109357,
FT ECO:0007744|PDB:6AZA"
FT DISULFID 5..10
FT /evidence="ECO:0000269|PubMed:30109357,
FT ECO:0007744|PDB:6AZA"
SQ SEQUENCE 17 AA; 1894 MW; 39FE97B6EEE828FB CRC64;
RCKTCSKGRC RPKPNCG
