K1B2_OULSP
ID K1B2_OULSP Reviewed; 82 AA.
AC A0A330KUG5; A0A384E124;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 1.
DT 25-MAY-2022, entry version 8.
DE RecName: Full=U-actitoxin-Oulsp2 {ECO:0000305|PubMed:29772211};
DE Short=U-AITX-Oulsp2 {ECO:0000303|PubMed:29772211};
DE AltName: Full=OspTx2b {ECO:0000303|PubMed:29772211};
DE Flags: Precursor;
OS Oulactis sp. (Sea anemone).
OC Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC Actiniidae; Oulactis; unclassified Oulactis.
OX NCBI_TaxID=2093647;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SYNTHESIS OF 47-82, STRUCTURE BY NMR OF 47-82,
RP AND DISULFIDE BOND.
RC STRAIN=MM-2018;
RX PubMed=29772211; DOI=10.1016/j.toxicon.2018.05.006;
RA Krishnarjuna B., Villegas-Moreno J., Mitchell M.L., Csoti A., Peigneur S.,
RA Amero C., Pennington M.W., Tytgat J., Panyi G., Norton R.S.;
RT "Synthesis, folding, structure and activity of a predicted peptide from the
RT sea anemone Oulactis sp. with an ShKT fold.";
RL Toxicon 150:50-59(2018).
CC -!- FUNCTION: Probable toxin with unknown function. In contrast to similar
CC toxins, this toxin does not inhibit voltage-gated potassium channels
CC (tested at 100 nM). Does not show antimicrobial activities against
CC bacteria and yeasts. {ECO:0000269|PubMed:29772211}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:29772211}.
CC Nematocyst {ECO:0000305|PubMed:29772211}.
CC -!- MISCELLANEOUS: The 52-Leu-Pro-53 bond exists only in the trans-
CC isomerization. {ECO:0000269|PubMed:29772211}.
CC -!- MISCELLANEOUS: Has no effect on hKv1.1/KCNA1, hKv1.2/KCNA2,
CC hKv1.3/KCNA3, hKv11.1/KCNH2/ERG1, hKCa1.1/KCNMA1, hKCa3.1/KCNN4, and
CC hNav1.4/SCN4A (when tested at 100 nM). {ECO:0000269|PubMed:29772211}.
CC -!- SIMILARITY: Belongs to the sea anemone type 1 potassium channel toxin
CC family. Type 1b subfamily. {ECO:0000305}.
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DR EMBL; LT985997; SPF25672.1; -; mRNA.
DR PDB; 6BUC; NMR; -; A=47-82.
DR PDBsum; 6BUC; -.
DR AlphaFoldDB; A0A330KUG5; -.
DR SMR; A0A330KUG5; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042151; C:nematocyst; IEA:UniProtKB-SubCell.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR InterPro; IPR003582; ShKT_dom.
DR PROSITE; PS51670; SHKT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cleavage on pair of basic residues; Disulfide bond;
KW Nematocyst; Secreted; Signal; Toxin.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..46
FT /evidence="ECO:0000305"
FT /id="PRO_0000448545"
FT CHAIN 47..82
FT /note="U-actitoxin-Oulsp2"
FT /evidence="ECO:0000305|PubMed:29772211"
FT /id="PRO_5016428214"
FT DOMAIN 48..82
FT /note="ShKT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01005"
FT REGION 70..71
FT /note="Theoritically crucial for binding to potassium
FT channels"
FT /evidence="ECO:0000250|UniProtKB:P29186"
FT DISULFID 48..82
FT /evidence="ECO:0000269|PubMed:29772211,
FT ECO:0007744|PDB:6BUC"
FT DISULFID 57..75
FT /evidence="ECO:0000269|PubMed:29772211,
FT ECO:0007744|PDB:6BUC"
FT DISULFID 66..79
FT /evidence="ECO:0000269|PubMed:29772211,
FT ECO:0007744|PDB:6BUC"
FT HELIX 54..62
FT /evidence="ECO:0007829|PDB:6BUC"
FT HELIX 65..67
FT /evidence="ECO:0007829|PDB:6BUC"
FT TURN 69..74
FT /evidence="ECO:0007829|PDB:6BUC"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:6BUC"
SQ SEQUENCE 82 AA; 9151 MW; 9DE78C5BEF5CC328 CRC64;
MNTKLVVVFL LSAILFVSVT ASRPGKDLER DEAYETYDDE RPYFKRACKD NLPAATCSNV
KANNNCSSEK YKTNCAKTCG EC
