ID   PEP_CENTE               Reviewed;          32 AA.
AC   C0HJW4;
DT   06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT   06-JUL-2016, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Peptide II.10.10 {ECO:0000303|PubMed:26921461};
OS   Centruroides tecomanus (Scorpion) (Centruroides limpidus tecomanus).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Centruroides.
OX   NCBI_TaxID=1028682;
RN   [1]
RP   PROTEIN SEQUENCE, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   TISSUE=Venom;
RX   PubMed=26921461; DOI=10.1016/j.toxicon.2016.02.017;
RA   Olamendi-Portugal T., Bartok A., Zamudio-Zuniga F., Balajthy A.,
RA   Becerril B., Panyi G., Possani L.D.;
RT   "Isolation, chemical and functional characterization of several new K(+)-
RT   channel blocking peptides from the venom of the scorpion Centruroides
RT   tecomanus.";
RL   Toxicon 115:1-12(2016).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26921461}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:26921461}.
CC   -!- DOMAIN: Has the structural arrangement of an alpha-helix connected to
CC       antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=3907.0; Method=Unknown;
CC       Evidence={ECO:0000269|PubMed:26921461};
CC   -!- MISCELLANEOUS: Has no effect on voltage-gated potassium channels
CC       Kv1.1/KCNA1, Kv1.2/KCNA2, Kv1.3/KCNA3 and Shaker IR (with inactivation
CC       domain removed) and on intermediate conductance calcium-activated
CC       potassium channel KCa3.1/KCNN4. Does not show antimicrobial activity as
CC       well. {ECO:0000269|PubMed:26921461}.
CC   -!- SIMILARITY: Belongs to the short scorpion toxin superfamily. Potassium
CC       channel inhibitor family. Alpha-KTx 10 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; C0HJW4; -.
DR   SMR; C0HJW4; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR036574; Scorpion_toxin-like_sf.
DR   SUPFAM; SSF57095; SSF57095; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Secreted.
FT   PEPTIDE         1..32
FT                   /note="Peptide II.10.10"
FT                   /evidence="ECO:0000269|PubMed:26921461"
FT                   /id="PRO_0000436540"
FT   DISULFID        5..24
FT                   /evidence="ECO:0000305"
FT   DISULFID        10..29
FT                   /evidence="ECO:0000305"
FT   DISULFID        14..31
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   32 AA;  3913 MW;  67C6D721DED2DAC7 CRC64;
     IRRYCDPRVC DRECLEKGKY FGRCIRDICK CN