ID   NDB4V_TITSE             Reviewed;           8 AA.
AC   P86828; C0HJT3;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   23-FEB-2022, entry version 12.
DE   RecName: Full=Venom peptide 7.1 {ECO:0000303|PubMed:27221550};
DE   AltName: Full=Venom peptide 7 {ECO:0000303|PubMed:18718845};
DE   Contains:
DE     RecName: Full=Venom peptide 7.2 {ECO:0000303|PubMed:27221550};
OS   Tityus serrulatus (Brazilian scorpion).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Scorpiones; Buthida; Buthoidea; Buthidae; Tityus.
OX   NCBI_TaxID=6887;
RN   [1]
RP   PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000269|PubMed:18718845};
RX   PubMed=18718845; DOI=10.1016/j.toxicon.2008.07.010;
RA   Rates B., Ferraz K.K., Borges M.H., Richardson M., De Lima M.E.,
RA   Pimenta A.M.;
RT   "Tityus serrulatus venom peptidomics: assessing venom peptide diversity.";
RL   Toxicon 52:611-618(2008).
RN   [2]
RP   PROTEIN SEQUENCE, FUNCTION, AND SUBCELLULAR LOCATION.
RC   TISSUE=Venom {ECO:0000303|PubMed:27221550};
RX   PubMed=27221550; DOI=10.1016/j.peptides.2016.05.008;
RA   Pucca M.B., Cerni F.A., Pinheiro-Junior E.L., Zoccal K.F., Bordon K.C.,
RA   Amorim F.G., Peigneur S., Vriens K., Thevissen K., Cammue B.P.,
RA   Junior R.B., Arruda E., Faccioli L.H., Tytgat J., Arantes E.C.;
RT   "Non-disulfide-bridged peptides from Tityus serrulatus venom: Evidence for
RT   proline-free ACE-inhibitors.";
RL   Peptides 82:44-51(2016).
CC   -!- FUNCTION: [Venom peptide 7.1]: Has a weak inhibitory effect on voltage-
CC       gated sodium channel Nav1.5/SCN5A. Inhibits acetylcholine esterase in
CC       vitro. Increases interleukin-6 secretion from macrophages in vitro. Has
CC       no antifungal, antiviral or cytotoxic activity.
CC       {ECO:0000269|PubMed:27221550}.
CC   -!- FUNCTION: [Venom peptide 7.2]: Strongly inhibits acetylcholine esterase
CC       in vitro. Increases Il-6 secretion from macrophages in vitro. Has no
CC       antifungal, antiviral or cytotoxic activity.
CC       {ECO:0000269|PubMed:27221550}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18718845,
CC       ECO:0000269|PubMed:27221550}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland. {ECO:0000305}.
CC   -!- MISCELLANEOUS: No effect on voltage-gated potassium channels. No effect
CC       on voltage-gated sodium channels Nav1.2/SCN2A, Nav1.3/SCN3A,
CC       Nav1.4/SCN4A and a sodium channel from B.germanica.
CC       {ECO:0000269|PubMed:27221550}.
CC   -!- SIMILARITY: Belongs to the non-disulfide-bridged peptide (NDBP)
CC       superfamily. Short antimicrobial peptide (group 4) family.
CC       {ECO:0000305}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Ion channel impairing toxin; Secreted; Toxin;
KW   Voltage-gated sodium channel impairing toxin.
FT   PEPTIDE         1..8
FT                   /note="Venom peptide 7.1"
FT                   /evidence="ECO:0000269|PubMed:18718845"
FT                   /id="PRO_0000401156"
FT   PEPTIDE         1..6
FT                   /note="Venom peptide 7.2"
FT                   /evidence="ECO:0000269|PubMed:27221550"
FT                   /id="PRO_0000438307"
FT   UNSURE          7
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:18718845"
FT   UNSURE          8
FT                   /note="K or Q"
FT                   /evidence="ECO:0000269|PubMed:18718845"
SQ   SEQUENCE   8 AA;  972 MW;  3933387325A40734 CRC64;
     RLRSKGKK