ID   TX121_URTEQ             Reviewed;          74 AA.
AC   C0HK26;
DT   05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   25-MAY-2022, entry version 12.
DE   RecName: Full=Tau-AnmTx Ueq 12-1 {ECO:0000303|PubMed:28468269};
DE            Short=Ueq 12-1 {ECO:0000303|PubMed:28468269};
DE   Flags: Precursor;
OS   Urticina eques (Sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Urticina.
OX   NCBI_TaxID=417072 {ECO:0000303|PubMed:28468269};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 30-63, STRUCTURE BY NMR OF
RP   30-74, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS
RP   SPECTROMETRY, AND DISULFIDE BONDS.
RX   PubMed=28468269; DOI=10.3390/toxins9050154;
RA   Logashina Y.A., Solstad R.G., Mineev K.S., Korolkova Y.V., Mosharova I.V.,
RA   Dyachenko I.A., Palikov V.A., Palikova Y.A., Murashev A.N., Arseniev A.S.,
RA   Kozlov S.A., Stensvag K., Haug T., Andreev Y.A.;
RT   "New disulfide-stabilized fold provides sea anemone peptide to exhibit both
RT   antimicrobial and TRPA1 potentiating properties.";
RL   Toxins 9:0-0(2017).
CC   -!- FUNCTION: Potentiates activation of mammalian TRPA1, a non-selective
CC       cation channel involved in perception of pain, in vitro yet has an
CC       analgesic and anti-inflammatory effect in vivo. Has antibacterial
CC       activity against C.glutamicum (MIC=50 uM) and, to a lesser extent,
CC       against S.aureus but not against P.aeruginosa or E.coli.
CC       {ECO:0000269|PubMed:28468269}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28468269}.
CC   -!- TISSUE SPECIFICITY: Detected in mucus secreted from ectoderm.
CC       {ECO:0000269|PubMed:28468269}.
CC   -!- MASS SPECTROMETRY: Mass=4788.63; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:28468269};
CC   -!- MISCELLANEOUS: Has no effect on mammalian TRPV1 and TRPV3.
CC       {ECO:0000269|PubMed:28468269}.
CC   -!- SIMILARITY: Belongs to the Cnidaria small cysteine-rich protein (SCRiP)
CC       family. {ECO:0000305}.
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DR   PDB; 5LAH; NMR; -; A=30-74.
DR   PDBsum; 5LAH; -.
DR   AlphaFoldDB; C0HK26; -.
DR   BMRB; C0HK26; -.
DR   SMR; C0HK26; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial;
KW   Cleavage on pair of basic residues; Direct protein sequencing;
KW   Disulfide bond; Secreted; Signal; Toxin.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   PROPEP          19..27
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000305|PubMed:28468269"
FT                   /id="PRO_0000440863"
FT   PEPTIDE         30..74
FT                   /note="Tau-AnmTx Ueq 12-1"
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT                   /id="PRO_0000440864"
FT   DISULFID        30..37
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT   DISULFID        40..71
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT   DISULFID        46..64
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT   DISULFID        51..72
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT   DISULFID        58..73
FT                   /evidence="ECO:0000269|PubMed:28468269"
FT   STRAND          45..49
FT                   /evidence="ECO:0007829|PDB:5LAH"
FT   HELIX           59..61
FT                   /evidence="ECO:0007829|PDB:5LAH"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:5LAH"
SQ   SEQUENCE   74 AA;  8080 MW;  444A7C6FBC82E723 CRC64;
     MCLLMLVLGA MYVQGWHSAG FGKRTLKKRC YPGQPGCGHC SRPNYCEGAR CESGFHDCGS
     DHWCDASGDR CCCA