ID   AEQL2_NEMVE             Reviewed;         117 AA.
AC   P0DQS0;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   23-FEB-2022, entry version 2.
DE   RecName: Full=Protein Aeq5-like2 {ECO:0000303|PubMed:33060291};
DE   AltName: Full=Nve8041 {ECO:0000303|PubMed:33060291};
OS   Nematostella vectensis (Starlet sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Edwardsiidae; Nematostella.
OX   NCBI_TaxID=45351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=33060291; DOI=10.1073/pnas.2011120117;
RA   Sachkova M.Y., Landau M., Surm J.M., Macrander J., Singer S.A.,
RA   Reitzel A.M., Moran Y.;
RT   "Toxin-like neuropeptides in the sea anemone Nematostella unravel
RT   recruitment from the nervous system to venom.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:27481-27492(2020).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Expressed in endodermal ganglion neurons,
CC       apparently bipolar and following mesentery folds (observed in both
CC       planulae and primary polyps). It not expressed in nematocytes.
CC       {ECO:0000269|PubMed:33060291}.
CC   -!- PTM: The mature peptide may be cleaved at a dibasic residue site and be
CC       shorter than the sequence shown (possibly residues 1-94).
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=National Center for Biotechnology Information
CC       (NCBI);
CC       URL="https://www.ncbi.nlm.nih.gov/nuccore/XM_032367382.1/";
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DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..117
FT                   /note="Protein Aeq5-like2"
FT                   /evidence="ECO:0000305|PubMed:33060291"
FT                   /id="PRO_0000453919"
FT   TOPO_DOM        1..36
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305|PubMed:33060291"
FT   TRANSMEM        37..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..117
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305|PubMed:33060291"
FT   DISULFID        59..94
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        63..90
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        70..83
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
FT   DISULFID        74..80
FT                   /evidence="ECO:0000250|UniProtKB:Q3C258"
SQ   SEQUENCE   117 AA;  13369 MW;  31732E61127F3D49 CRC64;
     MLVNARAIRQ SIGIVVAQCR RDLESNRTLD YRTRMRTSLI LVAMVMVSVL LPYTYGSSCD
     SFCTEQANKC LTGCEGFVGC MECTNFAGHC REQCRKRSVK RRKEIRARFT KEPTEES