ID   AP_HELPO                Reviewed;          13 AA.
AC   B3EWK7;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   17-JUN-2020, entry version 7.
DE   RecName: Full=Activity-dependent peptide {ECO:0000303|PubMed:20716464};
DE   Flags: Fragment;
OS   Helix pomatia (Roman snail) (Edible snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Helicoidea; Helicidae; Helix.
OX   NCBI_TaxID=6536;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, AND MASS SPECTROMETRY.
RC   TISSUE=CNS {ECO:0000269|PubMed:20716464};
RX   PubMed=20716464; DOI=10.1016/j.npep.2010.07.003;
RA   Pirger Z., Lubics A., Reglodi D., Laszlo Z., Mark L., Kiss T.;
RT   "Mass spectrometric analysis of activity-dependent changes of neuropeptide
RT   profile in the snail, Helix pomatia.";
RL   Neuropeptides 44:475-483(2010).
CC   -!- FUNCTION: Up-regulated in CNS of active, non-hibernating snails
CC       suggesting involvement in the regulation of hibernation and maintenance
CC       of the active state. {ECO:0000269|PubMed:20716464}.
CC   -!- MASS SPECTROMETRY: Mass=1110.75; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:20716464};
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DR   GO; GO:0042750; P:hibernation; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hibernation.
FT   CHAIN           1..>13
FT                   /note="Activity-dependent peptide"
FT                   /id="PRO_0000418107"
FT   NON_TER         13
FT                   /evidence="ECO:0000303|PubMed:20716464"
SQ   SEQUENCE   13 AA;  1110 MW;  282EE3704FFD85B8 CRC64;
     GSGASGSMPA TTS