ID   DFAM1_LYMST             Reviewed;          13 AA.
AC   P80178;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   22-APR-2020, entry version 46.
DE   RecName: Full=Lymna-DF-amide 1;
OS   Lymnaea stagnalis (Great pond snail) (Helix stagnalis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC   Lymnaeidae; Lymnaea.
OX   NCBI_TaxID=6523;
RN   [1]
RP   PROTEIN SEQUENCE, AND AMIDATION AT PHE-13.
RC   TISSUE=Ganglion;
RX   PubMed=8477756; DOI=10.1111/j.1432-1033.1993.tb17831.x;
RA   Johnsen A.H., Rehfeld J.F.;
RT   "LymnaDFamides, a new family of neuropeptides from the pond snail, Lymnaea
RT   stagnalis. Clue to cholecystokinin immunoreactivity in invertebrates?";
RL   Eur. J. Biochem. 213:875-879(1993).
CC   -!- SUBCELLULAR LOCATION: Secreted.
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DR   PIR; S32471; S32471.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Amidation; Direct protein sequencing; Neuropeptide; Secreted.
FT   PEPTIDE         1..13
FT                   /note="Lymna-DF-amide 1"
FT                   /id="PRO_0000043902"
FT   MOD_RES         13
FT                   /note="Phenylalanine amide"
FT                   /evidence="ECO:0000269|PubMed:8477756"
SQ   SEQUENCE   13 AA;  1519 MW;  9CA07BA3F5D5B455 CRC64;
     PYDRISNSAF SDF