ID   LWA_ANESU               Reviewed;         126 AA.
AC   Q17093;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=LWamide neuropeptides;
DE   Contains:
DE     RecName: Full=LWamide I;
DE   Contains:
DE     RecName: Full=LWamide II a;
DE   Contains:
DE     RecName: Full=LWamide II b;
DE   Contains:
DE     RecName: Full=Metamorphosin A;
DE              Short=MMA;
DE   Contains:
DE     RecName: Full=IWamide;
DE   Flags: Precursor; Fragment;
OS   Anemonia sulcata (Mediterranean snakelocks sea anemone).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Actiniaria;
OC   Actiniidae; Anemonia.
OX   NCBI_TaxID=6108;
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gajewski M., Leitz T., Schlossherr J., Plickert G.;
RT   "LWamides from Cnidaria constitute a novel family of neuropeptides with
RT   morphogenetic activity.";
RL   Roux's Arch. Dev. Biol. 205:232-242(1996).
CC   -!- FUNCTION: Metamorphosin A may be part of an internal signaling system
CC       involved in control of metamorphosis. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the LWamide neuropeptide family. {ECO:0000305}.
CC   -!- CAUTION: Opinions are divided on whether Anemonia viridis (Forsskal,
CC       1775) and Anemonia sulcata (Pennant, 1777) are separate species.
CC       {ECO:0000305}.
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DR   EMBL; X89736; CAA61888.1; -; mRNA.
DR   AlphaFoldDB; Q17093; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0007218; P:neuropeptide signaling pathway; IEA:UniProtKB-KW.
PE   2: Evidence at transcript level;
KW   Amidation; Cleavage on pair of basic residues; Neuropeptide; Repeat;
KW   Secreted.
FT   PROPEP          1..2
FT                   /note="1"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010029"
FT   PEPTIDE         3..8
FT                   /note="Metamorphosin A"
FT                   /id="PRO_0000010030"
FT   PROPEP          11..15
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010031"
FT   PEPTIDE         16..20
FT                   /note="LWamide I"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010032"
FT   PEPTIDE         24..29
FT                   /note="Metamorphosin A"
FT                   /id="PRO_0000010033"
FT   PROPEP          32..36
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010034"
FT   PEPTIDE         37..41
FT                   /note="LWamide I"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010035"
FT   PEPTIDE         45..50
FT                   /note="LWamide II a"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010036"
FT   PROPEP          53..57
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010037"
FT   PEPTIDE         58..62
FT                   /note="LWamide I"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010038"
FT   PEPTIDE         66..71
FT                   /note="LWamide II b"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010039"
FT   PROPEP          74..78
FT                   /note="2"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010040"
FT   PEPTIDE         79..83
FT                   /note="LWamide I"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010041"
FT   PROPEP          86..93
FT                   /note="3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010042"
FT   PEPTIDE         94..99
FT                   /note="IWamide"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010043"
FT   PROPEP          102..126
FT                   /note="4"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000010044"
FT   REGION          1..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         8
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         20
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         29
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         41
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         50
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         62
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         71
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         83
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         99
FT                   /note="Tryptophan amide"
FT                   /evidence="ECO:0000255"
FT   VARIANT         67
FT                   /note="H -> Q"
FT   NON_TER         1
SQ   SEQUENCE   126 AA;  13990 MW;  1085CEE373E07566 CRC64;
     KRQQPGLWGR SADPQQAGLW GKRQQPGLWG RSADPQQAGL WGKRQNPGLW GRSADPQQAG
     LWGKRQHPGL WGRSADPQQA GLWGRSAGSG KRQERIGIWG RSAEPPQYKE LEDLKQKSAI
     PKAKPQ