LWA_HYDEC
ID LWA_HYDEC Reviewed; 419 AA.
AC Q25060;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 44.
DE RecName: Full=LWamide neuropeptides;
DE Contains:
DE RecName: Full=LWamide I;
DE Contains:
DE RecName: Full=LWamide II;
DE Contains:
DE RecName: Full=LWS;
DE Flags: Precursor;
OS Hydractinia echinata (Snail fur) (Hermit crab hydroid).
OC Eukaryota; Metazoa; Cnidaria; Hydrozoa; Hydroidolina; Anthoathecata;
OC Filifera; Hydractiniidae; Hydractinia.
OX NCBI_TaxID=35630;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
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: LWamide peptides may be involved in induction of
CC metamorphosis.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q25060-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q25060-2; Sequence=VSP_050202;
CC -!- TISSUE SPECIFICITY: In planula larvae, expressed in a narrow ring of
CC ectodermal neurosensory cells around the widest circumference at the
CC anterior of the larvae. In primary polyps, expression is confined to
CC endodermal cells of the hypostome. In mature polyps, expression is
CC strong in the epidermis from the tentacle level to the base of the
CC polyp and weak in the gastrodermal cells in the apical hypostome.
CC {ECO:0000269|Ref.1}.
CC -!- DEVELOPMENTAL STAGE: Expressed at a low level in mature polyps and
CC planula larvae, and at a high level in primary polyps.
CC {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the LWamide neuropeptide family. {ECO:0000305}.
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DR EMBL; X89734; CAA61886.1; -; mRNA.
DR AlphaFoldDB; Q25060; -.
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 Alternative splicing; Amidation; Cleavage on pair of basic residues;
KW Neuropeptide; Repeat; Secreted; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..104
FT /evidence="ECO:0000255"
FT /id="PRO_0000010045"
FT PEPTIDE 105..110
FT /note="LWamide I"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010046"
FT PROPEP 113..140
FT /evidence="ECO:0000255"
FT /id="PRO_0000010047"
FT PEPTIDE 141..146
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010048"
FT PROPEP 149..150
FT /evidence="ECO:0000255"
FT /id="PRO_0000010049"
FT PEPTIDE 151..156
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010050"
FT PROPEP 159..160
FT /evidence="ECO:0000255"
FT /id="PRO_0000010051"
FT PEPTIDE 161..166
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010052"
FT PROPEP 169..170
FT /evidence="ECO:0000255"
FT /id="PRO_0000010053"
FT PEPTIDE 171..176
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010054"
FT PROPEP 179..180
FT /evidence="ECO:0000255"
FT /id="PRO_0000010055"
FT PEPTIDE 181..186
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010056"
FT PROPEP 189..190
FT /evidence="ECO:0000255"
FT /id="PRO_0000010057"
FT PEPTIDE 191..196
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010058"
FT PROPEP 199..200
FT /evidence="ECO:0000255"
FT /id="PRO_0000010059"
FT PEPTIDE 201..206
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010060"
FT PROPEP 209..210
FT /evidence="ECO:0000255"
FT /id="PRO_0000010061"
FT PEPTIDE 211..216
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010062"
FT PROPEP 218..220
FT /note="Seems to have a sequencing error or a mutation in
FT position 218; Gly instead of Arg"
FT /id="PRO_0000010063"
FT PEPTIDE 221..226
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010064"
FT PROPEP 229..230
FT /evidence="ECO:0000255"
FT /id="PRO_0000010065"
FT PEPTIDE 231..236
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010066"
FT PROPEP 239..240
FT /evidence="ECO:0000255"
FT /id="PRO_0000010067"
FT PEPTIDE 241..246
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010068"
FT PROPEP 249..250
FT /evidence="ECO:0000255"
FT /id="PRO_0000010069"
FT PEPTIDE 251..256
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010070"
FT PROPEP 259..260
FT /evidence="ECO:0000255"
FT /id="PRO_0000010071"
FT PEPTIDE 261..266
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010072"
FT PROPEP 269..270
FT /evidence="ECO:0000255"
FT /id="PRO_0000010073"
FT PEPTIDE 271..276
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010074"
FT PROPEP 279..280
FT /evidence="ECO:0000255"
FT /id="PRO_0000010075"
FT PEPTIDE 281..286
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010076"
FT PROPEP 289..290
FT /evidence="ECO:0000255"
FT /id="PRO_0000010077"
FT PEPTIDE 291..296
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010078"
FT PROPEP 299..300
FT /evidence="ECO:0000255"
FT /id="PRO_0000010079"
FT PEPTIDE 301..307
FT /note="LWS"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010080"
FT PROPEP 309..320
FT /evidence="ECO:0000255"
FT /id="PRO_0000010081"
FT PEPTIDE 321..326
FT /note="LWamide II"
FT /evidence="ECO:0000255"
FT /id="PRO_0000010082"
FT PROPEP 329..419
FT /evidence="ECO:0000255"
FT /id="PRO_0000010083"
FT REGION 27..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 146
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 156
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 166
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 176
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 186
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 196
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 206
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 216
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 226
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 236
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 246
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 256
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 266
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 276
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 286
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 296
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT MOD_RES 326
FT /note="Tryptophan amide"
FT /evidence="ECO:0000255"
FT VAR_SEQ 185..214
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_050202"
FT VARIANT 66
FT /note="I -> T (in clone M6)"
FT VARIANT 414
FT /note="K -> N (in clone M6)"
SQ SEQUENCE 419 AA; 47058 MW; D383FFBE7D3775DC CRC64;
MEKEMRNLML LVLLTVILDN GIGKCNAKSE EDQDGNARNN RIDKNDDNSD SIEKYLREVT
DELSKILAKR IYRDIQLREN NKKAENRQSW IGDLENLDID STVQRPPGLW GREADFDNTR
AHDSAQISDE KQSGLWVGDA KPPGLWGRDA KPPGLWGRDA KPPGLWGRDA KPPGLWGRDA
KPPGLWGRDA KPPGLWGRDA KPPGLWGRDA KPPGLWGGDA KPPGLWGRDA KPPGLWGRDA
KPPGLWGRDA KPPGLWGRDA KPPGLWGRDA KPPGLWGRDT KPPGLWGRDA KPPGLWGRDA
KPPSLWSKDN NVIKSRSDDA KPPGLWGRQV EDGPTKIWGD GFLDAERHIR LLKNDERFNR
LEKKADMEEE LRVAQGPSVT NAKDTFGELA DLLRKRIVKR LHKNDSLNNR RNNKKNNKF
