ID   NEUM_SERCA              Reviewed;         241 AA.
AC   Q98987;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Neuromodulin;
DE   AltName: Full=Axonal membrane protein GAP-43;
DE   AltName: Full=Growth-associated protein 43;
DE   Flags: Fragment;
GN   Name=GAP43;
OS   Serinus canaria (Island canary) (Fringilla canaria).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Fringillidae;
OC   Carduelinae; Serinus.
OX   NCBI_TaxID=9135;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Wasserschlager;
RA   Clayton D.F., Jin H., Siepka S.M., Mello C.V., George J.M.;
RT   "Developmental regulation of GAP43 mRNA in the avian song control
RT   circuit.";
RL   Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This protein is associated with nerve growth. It is a major
CC       component of the motile 'growth cones' that form the tips of elongating
CC       axons. Plays a role in axonal and dendritic filopodia induction (By
CC       similarity). {ECO:0000250|UniProtKB:P17677}.
CC   -!- SUBUNIT: Binds calmodulin with a greater affinity in the absence of
CC       Ca(2+) than in its presence. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17677};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}; Cytoplasmic
CC       side {ECO:0000250|UniProtKB:P17677}. Cell projection, growth cone
CC       membrane {ECO:0000250|UniProtKB:P17677}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P17677}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:P17677}. Synapse {ECO:0000250|UniProtKB:P17677}.
CC       Cell projection, filopodium membrane {ECO:0000250|UniProtKB:P17677};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P17677}.
CC   -!- PTM: Palmitoylated (By similarity). Palmitoylation is essential for
CC       plasma membrane association (By similarity).
CC       {ECO:0000250|UniProtKB:P06837, ECO:0000250|UniProtKB:P17677}.
CC   -!- SIMILARITY: Belongs to the neuromodulin family. {ECO:0000305}.
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DR   EMBL; U75453; AAB18340.1; -; mRNA.
DR   AlphaFoldDB; Q98987; -.
DR   SMR; Q98987; -.
DR   Proteomes; UP000694409; Unplaced.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR001422; Neuromodulin.
DR   InterPro; IPR017454; Neuromodulin_C.
DR   InterPro; IPR018947; Neuromodulin_gap-junction_N.
DR   InterPro; IPR033137; Neuromodulin_P_site.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF06614; Neuromodulin; 1.
DR   Pfam; PF10580; Neuromodulin_N; 1.
DR   PRINTS; PR00215; NEUROMODULIN.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   PROSITE; PS00413; NEUROMODULIN_2; 1.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Cell membrane; Cell projection; Developmental protein;
KW   Differentiation; Growth regulation; Lipoprotein; Membrane; Neurogenesis;
KW   Phosphoprotein; Reference proteome; Synapse.
FT   CHAIN           <1..241
FT                   /note="Neuromodulin"
FT                   /id="PRO_0000159601"
FT   DOMAIN          25..54
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..30
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..72
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..173
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        206..241
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   241 AA;  25019 MW;  986F846E27449AE0 CRC64;
     TKQVEKNEDG DQKIEQDGIK PEDKAHKAAT KIQASFRGHI TRKKLKGEKK GDAPASETDA
     ADKKEEGPAG GAAENKESEA PAATEAAAAD SAQQEEGSKD SSAPAEEKKG DGAADTGSEQ
     PAPQAATPAA SSEEKTAAAA APERESTPKA STDNSPSLKA DEAQDKEEPK QADVPAADTT
     ATTTPAAEDA TAKATAQPQM ETVESSQTEE KTDAVEETKP TESAQQEEMK EEESKADQEN
     A