ID U3JU27_FICAL Unreviewed; 381 AA.
AC U3JU27;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 2.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Neuromodulin {ECO:0000256|ARBA:ARBA00021591, ECO:0000256|RuleBase:RU368113};
DE AltName: Full=Axonal membrane protein GAP-43 {ECO:0000256|ARBA:ARBA00030597, ECO:0000256|RuleBase:RU368113};
DE AltName: Full=Growth-associated protein 43 {ECO:0000256|ARBA:ARBA00033250, ECO:0000256|RuleBase:RU368113};
GN Name=GAP43 {ECO:0000313|Ensembl:ENSFALP00000006281.2};
OS Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000006281.2, ECO:0000313|Proteomes:UP000016665};
RN [1] {ECO:0000313|Ensembl:ENSFALP00000006281.2, ECO:0000313|Proteomes:UP000016665}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23103876; DOI=10.1038/nature11584;
RA Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA Wolf J.B.;
RT "The genomic landscape of species divergence in Ficedula flycatchers.";
RL Nature 491:756-760(2012).
RN [2] {ECO:0000313|Ensembl:ENSFALP00000006281.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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.
CC {ECO:0000256|ARBA:ARBA00025215, ECO:0000256|RuleBase:RU368113}.
CC -!- SUBUNIT: Binds calmodulin with a greater affinity in the absence of
CC Ca(2+) than in its presence. {ECO:0000256|RuleBase:RU368113}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU368113};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU368113};
CC Cytoplasmic side {ECO:0000256|RuleBase:RU368113}. Cell projection,
CC growth cone membrane {ECO:0000256|ARBA:ARBA00004503,
CC ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004503, ECO:0000256|RuleBase:RU368113};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004503,
CC ECO:0000256|RuleBase:RU368113}. Synapse {ECO:0000256|ARBA:ARBA00034103,
CC ECO:0000256|RuleBase:RU368113}. Cell projection, filopodium membrane
CC {ECO:0000256|RuleBase:RU368113}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU368113}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- PTM: Palmitoylated. Palmitoylation is essential for plasma membrane
CC association. {ECO:0000256|RuleBase:RU368113}.
CC -!- SIMILARITY: Belongs to the neuromodulin family.
CC {ECO:0000256|ARBA:ARBA00005890, ECO:0000256|RuleBase:RU368113}.
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DR AlphaFoldDB; U3JU27; -.
DR STRING; 59894.ENSFALP00000006281; -.
DR Ensembl; ENSFALT00000006310.2; ENSFALP00000006281.2; ENSFALG00000006031.2.
DR eggNOG; ENOG502RXWF; Eukaryota.
DR GeneTree; ENSGT00730000111265; -.
DR HOGENOM; CLU_102989_0_0_1; -.
DR OrthoDB; 4371674at2759; -.
DR Proteomes; UP000016665; Chromosome 1.
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-UniRule.
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-UniRule.
DR Gene3D; 1.20.5.190; -; 1.
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 PANTHER; PTHR10699; NEUROMODULIN; 1.
DR PANTHER; PTHR10699:SF15; NEUROMODULIN; 1.
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 3: Inferred from homology;
KW Calmodulin-binding {ECO:0000256|ARBA:ARBA00022860,
KW ECO:0000256|RuleBase:RU368113};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU368113};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273,
KW ECO:0000256|RuleBase:RU368113};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473,
KW ECO:0000256|RuleBase:RU368113};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782,
KW ECO:0000256|RuleBase:RU368113};
KW Growth regulation {ECO:0000256|ARBA:ARBA00022604,
KW ECO:0000256|RuleBase:RU368113};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288, ECO:0000256|RuleBase:RU368113};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902,
KW ECO:0000256|RuleBase:RU368113}; Palmitate {ECO:0000256|RuleBase:RU368113};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU368113};
KW Reference proteome {ECO:0000313|Proteomes:UP000016665};
KW Signal {ECO:0000256|SAM:SignalP};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU368113}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..381
FT /note="Neuromodulin"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5032461671"
FT DOMAIN 136..166
FT /note="Neuromodulin gap junction N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10580"
FT DOMAIN 203..381
FT /note="Neuromodulin (GAP-43) C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06614"
FT REGION 34..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 37798 MW; 26DF89E3C3AFD4B2 CRC64;
MCLFLCLCVS ANCPGVCARV LVCVCVCERE REGEREGGRE GGSGEGGGGG GGGGGGGGGG
GGGGGGGGGG GGGGGGGGGG GGGGGGGGGG GGGGGGGGGG REGVERVGGR DKREKRKRRE
EKEGRRRKEG DNTIMLCCMR RTKQVEKNED GDQKIEQDGI KPEDKAHKAA TKIQASFRGH
ITRKKLKGEK KGDAPASETD ATDKKEEGPA GGAAENKESE APAATEAAAD SAQQQEGSKD
SSAPAEEKKG DGAGETGSEQ PAPQAAAPAA SSEEKPAAAA APERESATKA STDNSPSLKA
DEAQDKEEPK QADVPAADTT ATATPAAEDA TAKATAQPQM ETVESSQTEE KTDAVEETKP
TESAQQEEVK EEESKADQEN A
//
