ID A0A3P9NKW6_POERE Unreviewed; 237 AA.
AC A0A3P9NKW6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 27.
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};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000010231.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000010231.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000010231.1};
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 RefSeq; XP_008424284.1; XM_008426062.2.
DR AlphaFoldDB; A0A3P9NKW6; -.
DR STRING; 8081.ENSPREP00000010231; -.
DR Ensembl; ENSPRET00000010348.1; ENSPREP00000010231.1; ENSPREG00000006981.1.
DR GeneID; 103474818; -.
DR KEGG; pret:103474818; -.
DR CTD; 2596; -.
DR GeneTree; ENSGT00730000111265; -.
DR OMA; PNQTNDK; -.
DR OrthoDB; 4371674at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000006981; Expressed in head.
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; IPR018947; Neuromodulin_gap-junction_N.
DR InterPro; IPR033137; Neuromodulin_P_site.
DR InterPro; IPR018243; Neuromodulin_palmitoyl_site.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF10580; Neuromodulin_N; 1.
DR PRINTS; PR00215; NEUROMODULIN.
DR SMART; SM00015; IQ; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00412; NEUROMODULIN_1; 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};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139, ECO:0000256|RuleBase:RU368113};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553,
KW ECO:0000256|RuleBase:RU368113};
KW Reference proteome {ECO:0000313|Proteomes:UP000242638};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU368113}.
FT DOMAIN 2..34
FT /note="Neuromodulin gap junction N-terminal"
FT /evidence="ECO:0000259|Pfam:PF10580"
FT REGION 1..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..107
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..190
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 25168 MW; 170DD0BA7147FFAD CRC64;
MLCCIRRTKP VEKNEDADQK IEQDGTPNKP EDKAHKAATK IQASFRGHIT RKKMKDGEEE
KDGDSPAAEE AANGEETKKA EGEEAPAKQE ETTGEEAKKE GEETNQAKTP GADKPANSPA
GTATSPVAAA PAAASPTAAT APSEPQKEEP KAEEKPKEVE ATAKSPTTAT AEEKKEEKSE
EKKEEARKAD VPAAVSPTAE KEEPNQTNDK KDAAEESKAE ENAHPDGAAE TSEAKED
//
