NEUM_CARAU
ID NEUM_CARAU Reviewed; 213 AA.
AC P17691;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Neuromodulin;
DE AltName: Full=Axonal membrane protein GAP-43;
DE AltName: Full=Growth-associated protein 43;
GN Name=gap43;
OS Carassius auratus (Goldfish).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Carassius.
OX NCBI_TaxID=7957;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2641999; DOI=10.1016/0896-6273(89)90254-7;
RA Labate M.E., Skene J.H.P.;
RT "Selective conservation of GAP-43 structure in vertebrate evolution.";
RL Neuron 3:299-310(1989).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M26250; AAA03010.1; -; mRNA.
DR PIR; JQ0075; JQ0075.
DR AlphaFoldDB; P17691; -.
DR Proteomes; UP000515129; Genome assembly.
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; 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 2: Evidence at transcript level;
KW Calmodulin-binding; Cell membrane; Cell projection; Developmental protein;
KW Differentiation; Growth regulation; Lipoprotein; Membrane; Neurogenesis;
KW Palmitate; Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..213
FT /note="Neuromodulin"
FT /id="PRO_0000159602"
FT DOMAIN 32..61
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..173
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 3
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P06837"
SQ SEQUENCE 213 AA; 23569 MW; 31078ACB7B1682EC CRC64;
MLCCIRRTKP VEKNEEADQE IKQDGTKPEE NAHKAATKIQ ASFRGHITRK KMKDEDKDGE
NDTAPDESAE TEEKEERVSP SEEKPVEVST ETAEESKPAE QPNSPAAEAP PTAATDSAPS
DTPTKEEAQE QLQDAEEPKE TENTAAADDI TTQKEEEKEE EEEEEEEEEE AKRADVPDDT
PAATESQETD QTDKKEALDD SKPAEEAGKD QNV
