NEUM_XENLA
ID NEUM_XENLA Reviewed; 214 AA.
AC P55860; Q5D0C7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Neuromodulin;
DE AltName: Full=Axonal membrane protein GAP-43;
DE AltName: Full=Growth-associated protein 43;
GN Name=gap43;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9015344; DOI=10.1016/s0306-4522(96)00400-9;
RA Schrama L.H., Lepperdinger G., Moritz A., van den Engel N.K., Marquart A.,
RA Oestreicher A.B., Eggen B.J.L., Hage W.J., Richter K., Destree O.H.J.;
RT "B-50/growth-associated protein-43, a marker of neural development in
RT Xenopus laevis.";
RL Neuroscience 76:635-652(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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; X87582; CAA60886.1; -; mRNA.
DR EMBL; BC042240; AAH42240.1; -; mRNA.
DR RefSeq; NP_001080338.1; NM_001086869.1.
DR AlphaFoldDB; P55860; -.
DR PRIDE; P55860; -.
DR DNASU; 380030; -.
DR GeneID; 380030; -.
DR KEGG; xla:380030; -.
DR CTD; 380030; -.
DR Xenbase; XB-GENE-5899429; gap43.S.
DR OMA; GTPNKPE; -.
DR OrthoDB; 1531103at2759; -.
DR Proteomes; UP000186698; Chromosome 2S.
DR Bgee; 380030; Expressed in brain and 14 other tissues.
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 InterPro; IPR018243; Neuromodulin_palmitoyl_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; 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..214
FT /note="Neuromodulin"
FT /id="PRO_0000159603"
FT DOMAIN 32..61
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..214
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 214 AA; 23458 MW; 1EA0095F36C6CD5A CRC64;
MLCCMRRTKQ VEKNEDGDQK IDQDGNKPED KAHKAATKIQ ASFRGHIIRK KMKDDKKDDN
SEEAVENHKG EAKDEAATTE NKTPKTEEPT ADGPLEVKKE AISSPAEDKK QEPSSEKPKD
TPSEENQASA ESESTTKGST ENSPGVDASQ AKEESKKADV PEATQDAASE KEQEKAESSQ
EDVKKDEVEE IKASESAQQD EAVSEEAKPD QENA
