ID NEUM_MOUSE Reviewed; 227 AA. AC P06837; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 16-SEP-2015, entry version 144. DE RecName: Full=Neuromodulin; DE AltName: Full=Axonal membrane protein GAP-43; DE AltName: Full=Calmodulin-binding protein P-57; DE AltName: Full=Growth-associated protein 43; GN Name=Gap43; Synonyms=Basp2; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2442159; RA Cimler B.M., Giebelhaus D.H., Wakim B.T., Storm D.R., Moon R.T.; RT "Characterization of murine cDNAs encoding P-57, a neural-specific RT calmodulin-binding protein."; RL J. Biol. Chem. 262:12158-12163(1987). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Retina; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PROTEIN SEQUENCE OF 84-104, AND IDENTIFICATION BY MASS SPECTROMETRY. RC STRAIN=OF1; TISSUE=Hippocampus; RA Lubec G., Sunyer B., Chen W.-Q.; RL Submitted (JAN-2009) to UniProtKB. RN [4] RP IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; SRC; FGFR4 RP AND CTTN. RX PubMed=11433297; DOI=10.1038/35083041; RA Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.; RT "N-CAM modulates tumour-cell adhesion to matrix by inducing FGF- RT receptor signalling."; RL Nat. Cell Biol. 3:650-657(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic brain; RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., RA Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86; SER-96; THR-138; RP SER-142; SER-144; SER-145 AND THR-172, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, and Lung; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: This protein is associated with nerve growth. It is a CC major component of the motile "growth cones" that form the tips of CC elongating axons. Plays a role in axonal and dendritic filopodia CC induction. CC -!- SUBUNIT: Binds calmodulin with a greater affinity in the absence CC of Ca(2+) than in its presence (By similarity). Identified in a CC complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, CC GAP43 and CTTN. {ECO:0000250, ECO:0000269|PubMed:11433297}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cell projection, growth cone membrane; CC Peripheral membrane protein; Cytoplasmic side. Cell junction, CC synapse. Cell projection, filopodium membrane {ECO:0000250}; CC Peripheral membrane protein {ECO:0000250}. Note=Cytoplasmic CC surface of growth cone and synaptic plasma membranes. CC -!- PTM: Palmitoylation by ARF6 is essential for plasma membrane CC association and axonal and dendritic filopodia induction. CC Deacylated by LYPLA2 (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated at Ser-41 by PHK. Phosphorylation of this CC protein by a protein kinase C is specifically correlated with CC certain forms of synaptic plasticity. CC -!- SIMILARITY: Belongs to the neuromodulin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 IQ domain. {ECO:0000255|PROSITE- CC ProRule:PRU00116}. 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; J02809; AAA37377.1; -; mRNA. DR EMBL; BC028288; AAH28288.1; -; mRNA. DR EMBL; BC080758; AAH80758.1; -; mRNA. DR CCDS; CCDS28177.1; -. DR PIR; A29800; A29800. DR RefSeq; NP_032109.1; NM_008083.2. DR UniGene; Mm.1222; -. DR PDB; 4E53; X-ray; 2.69 A; A/B=34-57. DR PDBsum; 4E53; -. DR ProteinModelPortal; P06837; -. DR BioGrid; 199828; 1. DR IntAct; P06837; 5. DR MINT; MINT-4103374; -. DR STRING; 10090.ENSMUSP00000099881; -. DR PhosphoSite; P06837; -. DR MaxQB; P06837; -. DR PaxDb; P06837; -. DR PRIDE; P06837; -. DR Ensembl; ENSMUST00000102817; ENSMUSP00000099881; ENSMUSG00000047261. DR GeneID; 14432; -. DR KEGG; mmu:14432; -. DR UCSC; uc007zfv.1; mouse. DR CTD; 2596; -. DR MGI; MGI:95639; Gap43. DR eggNOG; NOG120480; -. DR GeneTree; ENSGT00730000111265; -. DR HOGENOM; HOG000013014; -. DR HOVERGEN; HBG006468; -. DR InParanoid; P06837; -. DR OMA; PEADQEH; -. DR OrthoDB; EOG744TBB; -. DR PhylomeDB; P06837; -. DR TreeFam; TF333213; -. DR ChiTaRS; Gap43; mouse. DR NextBio; 286053; -. DR PRO; PR:P06837; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; P06837; -. DR CleanEx; MM_GAP43; -. DR Genevisible; P06837; MM. DR GO; GO:0030424; C:axon; IDA:MGI. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0071944; C:cell periphery; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0031527; C:filopodium membrane; ISO:MGI. DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097481; C:neuronal postsynaptic density; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0014069; C:postsynaptic density; IDA:MGI. DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central. DR GO; GO:0035727; F:lysophosphatidic acid binding; IEA:Ensembl. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IEA:Ensembl. DR GO; GO:0001786; F:phosphatidylserine binding; IEA:Ensembl. DR GO; GO:0016198; P:axon choice point recognition; IMP:MGI. DR GO; GO:0007411; P:axon guidance; IMP:MGI. DR GO; GO:0045165; P:cell fate commitment; IMP:MGI. DR GO; GO:0010001; P:glial cell differentiation; IMP:MGI. DR GO; GO:0051489; P:regulation of filopodium assembly; ISO:MGI. DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW. DR GO; GO:0042246; P:tissue regeneration; IEA:Ensembl. 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; IPR018243; Neuromodulin_palmitoyl/P_site. DR PANTHER; PTHR10699:SF15; PTHR10699:SF15; 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; PS00412; NEUROMODULIN_1; 1. DR PROSITE; PS00413; NEUROMODULIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Calmodulin-binding; Cell junction; Cell membrane; KW Cell projection; Complete proteome; Developmental protein; KW Differentiation; Direct protein sequencing; Growth regulation; KW Lipoprotein; Membrane; Neurogenesis; Palmitate; Phosphoprotein; KW Reference proteome; Synapse. FT CHAIN 1 227 Neuromodulin. FT /FTId=PRO_0000159597. FT DOMAIN 31 60 IQ. {ECO:0000255|PROSITE- FT ProRule:PRU00116}. FT REGION 1 4 Important for membrane binding. FT MOD_RES 41 41 Phosphoserine; by PHK. {ECO:0000305}. FT MOD_RES 86 86 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 96 96 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 138 138 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 142 142 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 144 144 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 145 145 Phosphoserine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 172 172 Phosphothreonine. FT {ECO:0000244|PubMed:21183079}. FT MOD_RES 192 192 Phosphoserine; by CK2. {ECO:0000250}. FT MOD_RES 193 193 Phosphoserine; by CK2. {ECO:0000250}. FT LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}. FT LIPID 4 4 S-palmitoyl cysteine. {ECO:0000250}. FT HELIX 35 51 {ECO:0000244|PDB:4E53}. SQ SEQUENCE 227 AA; 23632 MW; 14803B2F8F0649F7 CRC64; MLCCMRRTKQ VEKNDEDQKI EQDGVKPEDK AHKAATKIQA SFRGHITRKK LKGEKKGDAP AAEAEAKEKD DAPVADGVEK KEGDGSATTD AAPATSPKAE EPSKAGDAPS EEKKGEGDAA PSEEKAGSAE TESAAKATTD NSPSSKAEDG PAKEEPKQAD VPAAVTDAAA TTPAAEDAAT KAAQPPTETA ESSQAEEEKD AVDEAKPKES ARQDEGKEDP EADQEHA //