ID NEUM_HUMAN Reviewed; 238 AA. AC P17677; A8K0Y4; DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1990, sequence version 1. DT 24-JAN-2024, entry version 217. DE RecName: Full=Neuromodulin; DE AltName: Full=Axonal membrane protein GAP-43; DE AltName: Full=Growth-associated protein 43; DE AltName: Full=Neural phosphoprotein B-50; DE AltName: Full=pp46; GN Name=GAP43; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3272162; DOI=10.1016/0896-6273(88)90196-1; RA Kosik K.S., Orecchio L.D., Bruns G.A.P., Benowitz L.I., McDonald G.P., RA Cox D.R., Neve R.; RT "Human GAP-43: its deduced amino acid sequence and chromosomal localization RT in mouse and human."; RL Neuron 1:127-132(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3272163; DOI=10.1016/0896-6273(88)90197-3; RA Ng S.-C., de la Monte S.M., Conboy G.L., Karns L.R., Fishman M.C.; RT "Cloning of human GAP-43: growth association and ischemic resurgence."; RL Neuron 1:133-139(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8231732; DOI=10.1016/0169-328x(93)90128-c; RA Nielander H.B., de Groen P.C., Eggen B.J., Schrama L.H., Gispen W.H., RA Schotman P.; RT "Structure of the human gene for the neural phosphoprotein B-50 (GAP-43)."; RL Brain Res. Mol. Brain Res. 19:293-302(1993). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain cortex, and Subthalamic nucleus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, PALMITOYLATION, AND MUTAGENESIS OF RP 3-CYS-CYS-4. RX PubMed=14978216; DOI=10.1091/mbc.e03-07-0493; RA Gauthier-Campbell C., Bredt D.S., Murphy T.H., El-Husseini A.; RT "Regulation of dendritic branching and filopodia formation in hippocampal RT neurons by specific acylated protein motifs."; RL Mol. Biol. Cell 15:2205-2217(2004). RN [9] RP DEACYLATION BY LYPLA2. RX PubMed=21152083; DOI=10.1371/journal.pone.0015045; RA Tomatis V.M., Trenchi A., Gomez G.A., Daniotti J.L.; RT "Acyl-protein thioesterase 2 catalyzes the deacylation of peripheral RT membrane-associated GAP-43."; RL PLoS ONE 5:E15045-E15045(2010). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP VARIANT ILE-59. RX PubMed=10391209; DOI=10.1038/10290; RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RT "Characterization of single-nucleotide polymorphisms in coding regions of RT human genes."; RL Nat. Genet. 22:231-238(1999). RN [12] RP ERRATUM OF PUBMED:10391209. RA Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., RA Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., RA Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., RA Lander E.S.; RL Nat. Genet. 23:373-373(1999). 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:0000269|PubMed:14978216, ECO:0000269|PubMed:21152083}. CC -!- SUBUNIT: Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, CC FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts (via IQ CC domain) with calmodulin (By similarity). Binds calmodulin with a CC greater affinity in the absence of Ca(2+) than in its presence (By CC similarity). {ECO:0000250|UniProtKB:P06836, CC ECO:0000250|UniProtKB:P06837}. CC -!- INTERACTION: CC P17677; P05067-8: APP; NbExp=3; IntAct=EBI-1267511, EBI-302661; CC P17677; P21917: DRD4; NbExp=3; IntAct=EBI-1267511, EBI-8592297; CC P17677; Q05655: PRKCD; NbExp=4; IntAct=EBI-1267511, EBI-704279; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14978216}; CC Peripheral membrane protein {ECO:0000269|PubMed:14978216}; Cytoplasmic CC side {ECO:0000269|PubMed:14978216}. Cell projection, growth cone CC membrane {ECO:0000269|PubMed:14978216}; Peripheral membrane protein CC {ECO:0000269|PubMed:14978216}; Cytoplasmic side CC {ECO:0000269|PubMed:14978216}. Synapse {ECO:0000269|PubMed:14978216}. CC Cell projection, filopodium membrane {ECO:0000269|PubMed:14978216}; CC Peripheral membrane protein {ECO:0000269|PubMed:14978216}. Perikaryon CC {ECO:0000250|UniProtKB:P07936}. Cell projection, dendrite CC {ECO:0000250|UniProtKB:P07936}. Cell projection, axon CC {ECO:0000250|UniProtKB:P07936}. Cytoplasm CC {ECO:0000250|UniProtKB:P07936}. Note=Cytoplasmic surface of growth cone CC and synaptic plasma membranes. {ECO:0000269|PubMed:14978216}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P17677-1; Sequence=Displayed; CC Name=2; CC IsoId=P17677-2; Sequence=VSP_042783; CC -!- PTM: Phosphorylated (By similarity). Phosphorylation of this protein by CC a protein kinase C is specifically correlated with certain forms of CC synaptic plasticity (By similarity). {ECO:0000250|UniProtKB:P07936}. CC -!- PTM: Palmitoylated by ZDHHC3 (By similarity). Palmitoylation is CC regulated by ARF6 and is essential for plasma membrane association and CC axonal and dendritic filopodia induction (PubMed:14978216). Deacylated CC by LYPLA2 (PubMed:21152083). {ECO:0000250|UniProtKB:P06837, CC ECO:0000269|PubMed:14978216, ECO:0000269|PubMed:21152083}. CC -!- SIMILARITY: Belongs to the neuromodulin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/gap43/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Gap-43 entry; CC URL="https://en.wikipedia.org/wiki/Gap-43_protein"; 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; M25667; AAA52516.1; -; mRNA. DR EMBL; S66541; AAB28649.1; -; Genomic_DNA. DR EMBL; S66533; AAB28649.1; JOINED; Genomic_DNA. DR EMBL; S66534; AAB28649.1; JOINED; Genomic_DNA. DR EMBL; AY842481; AAV88094.1; -; Genomic_DNA. DR EMBL; AK289699; BAF82388.1; -; mRNA. DR EMBL; AK290100; BAF82789.1; -; mRNA. DR EMBL; AC012598; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092468; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC119795; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC007936; AAH07936.1; -; mRNA. DR CCDS; CCDS33830.1; -. [P17677-1] DR CCDS; CCDS46890.1; -. [P17677-2] DR PIR; I52638; I52638. DR RefSeq; NP_001123536.1; NM_001130064.1. [P17677-2] DR RefSeq; NP_002036.1; NM_002045.3. [P17677-1] DR RefSeq; XP_016861617.1; XM_017006128.1. DR AlphaFoldDB; P17677; -. DR SMR; P17677; -. DR BioGRID; 108867; 35. DR DIP; DIP-452N; -. DR IntAct; P17677; 22. DR STRING; 9606.ENSP00000377372; -. DR TCDB; 1.A.71.2.1; the brain acid-soluble protein channel (basp1 channel) family. DR GlyCosmos; P17677; 1 site, 1 glycan. DR GlyGen; P17677; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P17677; -. DR PhosphoSitePlus; P17677; -. DR SwissPalm; P17677; -. DR BioMuta; GAP43; -. DR EPD; P17677; -. DR jPOST; P17677; -. DR MassIVE; P17677; -. DR MaxQB; P17677; -. DR PaxDb; 9606-ENSP00000377372; -. DR PeptideAtlas; P17677; -. DR ProteomicsDB; 53504; -. [P17677-1] DR ProteomicsDB; 53505; -. [P17677-2] DR Pumba; P17677; -. DR Antibodypedia; 2805; 1009 antibodies from 43 providers. DR DNASU; 2596; -. DR Ensembl; ENST00000305124.11; ENSP00000305010.7; ENSG00000172020.13. [P17677-1] DR Ensembl; ENST00000393780.3; ENSP00000377372.3; ENSG00000172020.13. [P17677-2] DR GeneID; 2596; -. DR KEGG; hsa:2596; -. DR MANE-Select; ENST00000305124.11; ENSP00000305010.7; NM_002045.4; NP_002036.1. DR UCSC; uc003ebr.3; human. [P17677-1] DR AGR; HGNC:4140; -. DR CTD; 2596; -. DR DisGeNET; 2596; -. DR GeneCards; GAP43; -. DR HGNC; HGNC:4140; GAP43. DR HPA; ENSG00000172020; Tissue enriched (brain). DR MIM; 162060; gene. DR neXtProt; NX_P17677; -. DR OpenTargets; ENSG00000172020; -. DR PharmGKB; PA28553; -. DR VEuPathDB; HostDB:ENSG00000172020; -. DR eggNOG; ENOG502RXWF; Eukaryota. DR GeneTree; ENSGT00730000111265; -. DR HOGENOM; CLU_102989_0_0_1; -. DR InParanoid; P17677; -. DR OMA; PNQTNDK; -. DR OrthoDB; 4371674at2759; -. DR PhylomeDB; P17677; -. DR TreeFam; TF333213; -. DR PathwayCommons; P17677; -. DR Reactome; R-HSA-373760; L1CAM interactions. DR SignaLink; P17677; -. DR SIGNOR; P17677; -. DR BioGRID-ORCS; 2596; 14 hits in 1154 CRISPR screens. DR ChiTaRS; GAP43; human. DR GeneWiki; Gap-43_protein; -. DR GenomeRNAi; 2596; -. DR Pharos; P17677; Tbio. DR PRO; PR:P17677; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P17677; Protein. DR Bgee; ENSG00000172020; Expressed in Brodmann (1909) area 10 and 154 other cell types or tissues. DR ExpressionAtlas; P17677; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell. DR GO; GO:0031527; C:filopodium membrane; IDA:UniProtKB. DR GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl. DR GO; GO:0032584; C:growth cone membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:LIFEdb. DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central. DR GO; GO:0098793; C:presynapse; IEA:Ensembl. DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central. DR GO; GO:0035727; F:lysophosphatidic acid binding; IBA:GO_Central. DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IBA:GO_Central. DR GO; GO:0001786; F:phosphatidylserine binding; IBA:GO_Central. DR GO; GO:0048708; P:astrocyte differentiation; IEA:Ensembl. DR GO; GO:0016198; P:axon choice point recognition; IBA:GO_Central. DR GO; GO:0031103; P:axon regeneration; IBA:GO_Central. DR GO; GO:0045165; P:cell fate commitment; IEA:Ensembl. DR GO; GO:0007205; P:protein kinase C-activating G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0060019; P:radial glial cell differentiation; IEA:Ensembl. DR GO; GO:0051489; P:regulation of filopodium assembly; IDA:UniProtKB. DR GO; GO:0040008; P:regulation of growth; IEA:InterPro. DR GO; GO:0099150; P:regulation of postsynaptic specialization assembly; IEA:Ensembl. DR GO; GO:0009611; P:response to wounding; TAS:ProtInc. DR GO; GO:0042246; P:tissue regeneration; IBA:GO_Central. DR DisProt; DP00951; -. 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 InterPro; IPR018243; Neuromodulin_palmitoyl_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; PS00412; NEUROMODULIN_1; 1. DR PROSITE; PS00413; NEUROMODULIN_2; 1. DR Genevisible; P17677; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calmodulin-binding; Cell membrane; Cell projection; KW Cytoplasm; Developmental protein; Differentiation; Growth regulation; KW Lipoprotein; Membrane; Neurogenesis; Palmitate; Phosphoprotein; KW Reference proteome; Synapse. FT CHAIN 1..238 FT /note="Neuromodulin" FT /id="PRO_0000159596" FT DOMAIN 31..60 FT /note="IQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116" FT REGION 1..238 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 8..36 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 51..78 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..118 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 133..155 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 209..238 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 41 FT /note="Phosphoserine; by PHK and PKC" FT /evidence="ECO:0000250|UniProtKB:P06836" FT MOD_RES 151 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06837" FT MOD_RES 153 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06837" FT MOD_RES 154 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P06837" FT MOD_RES 181 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P06837" FT MOD_RES 202 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:P06836" FT MOD_RES 203 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000250|UniProtKB:P06836" FT LIPID 3 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P06836" FT LIPID 4 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:P06836" FT VAR_SEQ 1..10 FT /note="MLCCMRRTKQ -> MTKSCSELCHPALHFLPCLGGLRKNLQRAVRPSPYSLG FT FLTFWISR (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_042783" FT VARIANT 59 FT /note="V -> I (in dbSNP:rs6291)" FT /evidence="ECO:0000269|PubMed:10391209" FT /id="VAR_014172" FT VARIANT 162 FT /note="K -> E (in dbSNP:rs11557762)" FT /id="VAR_050271" FT MUTAGEN 3..4 FT /note="CC->SS: Inhibits axonal and dendritic filopodia FT formation and reduces dendritic and axonal branching." FT /evidence="ECO:0000269|PubMed:14978216" SQ SEQUENCE 238 AA; 24803 MW; B3536D012A127CC8 CRC64; MLCCMRRTKQ VEKNDDDQKI EQDGIKPEDK AHKAATKIQA SFRGHITRKK LKGEKKDDVQ AAEAEANKKD EAPVADGVEK KGEGTTTAEA APATGSKPDE PGKAGETPSE EKKGEGDAAT EQAAPQAPAS SEEKAGSAET ESATKASTDN SPSSKAEDAP AKEEPKQADV PAAVTAAAAT TPAAEDAAAK ATAQPPTETG ESSQAEENIE AVDETKPKES ARQDEGKEEE PEADQEHA //