NEUM_HUMAN
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 03-AUG-2022, entry version 209.
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";
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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. [P17677-2]
DR AlphaFoldDB; P17677; -.
DR SMR; P17677; -.
DR BioGRID; 108867; 33.
DR DIP; DIP-452N; -.
DR IntAct; P17677; 21.
DR STRING; 9606.ENSP00000377372; -.
DR TCDB; 1.A.71.2.1; the brain acid-soluble protein channel (basp1 channel) family.
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; P17677; -.
DR PeptideAtlas; P17677; -.
DR PRIDE; P17677; -.
DR ProteomicsDB; 53504; -. [P17677-1]
DR ProteomicsDB; 53505; -. [P17677-2]
DR Antibodypedia; 2805; 873 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 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; GTPNKPE; -.
DR OrthoDB; 1531103at2759; -.
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; 12 hits in 1074 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 153 other tissues.
DR ExpressionAtlas; P17677; baseline and differential.
DR Genevisible; P17677; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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: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:UniProtKB-KW.
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 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 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
