FGF13_MOUSE
ID FGF13_MOUSE Reviewed; 245 AA.
AC P70377; B1AU21; O35338; Q3UR31; Q8VCY9; Q9JLA5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Fibroblast growth factor 13 {ECO:0000305};
DE Short=FGF-13;
DE AltName: Full=Fibroblast growth factor homologous factor 2;
DE Short=FHF-2;
GN Name=Fgf13 {ECO:0000312|MGI:MGI:109178}; Synonyms=Fhf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Eye;
RX PubMed=8790420; DOI=10.1073/pnas.93.18.9850;
RA Smallwood P.M., Munoz-Sanjuan I., Tong P., Macke J.P., Hendry S.H.,
RA Gilbert D.J., Copeland N.G., Jenkins N.A., Nathans J.;
RT "Fibroblast growth factor (FGF) homologous factors: new members of the FGF
RT family implicated in nervous system development.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9850-9857(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=9232594; DOI=10.1016/s0925-4773(97)00042-7;
RA Hartung H., Feldman B., Lovec H., Coulier F., Birnbaum D., Goldfarb M.;
RT "Murine FGF-12 and FGF-13: expression in embryonic nervous system,
RT connective tissue and heart.";
RL Mech. Dev. 64:31-39(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 3), ALTERNATIVE SPLICING,
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=10644718; DOI=10.1074/jbc.275.4.2589;
RA Munoz-Sanjuan I., Smallwood P.M., Nathans J.;
RT "Isoform diversity among fibroblast growth factor homologous factors is
RT generated by alternative promoter usage and differential splicing.";
RL J. Biol. Chem. 275:2589-2597(2000).
RN [8]
RP FUNCTION IN MAPK SIGNALING, AND INTERACTION WITH MAPK8IP2.
RX PubMed=11378392; DOI=10.1016/s0960-9822(01)00232-9;
RA Schoorlemmer J., Goldfarb M.;
RT "Fibroblast growth factor homologous factors are intracellular signaling
RT proteins.";
RL Curr. Biol. 11:793-797(2001).
RN [9]
RP FUNCTION IN MAPK SIGNALING.
RX PubMed=12244047; DOI=10.1074/jbc.m205520200;
RA Schoorlemmer J., Goldfarb M.;
RT "Fibroblast growth factor homologous factors and the islet brain-2 scaffold
RT protein regulate activation of a stress-activated protein kinase.";
RL J. Biol. Chem. 277:49111-49119(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION IN SODIUM CHANNEL REGULATION, TISSUE SPECIFICITY, INTERACTION WITH
RP SCN5A, AND SUBCELLULAR LOCATION.
RX PubMed=21817159; DOI=10.1161/circresaha.111.247957;
RA Wang C., Hennessey J.A., Kirkton R.D., Wang C., Graham V., Puranam R.S.,
RA Rosenberg P.B., Bursac N., Pitt G.S.;
RT "Fibroblast growth factor homologous factor 13 regulates Na+ channels and
RT conduction velocity in murine hearts.";
RL Circ. Res. 109:775-782(2011).
RN [12]
RP FUNCTION IN NEURON POLARIZATION, FUNCTION IN NEURON MIGRATION, DISRUPTION
RP PHENOTYPE, SUBCELLULAR LOCATION, AND TUBULIN-BINDING.
RX PubMed=22726441; DOI=10.1016/j.cell.2012.04.046;
RA Wu Q.F., Yang L., Li S., Wang Q., Yuan X.B., Gao X., Bao L., Zhang X.;
RT "Fibroblast growth factor 13 is a microtubule-stabilizing protein
RT regulating neuronal polarization and migration.";
RL Cell 149:1549-1564(2012).
RN [13]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=30679375; DOI=10.1126/science.aau8977;
RA Favuzzi E., Deogracias R., Marques-Smith A., Maeso P., Jezequel J.,
RA Exposito-Alonso D., Balia M., Kroon T., Hinojosa A.J., Maraver E.F.,
RA Rico B.;
RT "Distinct molecular programs regulate synapse specificity in cortical
RT inhibitory circuits.";
RL Science 363:413-417(2019).
CC -!- FUNCTION: Microtubule-binding protein which directly binds tubulin and
CC is involved in both polymerization and stabilization of microtubules
CC (PubMed:22726441). Through its action on microtubules, may participate
CC to the refinement of axons by negatively regulating axonal and leading
CC processes branching (PubMed:22726441). Plays a crucial role in neuron
CC polarization and migration in the cerebral cortex and the hippocampus
CC (PubMed:22726441). Regulates voltage-gated sodium channels transport
CC and function (PubMed:21817159). May also play a role in MAPK signaling
CC (PubMed:11378392, PubMed:12244047). Required for the development of
CC axonal initial segment-targeting inhibitory GABAergic synapses made by
CC chandelier neurons (PubMed:30679375). {ECO:0000269|PubMed:11378392,
CC ECO:0000269|PubMed:12244047, ECO:0000269|PubMed:21817159,
CC ECO:0000269|PubMed:22726441, ECO:0000269|PubMed:30679375}.
CC -!- FUNCTION: [Isoform 1]: Seems not to be involved in neuroblast
CC polarization and migration but regulates axon branching.
CC {ECO:0000269|PubMed:22726441}.
CC -!- SUBUNIT: Interacts with SCN8A; regulates SCN8A activity (By
CC similarity). Interacts with SCN1A; may regulate SCN1A activity (By
CC similarity). Interacts with SCN5A; the interaction is direct and may
CC regulate SNC5A density at membranes and function (PubMed:21817159). May
CC also interact with SCN2A and SCN11A (By similarity). Interacts with
CC MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity
CC (PubMed:11378392). {ECO:0000250|UniProtKB:Q92913,
CC ECO:0000269|PubMed:11378392, ECO:0000269|PubMed:21817159}.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC {ECO:0000269|PubMed:22726441}. Cell projection, growth cone
CC {ECO:0000269|PubMed:22726441}. Cell projection, dendrite
CC {ECO:0000269|PubMed:22726441}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:21817159}. Cytoplasm {ECO:0000269|PubMed:22726441}.
CC Note=Not secreted. Localizes to the lateral membrane and intercalated
CC disks of myocytes. {ECO:0000269|PubMed:22726441}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus
CC {ECO:0000250|UniProtKB:Q92913}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q92913}. Nucleus {ECO:0000250|UniProtKB:Q92913}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:10644718}. Nucleus {ECO:0000269|PubMed:10644718}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist.;
CC Name=1; Synonyms=FGF13A, mFHF-2(1S) {ECO:0000303|PubMed:10644718},
CC FGF13-S;
CC IsoId=P70377-1; Sequence=Displayed;
CC Name=2; Synonyms=FGF13B, mFHF-2(1U) {ECO:0000303|PubMed:10644718},
CC FGF13-U;
CC IsoId=P70377-2; Sequence=VSP_044131;
CC Name=3; Synonyms=FGF13-VY, mFHF-2(1Y+1V) {ECO:0000303|PubMed:10644718};
CC IsoId=P70377-3; Sequence=VSP_044130;
CC -!- TISSUE SPECIFICITY: Detected in brain, eye and heart. In brain, the
CC different isoforms display different patterns of expression. Expressed
CC in brain and heart (at protein level). Isoform 3 is highly expressed in
CC cardiac myocytes while isoform 1 is the most abundant in brain.
CC {ECO:0000269|PubMed:10644718, ECO:0000269|PubMed:21817159,
CC ECO:0000269|PubMed:9232594}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the subplate of the embryonic cortex
CC and the axonal tracts in the intermediate zone, and in axonal tracts of
CC projection neurons, specifically in the corticothalamic tract and the
CC corpus callosum (at protein level). Isoform 2 is transiently expressed
CC in the neocortex and hippocampus from 17 dpc to P7 (at protein level).
CC In embryonic brain, present in all divisions of the central and
CC peripheral nervous system and it is at least 5 times more abundant than
CC other FHFs. Detected in the subplate, ganglionic eminences, and
CC proliferative zones of the cortical wall at 14 dpc. Detected in the
CC cortical plate of the cerebral cortex, hippocampus, and striatum from
CC 17 dpc to P14. Expression is markedly reduced in adult brain where it
CC is most abundant in hippocampus. Also detected in developing kidney.
CC Expressed in developing chandelier neurons.
CC {ECO:0000269|PubMed:30679375, ECO:0000269|PubMed:9232594}.
CC -!- PTM: May be phosphorylated. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Conditional knockout mice lacking fgf13 in the
CC cerebral cortex or mice lacking fgf13 in most tissues display similar
CC phenotypes of impaired spatial acquisition and memory. The cued memory
CC and the capacity of novel object recognition are altered. They also
CC display anxiety-related and reduced depression-like behaviors. This is
CC associated with a disorganization of cortical structure and neural
CC circuits. The laminar formation of the neocortex is delayed and the
CC hippocampal development is also affected.
CC {ECO:0000269|PubMed:22726441}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; U66202; AAB18918.1; -; mRNA.
DR EMBL; AF020737; AAB71606.1; -; mRNA.
DR EMBL; AK141848; BAE24857.1; -; mRNA.
DR EMBL; AL669891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL672247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL713968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466583; EDL42180.1; -; Genomic_DNA.
DR EMBL; CH466583; EDL42182.1; -; Genomic_DNA.
DR EMBL; BC018238; AAH18238.1; -; mRNA.
DR EMBL; AF199608; AAF31395.1; -; mRNA.
DR CCDS; CCDS30157.1; -. [P70377-1]
DR CCDS; CCDS72383.1; -. [P70377-2]
DR RefSeq; NP_001277344.1; NM_001290415.1. [P70377-2]
DR RefSeq; NP_034330.2; NM_010200.3. [P70377-1]
DR AlphaFoldDB; P70377; -.
DR SMR; P70377; -.
DR BioGRID; 199642; 2.
DR STRING; 10090.ENSMUSP00000033473; -.
DR iPTMnet; P70377; -.
DR PhosphoSitePlus; P70377; -.
DR EPD; P70377; -.
DR PaxDb; P70377; -.
DR PeptideAtlas; P70377; -.
DR PRIDE; P70377; -.
DR ProteomicsDB; 271569; -. [P70377-1]
DR ProteomicsDB; 271570; -. [P70377-2]
DR ProteomicsDB; 271571; -. [P70377-3]
DR TopDownProteomics; P70377-2; -. [P70377-2]
DR ABCD; P70377; 2 sequenced antibodies.
DR DNASU; 14168; -.
DR Ensembl; ENSMUST00000033473; ENSMUSP00000033473; ENSMUSG00000031137. [P70377-1]
DR Ensembl; ENSMUST00000119306; ENSMUSP00000113206; ENSMUSG00000031137. [P70377-2]
DR GeneID; 14168; -.
DR KEGG; mmu:14168; -.
DR UCSC; uc009tht.3; mouse. [P70377-1]
DR UCSC; uc009thu.3; mouse. [P70377-2]
DR UCSC; uc009thv.2; mouse. [P70377-3]
DR CTD; 2258; -.
DR MGI; MGI:109178; Fgf13.
DR VEuPathDB; HostDB:ENSMUSG00000031137; -.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000162313; -.
DR InParanoid; P70377; -.
DR OMA; LYPSEHF; -.
DR OrthoDB; 1192273at2759; -.
DR PhylomeDB; P70377; -.
DR TreeFam; TF317805; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 14168; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Fgf13; mouse.
DR PRO; PR:P70377; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P70377; protein.
DR Bgee; ENSMUSG00000031137; Expressed in ventral tegmental area and 247 other tissues.
DR ExpressionAtlas; P70377; baseline and differential.
DR Genevisible; P70377; MM.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; IDA:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:BHF-UCL.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:MGI.
DR GO; GO:0017080; F:sodium channel regulator activity; IMP:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0021795; P:cerebral cortex cell migration; IMP:UniProtKB.
DR GO; GO:0045200; P:establishment of neuroblast polarity; IMP:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IMP:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; IMP:UniProtKB.
DR GO; GO:0007612; P:learning; IMP:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:MGI.
DR GO; GO:0007613; P:memory; IMP:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IMP:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; IMP:UniProtKB.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IMP:BHF-UCL.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IMP:BHF-UCL.
DR CDD; cd00058; FGF; 1.
DR InterPro; IPR028279; FGF13.
DR InterPro; IPR002209; Fibroblast_GF_fam.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR11486; PTHR11486; 1.
DR PANTHER; PTHR11486:SF145; PTHR11486:SF145; 1.
DR Pfam; PF00167; FGF; 1.
DR PRINTS; PR00263; HBGFFGF.
DR SMART; SM00442; FGF; 1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00247; HBGF_FGF; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasm; Membrane;
KW Microtubule; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..245
FT /note="Fibroblast growth factor 13"
FT /id="PRO_0000147608"
FT REGION 1..62
FT /note="Mediates targeting to the nucleus"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..201
FT /note="Mediates interaction with sodium channels"
FT /evidence="ECO:0000250"
FT REGION 157..164
FT /note="Tubulin-binding domain necessary and sufficient for
FT tubulin-binding"
FT REGION 213..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..63
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRPE -> MSGKVTKPKEEKDASKVLDDAPPGTQEYIMLRQDSIQSAELKKK
FT ESPFRAKCHEIFCCPPKQVHHKENTEPEE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10644718"
FT /id="VSP_044130"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MALLRKSYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_044131"
FT CONFLICT 2
FT /note="A -> T (in Ref. 1; AAB18918)"
FT /evidence="ECO:0000305"
FT CONFLICT 2
FT /note="Missing (in Ref. 2; AAB71606)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="L -> Q (in Ref. 2; AAB71606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 245 AA; 27588 MW; 5B96D41AC3A3DF78 CRC64;
MAAAIASSLI RQKRQARERE KSNACKCVSS PSKGKTSCDK NKLNVFSRVK LFGSKKRRRR
RPEPQLKGIV TKLYSRQGYH LQLQADGTID GTKDEDSTYT LFNLIPVGLR VVAIQGVQTK
LYLAMNSEGY LYTSEHFTPE CKFKESVFEN YYVTYSSMIY RQQQSGRGWY LGLNKEGEIM
KGNHVKKNKP AAHFLPKPLK VAMYKEPSLH DLTEFSRSGS GTPTKSRSVS GVLNGGKSMS
HNEST
