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 24-JAN-2024, entry version 154. 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 channel transport and CC 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}. 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; 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; 10090-ENSMUSP00000033473; -. DR PeptideAtlas; 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; ENSMUST00000033473.12; ENSMUSP00000033473.6; ENSMUSG00000031137.18. [P70377-1] DR Ensembl; ENSMUST00000119306.2; ENSMUSP00000113206.2; ENSMUSG00000031137.18. [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 AGR; MGI:109178; -. DR CTD; 2258; -. DR MGI; MGI:109178; Fgf13. DR VEuPathDB; HostDB:ENSMUSG00000031137; -. DR eggNOG; KOG3885; Eukaryota. DR GeneTree; ENSGT00940000162313; -. DR InParanoid; P70377; -. DR OMA; GTCEKNK; -. DR OrthoDB; 5348469at2759; -. DR PhylomeDB; P70377; -. DR TreeFam; TF317805; -. DR BioGRID-ORCS; 14168; 1 hit in 79 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 249 other cell types or tissues. DR ExpressionAtlas; P70377; baseline and differential. 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: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:0048755; P:branching morphogenesis of a nerve; IMP:MGI. 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:0007611; P:learning or memory; IMP:MGI. 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:1905152; P:positive regulation of voltage-gated sodium channel activity; ISS: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:0006814; P:sodium ion transport; IMP:BHF-UCL. DR CDD; cd00058; FGF; 1. DR Gene3D; 2.80.10.50; -; 1. DR InterPro; IPR002209; Fibroblast_GF_fam. DR InterPro; IPR008996; IL1/FGF. DR PANTHER; PTHR11486; FIBROBLAST GROWTH FACTOR; 1. DR PANTHER; PTHR11486:SF77; FIBROBLAST GROWTH FACTOR 13; 1. DR Pfam; PF00167; FGF; 1. DR PRINTS; PR00263; HBGFFGF. DR PRINTS; PR00262; IL1HBGF. DR SMART; SM00442; FGF; 1. DR SUPFAM; SSF50353; Cytokine; 1. DR PROSITE; PS00247; HBGF_FGF; 1. DR Genevisible; P70377; MM. 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 //