FGF13_RAT
ID FGF13_RAT Reviewed; 245 AA.
AC Q9ERW3;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Fibroblast growth factor 13;
DE Short=FGF-13;
GN Name=Fgf13;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Spinal ganglion;
RA Xiao H., Huang Q., Zhang F., Guo C., Chen Z., Han Z., Zhang X.;
RT "Rattus norvegicus fibroblast growth factor 13.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
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 [4]
RP PHOSPHORYLATION.
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).
CC -!- FUNCTION: Microtubule-binding protein which directly binds tubulin and
CC is involved in both polymerization and stabilization of microtubules
CC (By similarity). Through its action on microtubules, may participate in
CC the refinement of axons by negatively regulating axonal and leading
CC processes branching (By similarity). Plays a crucial role in neuron
CC polarization and migration in the cerebral cortex and the hippocampus
CC (By similarity). Regulates voltage-gated sodium channels transport and
CC function (By similarity). May also play a role in MAPK signaling (By
CC similarity). Required for the development of axonal initial segment-
CC targeting inhibitory GABAergic synapses made by chandelier neurons (By
CC similarity). {ECO:0000250|UniProtKB:P70377,
CC ECO:0000250|UniProtKB:Q92913}.
CC -!- SUBUNIT: Interacts with SCN8A; regulates SCN8A activity. Interacts with
CC SCN1A; may regulate SCN1A activity. Interacts with SCN5A; the
CC interaction is direct and may regulate SNC5A density at membranes and
CC function. May also interact with SCN2A and SCN11A. Interacts with
CC MAPK8IP2; may regulate the MAPK8IP2 scaffolding activity.
CC {ECO:0000250|UniProtKB:Q92913}.
CC -!- SUBCELLULAR LOCATION: Cell projection, filopodium
CC {ECO:0000250|UniProtKB:P70377}. Cell projection, growth cone
CC {ECO:0000250|UniProtKB:P70377}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P70377}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P70377}. Cytoplasm
CC {ECO:0000250|UniProtKB:P70377}. Nucleus {ECO:0000250|UniProtKB:P61329}.
CC Note=Not secreted. Localizes to the lateral membrane and intercalated
CC disks of myocytes. {ECO:0000250|UniProtKB:P70377}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ERW3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ERW3-2; Sequence=VSP_044133;
CC -!- PTM: May be phosphorylated. {ECO:0000269|PubMed:12244047}.
CC -!- SIMILARITY: Belongs to the heparin-binding growth factors family.
CC {ECO:0000305}.
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DR EMBL; AF271786; AAG15492.1; -; mRNA.
DR EMBL; AABR06108696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108698; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06108700; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474019; EDL86166.1; -; Genomic_DNA.
DR EMBL; CH474019; EDL86169.1; -; Genomic_DNA.
DR RefSeq; NP_445880.1; NM_053428.1. [Q9ERW3-2]
DR RefSeq; XP_006257654.1; XM_006257592.1. [Q9ERW3-1]
DR AlphaFoldDB; Q9ERW3; -.
DR SMR; Q9ERW3; -.
DR STRING; 10116.ENSRNOP00000062217; -.
DR iPTMnet; Q9ERW3; -.
DR PhosphoSitePlus; Q9ERW3; -.
DR PaxDb; Q9ERW3; -.
DR ABCD; Q9ERW3; 4 sequenced antibodies.
DR Ensembl; ENSRNOT00000064780; ENSRNOP00000062217; ENSRNOG00000042753. [Q9ERW3-2]
DR Ensembl; ENSRNOT00000077402; ENSRNOP00000072195; ENSRNOG00000042753. [Q9ERW3-1]
DR GeneID; 84488; -.
DR KEGG; rno:84488; -.
DR CTD; 2258; -.
DR RGD; 620164; Fgf13.
DR eggNOG; KOG3885; Eukaryota.
DR GeneTree; ENSGT00940000163347; -.
DR HOGENOM; CLU_081609_2_0_1; -.
DR InParanoid; Q9ERW3; -.
DR OrthoDB; 1192273at2759; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:Q9ERW3; -.
DR Proteomes; UP000002494; Chromosome X.
DR Proteomes; UP000234681; Chromosome x.
DR Bgee; ENSRNOG00000042753; Expressed in Ammon's horn and 16 other tissues.
DR ExpressionAtlas; Q9ERW3; baseline and differential.
DR Genevisible; Q9ERW3; RN.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISS:UniProtKB.
DR GO; GO:0016328; C:lateral plasma membrane; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0030295; F:protein kinase activator activity; ISO:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0021795; P:cerebral cortex cell migration; ISS:UniProtKB.
DR GO; GO:0045200; P:establishment of neuroblast polarity; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISS:UniProtKB.
DR GO; GO:0007612; P:learning; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0007613; P:memory; ISS:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; ISS:UniProtKB.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0001764; P:neuron migration; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; ISO:RGD.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IBA:GO_Central.
DR GO; GO:1990834; P:response to odorant; IEP:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
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_0000419208"
FT REGION 1..62
FT /note="Mediates targeting to the nucleus"
FT /evidence="ECO:0000250"
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 213..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92913"
FT VAR_SEQ 1..62
FT /note="MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLF
FT GSKKRRRRRP -> MALLRKSYS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_044133"
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
