ID   SCN8A_MOUSE             Reviewed;        1978 AA.
AC   Q9WTU3; Q3TYI3; Q60828; Q60858; Q62449;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   14-OCT-2015, entry version 127.
DE   RecName: Full=Sodium channel protein type 8 subunit alpha;
DE   AltName: Full=Sodium channel protein type VIII subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.6;
GN   Name=Scn8a; Synonyms=Nbna1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:AAD20438.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAD20438.1};
RX   PubMed=9828131; DOI=10.1006/geno.1998.5550;
RA   Plummer N.W., Galt J., Jones J.M., Burgess D.L., Sprunger L.K.,
RA   Kohrman D.C., Meisler M.H.;
RT   "Exon organization, coding sequence, physical mapping, and polymorphic
RT   intragenic markers for the human neuronal sodium channel gene SCN8A.";
RL   Genomics 54:287-296(1998).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
RP   DISEASE.
RC   STRAIN=C57BL/6J {ECO:0000269|PubMed:7670495};
RC   TISSUE=Brain {ECO:0000269|PubMed:7670495};
RX   PubMed=7670495; DOI=10.1038/ng0895-461;
RA   Burgess D.L., Kohrman D.C., Galt J., Plummer N.W., Jones J.M.,
RA   Spear B., Meisler M.H.;
RT   "Mutation of a new sodium channel gene, Scn8a, in the mouse mutant
RT   'motor endplate disease'.";
RL   Nat. Genet. 10:461-465(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-804, AND VARIANT LEU-5.
RC   STRAIN=C57BL/6J; TISSUE=Visual cortex;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 93-205, AND DISEASE.
RC   STRAIN=129/Sv {ECO:0000269|PubMed:8663325};
RC   TISSUE=Brain {ECO:0000269|PubMed:8663325};
RX   PubMed=8663325; DOI=10.1074/jbc.271.29.17576;
RA   Kohrman D.C., Harris J.B., Meisler M.H.;
RT   "Mutation detection in the med and medJ alleles of the sodium channel
RT   Scn8a. Unusual splicing due to a minor class AT-AC intron.";
RL   J. Biol. Chem. 271:17576-17581(1996).
RN   [5] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1411-1686.
RA   Fan Z., Kyle J.W., Makielski J.C.;
RT   "A putative novel Na channel alpha subunit cDNA isolated from mouse
RT   NB2a neuroblastoma cells.";
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INTERACTION WITH NEDD4 AND NEDD4L.
RX   PubMed=15123669; DOI=10.1074/jbc.M402820200;
RA   Fotia A.B., Ekberg J., Adams D.J., Cook D.I., Poronnik P., Kumar S.;
RT   "Regulation of neuronal voltage-gated sodium channels by the
RT   ubiquitin-protein ligases Nedd4 and Nedd4-2.";
RL   J. Biol. Chem. 279:28930-28935(2004).
RN   [7] {ECO:0000305}
RP   ALTERNATIVE SPLICING (ISOFORMS 1; 4 AND 5).
RC   TISSUE=Brain {ECO:0000269|PubMed:9295353}, and
RC   Fetal brain {ECO:0000269|PubMed:9295353};
RX   PubMed=9295353; DOI=10.1074/jbc.272.38.24008;
RA   Plummer N.W., McBurney M.W., Meisler M.H.;
RT   "Alternative splicing of the sodium channel SCN8A predicts a truncated
RT   two-domain protein in fetal brain and non-neuronal cells.";
RL   J. Biol. Chem. 272:24008-24015(1997).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=19136557; DOI=10.1074/jbc.M801892200;
RA   Carrithers M.D., Chatterjee G., Carrithers L.M., Offoha R.,
RA   Iheagwara U., Rahner C., Graham M., Waxman S.G.;
RT   "Regulation of podosome formation in macrophages by a splice variant
RT   of the sodium channel SCN8A.";
RL   J. Biol. Chem. 284:8114-8126(2009).
RN   [9] {ECO:0000305}
RP   VARIANT MEDJO THR-1317, AND VARIANT LEU-5.
RC   STRAIN=DBA/2WyDi {ECO:0000269|PubMed:8815882};
RX   PubMed=8815882;
RA   Kohrman D.C., Smith M.R., Goldin A.L., Harris J., Meisler M.H.;
RT   "A missense mutation in the sodium channel Scn8a is responsible for
RT   cerebellar ataxia in the mouse mutant jolting.";
RL   J. Neurosci. 16:5993-5999(1996).
RN   [10] {ECO:0000305}
RP   DISEASE.
RX   PubMed=11532991; DOI=10.1093/hmg/10.17.1819;
RA   De Repentigny Y., Cote P.D., Pool M., Bernier G., Girard S.,
RA   Vidal S.M., Kothary R.;
RT   "Pathological and genetic analysis of the degenerating muscle (dmu)
RT   mouse: a new allele of Scn8a.";
RL   Hum. Mol. Genet. 10:1819-1827(2001).
CC   -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability
CC       of excitable membranes. Assuming opened or closed conformations in
CC       response to the voltage difference across the membrane, the
CC       protein forms a sodium-selective channel through which Na(+) ions
CC       may pass in accordance with their electrochemical gradient. In
CC       macrophages, isoform 5 may participate in the control of podosome
CC       and invadopodia formation. {ECO:0000269|PubMed:19136557}.
CC   -!- SUBUNIT: Interacts with FGF13; may regulate SCN8A activity (By
CC       similarity). Interacts with NEDD4 and NEDD4L. {ECO:0000250,
CC       ECO:0000269|PubMed:15123669}.
CC   -!- INTERACTION:
CC       P14873:Map1b; NbExp=7; IntAct=EBI-6396042, EBI-764653;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:19136557};
CC       Multi-pass membrane protein {ECO:0000269|PubMed:19136557}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1 {ECO:0000269|PubMed:9295353, ECO:0000269|PubMed:9828131};
CC       Synonyms=18A {ECO:0000269|PubMed:9295353};
CC         IsoId=Q9WTU3-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:7670495};
CC         IsoId=Q9WTU3-2; Sequence=VSP_050594;
CC         Note=Due to aberrant splicing.;
CC       Name=3 {ECO:0000269|PubMed:9828131};
CC         IsoId=Q9WTU3-3; Sequence=VSP_050595;
CC       Name=4 {ECO:0000269|PubMed:9295353}; Synonyms=18N
CC       {ECO:0000269|PubMed:9295353};
CC         IsoId=Q9WTU3-4; Sequence=VSP_050596, VSP_050597;
CC       Name=5 {ECO:0000269|PubMed:9295353};
CC         IsoId=Q9WTU3-5; Sequence=VSP_050598;
CC   -!- TISSUE SPECIFICITY: Expressed in brain, cerebellum and spinal
CC       cord. Isoform 5 may be expressed in non-neuronal tissues, such as
CC       peritoneal macrophages. {ECO:0000269|PubMed:19136557,
CC       ECO:0000269|PubMed:7670495}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged
CC       segment (S4). Segments S4 are probably the voltage-sensors and are
CC       characterized by a series of positively charged amino acids at
CC       every third position. {ECO:0000305}.
CC   -!- PTM: May be ubiquitinated by NEDD4L; which would promote its
CC       endocytosis. {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-1495 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and
CC       reduces peak sodium currents. {ECO:0000250}.
CC   -!- DISEASE: Note=Defects in Scn8a are the cause of motor endplate
CC       disease (med). Med is a recessive neuromuscular disorder that is
CC       characterized by lack of signal transmission at the neuromuscular
CC       junction, excess preterminal arborization and degeneration of
CC       cerebellar Purkinje cells. It produces early onset progressive
CC       paralysis of hind limbs, severe muscle atrophy and juvenile
CC       lethality.
CC   -!- DISEASE: Note=Defects in Scn8a are the cause of the jolting mutant
CC       (medjo), a mild form of motor endplate disease which is
CC       characterized by the absence of spontaneous, regular, simple
CC       discharges from Purkinje cells. After 3 weeks of age, jolting mice
CC       are unsteady and have wide-based gait and a rhythmical tremor of
CC       head and neck induced by attempted movement.
CC   -!- DISEASE: Note=Defects in Scn8a are a cause of degenerating muscle
CC       (dmu). Dmu is an autosomal recessive neuromuscular disorder that
CC       is characterized by skeletal and cardiac muscle degeneration. It
CC       produces early onset progressive loss of mobility of the hind
CC       limbs and subsequent lethality in the first month of life.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.6/SCN8A subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 IQ domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00116, ECO:0000305}.
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DR   EMBL; AF049617; AAD20438.1; -; mRNA.
DR   EMBL; U26707; AAC52242.1; -; mRNA.
DR   EMBL; AK158609; BAE34580.1; -; mRNA.
DR   EMBL; U59964; AAC52708.1; -; Genomic_DNA.
DR   EMBL; U59963; AAC52708.1; JOINED; Genomic_DNA.
DR   EMBL; U23158; AAA65599.1; -; mRNA.
DR   CCDS; CCDS57011.1; -. [Q9WTU3-1]
DR   RefSeq; NP_001070967.1; NM_001077499.2.
DR   RefSeq; NP_035453.2; NM_011323.3.
DR   UniGene; Mm.385012; -.
DR   PDB; 3WFN; X-ray; 1.95 A; B/C/D/E=1893-1914.
DR   PDBsum; 3WFN; -.
DR   ProteinModelPortal; Q9WTU3; -.
DR   SMR; Q9WTU3; 1765-1911.
DR   BioGrid; 203103; 3.
DR   IntAct; Q9WTU3; 1.
DR   STRING; 10090.ENSMUSP00000080842; -.
DR   BindingDB; Q9WTU3; -.
DR   ChEMBL; CHEMBL1914275; -.
DR   GuidetoPHARMACOLOGY; 583; -.
DR   PhosphoSite; Q9WTU3; -.
DR   PaxDb; Q9WTU3; -.
DR   PRIDE; Q9WTU3; -.
DR   GeneID; 20273; -.
DR   KEGG; mmu:20273; -.
DR   CTD; 6334; -.
DR   MGI; MGI:103169; Scn8a.
DR   eggNOG; COG1226; -.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG091796; -.
DR   InParanoid; Q9WTU3; -.
DR   KO; K04840; -.
DR   PhylomeDB; Q9WTU3; -.
DR   ChiTaRS; Scn8a; mouse.
DR   NextBio; 297955; -.
DR   PRO; PR:Q9WTU3; -.
DR   Proteomes; UP000000589; Unplaced.
DR   CleanEx; MM_SCN8A; -.
DR   Genevisible; Q9WTU3; MM.
DR   GO; GO:0030425; C:dendrite; IDA:MGI.
DR   GO; GO:0016020; C:membrane; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0033268; C:node of Ranvier; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0034706; C:sodium channel complex; IPI:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IC:UniProtKB.
DR   GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; NAS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR   GO; GO:0007628; P:adult walking behavior; IMP:MGI.
DR   GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR   GO; GO:0007517; P:muscle organ development; IMP:MGI.
DR   GO; GO:0050905; P:neuromuscular process; IMP:MGI.
DR   GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR   GO; GO:0009636; P:response to toxic substance; IDA:MGI.
DR   GO; GO:0007605; P:sensory perception of sound; IMP:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; NAS:UniProtKB.
DR   Gene3D; 1.20.120.350; -; 4.
DR   InterPro; IPR027359; Channel_four-helix_dom.
DR   InterPro; IPR024583; DUF3451.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR008054; Na_channel_a8su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF132; PTHR10037:SF132; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   Pfam; PF11933; Na_trans_cytopl; 1.
DR   PRINTS; PR00170; NACHANNEL.
DR   PRINTS; PR01667; NACHANNEL8.
DR   SMART; SM00015; IQ; 1.
DR   PROSITE; PS50096; IQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW   Disease mutation; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW   Repeat; Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1   1978       Sodium channel protein type 8 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048501.
FT   TOPO_DOM      1    127       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    128    151       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    152    159       Extracellular. {ECO:0000255}.
FT   TRANSMEM    160    179       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    180    192       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    193    211       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    212    217       Extracellular. {ECO:0000255}.
FT   TRANSMEM    218    237       Helical; Name=S4 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    238    252       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    253    277       Helical; Voltage-sensor; Name=S5 of
FT                                repeat I. {ECO:0000255}.
FT   TOPO_DOM    278    387       Extracellular. {ECO:0000255}.
FT   TRANSMEM    388    413       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    414    745       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    746    770       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    771    781       Extracellular. {ECO:0000255}.
FT   TRANSMEM    782    805       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    806    813       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    814    833       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    834    839       Extracellular. {ECO:0000255}.
FT   TRANSMEM    840    860       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000255}.
FT   TOPO_DOM    861    875       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    876    896       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    897    949       Extracellular. {ECO:0000255}.
FT   TRANSMEM    950    975       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    976   1191       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1192   1215       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1216   1228       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1229   1254       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1255   1260       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1261   1282       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1283   1286       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1287   1308       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000255}.
FT   TOPO_DOM   1309   1327       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1328   1349       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1350   1435       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1436   1462       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1463   1515       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1516   1539       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1540   1550       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1551   1574       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1575   1580       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1581   1604       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1605   1614       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1615   1636       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000255}.
FT   TOPO_DOM   1637   1651       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM   1652   1674       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1675   1739       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1740   1764       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1765   1978       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      114    442       I. {ECO:0000305}.
FT   REPEAT      733   1005       II. {ECO:0000305}.
FT   REPEAT     1178   1493       III. {ECO:0000305}.
FT   REPEAT     1502   1799       IV. {ECO:0000305}.
FT   DOMAIN     1893   1922       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116, ECO:0000305}.
FT   NP_BIND     891    898       ATP. {ECO:0000255}.
FT   MOD_RES     518    518       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O88420}.
FT   MOD_RES     520    520       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O88420}.
FT   MOD_RES    1495   1495       Phosphoserine; by PKC. {ECO:0000250}.
FT   CARBOHYD    215    215       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    289    289       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    295    295       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    308    308       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    326    326       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1356   1356       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1370   1370       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD   1381   1381       N-linked (GlcNAc...). {ECO:0000255}.
FT   VAR_SEQ     428    673       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:7670495}.
FT                                /FTId=VSP_050594.
FT   VAR_SEQ     664    664       E -> EVKIDKAATDS (in isoform 3).
FT                                {ECO:0000303|PubMed:9828131}.
FT                                /FTId=VSP_050595.
FT   VAR_SEQ    1272   1312       Missing (in isoform 5).
FT                                {ECO:0000303|PubMed:9295353}.
FT                                /FTId=VSP_050598.
FT   VAR_SEQ    1273   1280       SLVSLIAN -> PLSLSGLI (in isoform 4).
FT                                {ECO:0000303|PubMed:9295353}.
FT                                /FTId=VSP_050596.
FT   VAR_SEQ    1281   1978       Missing (in isoform 4).
FT                                {ECO:0000303|PubMed:9295353}.
FT                                /FTId=VSP_050597.
FT   VARIANT       5      5       V -> L. {ECO:0000269|PubMed:16141072,
FT                                ECO:0000269|PubMed:8815882}.
FT   VARIANT    1317   1317       A -> T (in medjo).
FT                                {ECO:0000269|PubMed:8815882}.
FT   CONFLICT    207    207       V -> I (in Ref. 3; BAE34580).
FT                                {ECO:0000305}.
FT   CONFLICT    212    212       D -> N (in Ref. 3; BAE34580).
FT                                {ECO:0000305}.
FT   CONFLICT    554    554       P -> T (in Ref. 3; BAE34580).
FT                                {ECO:0000305}.
FT   CONFLICT    596    596       G -> D (in Ref. 3; BAE34580).
FT                                {ECO:0000305}.
FT   CONFLICT   1498   1498       P -> A (in Ref. 5; AAA65599).
FT                                {ECO:0000305}.
FT   CONFLICT   1504   1504       R -> E (in Ref. 5; AAA65599).
FT                                {ECO:0000305}.
FT   HELIX      1893   1912       {ECO:0000244|PDB:3WFN}.
SQ   SEQUENCE   1978 AA;  225141 MW;  9EA4A8E610707220 CRC64;
     MAARVLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
     AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
     IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPEWSKN VEYTFTGIYT FESLVKIIAR
     GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
     VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTRGF
     DWEEYINNKT NFYMVPGMLE PLLCGNSSDA GQCPEGFQCM KAGRNPNYGY TSFDTFSWAF
     LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
     TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEDG VGSPRSSSEL
     SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
     SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
     LFIPIRARER RSSYSGYSGY SQCSRSSRIF PSLRRSVKRN STVDCNGVVS LIGPGSHIGR
     LLPEATTEVE IKKKGPGSLL VSMEQLASYG RKDRINSIMS VVTNTLVEEL EESQRKCPPC
     WYKFANTFLI WECHPYWIKL KEIVNLIVMD PFVDLAITIC IVLNTLFMAM EHHPMTPQFE
     HVLAVGNLVF TGIFTAEMFL KLIAMDPYYY FQEGWNIFDG FIVSLSLMEL GLADVEGLSV
     LRSFRLLRVF KLAKSWPTLN MLIKIIGNSV GALGNLTLVL AIIVFIFAVV GMQLFGKSYK
     ECVCKISQEC KLPRWHMNDF FHSFLIVFRV LCGEWIETMW DCMEVAGQAM CLIVFMMVMV
     IGNLVVLNLF LALLLSSFSA DNLAATDDDG EMNNLQISVI RIKKGVAWAK VKVHAFMQAH
     FKQREADEVK PLDELYEKKA NCIANHTGVD IHRNGDFQKN GNGTTSGIGS SVEKYIIDED
     HMSFINNPNL TVRVPIAVGE SDFENLNTED VSSESDPEGS KDKLDDTSSS EGSTIDIKPE
     VEEVPVEQPE EYLDPDACFT EGCVQRFKCC QVNIEEGLGK SWWILRKTCF LIVEHNWFET
     FIIFMILLSS GALAFEDIYI EQRKTIRTIL EYADKVFTYI FILEMLLKWT AYGFVKFFTN
     AWCWLDFLIV AVSLVSLIAN ALGYSELGAI KSLRTLRALR PLRALSRFEG MRVVVNALVG
     AIPSIMNVLL VCLIFWLIFS IMGVNLFAGK YHYCFNETSE IRFEIDEVNN KTDCEKLMEG
     NNTEIRWKNV KINFDNVGAG YLALLQVATF KGWMDIMYAA VDSRKPDEQP DYEGNIYMYI
     YFVIFIIFGS FFTLNLFIGV IIDNFNQQKK KFGGQDIFMT EEQKKYYNAM KKLGSKKPQK
     PIPRPLNKIQ GIVFDFVTQQ AFDIVIMMLI CLNMVTMMVE TDTQSKQMEN ILYWINLVFV
     IFFTCECVLK MFALRHYYFT IGWNIFDFVV VILSIVGMFL ADIIEKYFVS PTLFRVIRLA
     RIGRILRLIK GAKGIRTLLF ALMMSLPALF NIGLLLFLVM FIFSIFGMSN FAYVKHEAGI
     DDMFNFETFG NSMICLFQIT TSAGWDGLLL PILNRPPDCS LDKEHPGSGF KGDCGNPSVG
     IFFFVSYIII SFLIVVNMYI AIILENFSVA TEESADPLSE DDFETFYEIW EKFDPDATQF
     IEYCKLADFA DALEHPLRVP KPNTIELIAM DLPMVSGDRI HCLDILFAFT KRVLGDSGEL
     DILRQQMEER FVASNPSKVS YEPITTTLRR KQEEVSAVVL QRAYRGHLAR RGFICRKITS
     NKLENGGTHR EKKESTPSTA SLPSYDSVTK PDKEKQQRAE EGRRERAKRQ KEVRESKC
//