SCN4A_MOUSE
ID SCN4A_MOUSE Reviewed; 1841 AA.
AC Q9ER60; A2VDE9; B1ARK0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Sodium channel protein type 4 subunit alpha;
DE AltName: Full=Sodium channel protein skeletal muscle subunit alpha;
DE AltName: Full=Sodium channel protein type IV subunit alpha;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4;
GN Name=Scn4a;
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], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Heart;
RX PubMed=11834499; DOI=10.1152/ajpheart.00644.2001;
RA Zimmer T., Bollensdorff C., Haufe V., Birch-Hirschfeld E., Benndorf K.;
RT "Mouse heart Na+ channels: primary structure and function of two isoforms
RT and alternatively spliced variants.";
RL Am. J. Physiol. 282:H1007-H1017(2002).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1841.
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 [4]
RP INTERACTION WITH SNTA1; SNTB1 AND SNTB2.
RX PubMed=9412493; DOI=10.1523/jneurosci.18-01-00128.1998;
RA Gee S.H., Madhavan R., Levinson S.R., Caldwell J.H., Sealock R.,
RA Froehner S.C.;
RT "Interaction of muscle and brain sodium channels with multiple members of
RT the syntrophin family of dystrophin-associated proteins.";
RL J. Neurosci. 18:128-137(1998).
RN [5]
RP FUNCTION, MUTAGENESIS OF MET-1586, AND TISSUE SPECIFICITY.
RX PubMed=18317596; DOI=10.1172/jci32638;
RA Hayward L.J., Kim J.S., Lee M.Y., Zhou H., Kim J.W., Misra K.,
RA Salajegheh M., Wu F.F., Matsuda C., Reid V., Cros D., Hoffman E.P.,
RA Renaud J.M., Cannon S.C., Brown R.H. Jr.;
RT "Targeted mutation of mouse skeletal muscle sodium channel produces
RT myotonia and potassium-sensitive weakness.";
RL J. Clin. Invest. 118:1437-1449(2008).
RN [6]
RP FUNCTION, AND MUTAGENESIS OF ARG-663.
RX PubMed=21881211; DOI=10.1172/jci57398;
RA Wu F., Mi W., Burns D.K., Fu Y., Gray H.F., Struyk A.F., Cannon S.C.;
RT "A sodium channel knockin mutant (NaV1.4-R669H) mouse model of hypokalemic
RT periodic paralysis.";
RL J. Clin. Invest. 121:4082-4094(2011).
CC -!- FUNCTION: Pore-forming subunit of a voltage-gated sodium channel
CC complex through which Na(+) ions pass in accordance with their
CC electrochemical gradient. Alternates between resting, activated and
CC inactivated states (PubMed:11834499). Required for normal muscle fiber
CC excitability, normal muscle contraction and relaxation cycles, and
CC constant muscle strength in the presence of fluctuating K(+) levels
CC (PubMed:18317596, PubMed:21881211). {ECO:0000269|PubMed:11834499,
CC ECO:0000269|PubMed:18317596, ECO:0000269|PubMed:21881211}.
CC -!- ACTIVITY REGULATION: Channel activity is regulated by the ancillary
CC beta subunit SCN1B. SCN1B strongly enhances the presence of the pore-
CC forming alpha subunit at the cell surface (By similarity). Interaction
CC with SCN1B is required for rapid channel inactivation and rapid
CC recovery after inactivation, and prevents decrease of channel activity
CC in response to repetitive, high-frequency depolarizations (By
CC similarity). The channel is inhibited by tetrodotoxin
CC (PubMed:11834499). {ECO:0000250|UniProtKB:P15390,
CC ECO:0000250|UniProtKB:P35499, ECO:0000269|PubMed:11834499}.
CC -!- SUBUNIT: Component of a voltage-sensitive sodium channel complex that
CC consists of a pore-forming alpha subunit and one or more regulatory
CC beta subunits. Interacts with SCN1B (By similarity). Heterooligomer
CC with SCN2B or SCN4B; disulfide-linked (By similarity). Interacts with
CC the PDZ domain of the syntrophins SNTA1, SNTB1 and SNTB2
CC (PubMed:9412493). Interacts with the conotoxin GVIIJ (By similarity).
CC {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P15390,
CC ECO:0000269|PubMed:9412493}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11834499};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
CC -!- TISSUE SPECIFICITY: Detected in quadriceps muscle (at protein level)
CC (PubMed:18317596). Detected in hind-limb skeletal muscles, but not in
CC heart or brain (PubMed:18317596). Detected at low levels in the
CC myocardium. {ECO:0000269|PubMed:11834499, ECO:0000269|PubMed:18317596}.
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 every
CC third position. {ECO:0000250|UniProtKB:P35499}.
CC -!- PTM: Phosphorylation at Ser-1322 by PKC in a highly conserved
CC cytoplasmic loop slows inactivation of the sodium channel and reduces
CC peak sodium currents. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.4/SCN4A subfamily. {ECO:0000305}.
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DR EMBL; AJ278787; CAC17146.1; -; mRNA.
DR EMBL; AL604045; CAM23795.1; -; Genomic_DNA.
DR EMBL; BC129805; AAI29806.1; -; mRNA.
DR CCDS; CCDS48961.1; -.
DR RefSeq; NP_573462.2; NM_133199.2.
DR AlphaFoldDB; Q9ER60; -.
DR SMR; Q9ER60; -.
DR STRING; 10090.ENSMUSP00000021056; -.
DR BindingDB; Q9ER60; -.
DR ChEMBL; CHEMBL3616353; -.
DR GlyGen; Q9ER60; 10 sites.
DR iPTMnet; Q9ER60; -.
DR PhosphoSitePlus; Q9ER60; -.
DR MaxQB; Q9ER60; -.
DR PaxDb; Q9ER60; -.
DR PRIDE; Q9ER60; -.
DR ProteomicsDB; 253413; -.
DR DNASU; 110880; -.
DR GeneID; 110880; -.
DR KEGG; mmu:110880; -.
DR CTD; 6329; -.
DR MGI; MGI:98250; Scn4a.
DR eggNOG; KOG2301; Eukaryota.
DR InParanoid; Q9ER60; -.
DR OrthoDB; 56920at2759; -.
DR PhylomeDB; Q9ER60; -.
DR Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR BioGRID-ORCS; 110880; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q9ER60; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9ER60; protein.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:MGI.
DR GO; GO:0006812; P:cation transport; ISO:MGI.
DR GO; GO:0015871; P:choline transport; ISO:MGI.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0100001; P:regulation of skeletal muscle contraction by action potential; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR GO; GO:0006814; P:sodium ion transport; IDA:MGI.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR008052; Na_channel_a4su_mammal.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01665; NACHANNEL4.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sodium;
KW Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT CHAIN 1..1841
FT /note="Sodium channel protein type 4 subunit alpha"
FT /id="PRO_0000371316"
FT TOPO_DOM 1..131
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 132..150
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 151..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..178
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 179..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..210
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 211..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..233
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 234..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..272
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 273..385
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 386..410
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 411..417
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 418..438
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 439..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 573..591
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 592..602
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 603..622
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 623..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 637..656
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 657..658
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 659..676
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 677..692
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 693..711
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 712..740
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 741..761
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 762..772
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 773..791
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 792..1026
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1027..1044
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1045..1057
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1058..1076
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1077..1090
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1091..1109
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1110..1117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1118..1136
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1137..1153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1154..1173
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1174..1224
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1225..1246
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1247..1263
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1264..1285
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1286..1348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1349..1366
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1367..1377
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1378..1396
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1397..1408
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1409..1426
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1427..1439
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1440..1456
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1457..1475
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1476..1493
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1494..1515
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1516..1538
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1539..1568
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1569..1591
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1592..1841
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 113..448
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 554..826
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1007..1320
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1329..1627
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1721..1750
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 32..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 925..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1304..1306
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT REGION 1776..1841
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..888
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 969..983
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1782..1797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1829
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 401
FT /note="Important for inhibition by tetrodotoxin"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT MOD_RES 1322
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 315
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 327
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1199
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..354
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 363..369
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 723
FT /note="Interchain; with SCN2B or SCN4B"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 723
FT /note="Interchain; with the conotoxin GVIIJ (when the
FT channel is not linked to SCN2B or SCN4B; the bond to SCN2B
FT or SCN4B protects the channel from the inhibition by
FT toxin)"
FT /evidence="ECO:0000250|UniProtKB:P04775"
FT DISULFID 725..731
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 763..772
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1183..1203
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1547..1562
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT MUTAGEN 663
FT /note="R->F: Homozygous mice are born at the expected
FT Mendelian rate and have no visible phenotype. Hind-limb
FT muscles show decreased excitability and decreased force
FT when K(+) levels are low (in vivo). Isolated soleus muscle
FT from homozygous mice has an increased susceptibility to
FT loss of force generation at 2 mM K(+)."
FT /evidence="ECO:0000269|PubMed:21881211"
FT MUTAGEN 1586
FT /note="M->V: A very low percentage of homozygous mice are
FT present at 30 days after birth, suggesting high perinatal
FT lethality. In anesthesized heterozygous mice,
FT electromyographs from hind-limb muscle show high background
FT activity, indicative of myotonia. Isolated extensor
FT digitorum longus muscle from heterozygous mice displays
FT reduced twitch force, with a normal speed of muscle
FT contraction, but an increased muscle relaxation half-time.
FT Isolated skeletal muscle from heterozygous mice has
FT strongly decreased force when the K(+) levels are increased
FT to 10 mM. Homozygous mice display prominent hind-limb
FT weakness and muscle atrophy."
FT /evidence="ECO:0000269|PubMed:18317596"
FT CONFLICT 131
FT /note="A -> T (in Ref. 2; CAM23795)"
FT /evidence="ECO:0000305"
FT CONFLICT 1056
FT /note="R -> Q (in Ref. 2; CAM23795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1841 AA; 208798 MW; 0766DFD33A9E0E55 CRC64;
MASSSLPTLV PPGPHCLRPF TPESLAAIEQ RAMEEEARLQ RNKQMEIEEP ERKPRSDLEA
GKNLPLIYGD PPPEVIGVPL EDLDPYYSDK KTFIVLNKGK AIFRFSATPA LYMLSPFSIV
RRVAIKVLIH ALFSMFIMIT ILTNCVFMTM SNPPSWSKDV EYTFTGIYTF ESLIKMLARG
FCIDDFTFLR DPWNWLDFSV ITMAYVTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV
GALIQSVKKL SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPPPMNDT NTTWYGNDTW
YGNDTWYGND TWYGNDTWNS QESWVSNSTF DWEAYINDEG NFYFLEGSND ALLCGNSSDA
GHCPEGYECM KAGRNPNYGY TSYDTFSWAF LALFRLMTQD YWENLFQLTL RAAGKTYMIF
FVVIIFLGSF YLINLILAVV AMAYAEQNEA TLAEDQEKEE EFQQMLEKFK KHQEELEKAK
AAQALEGGEE ADGDPTHSKD CNGSLDTSGE KGPPRPSCSA ESAISDAMEE LEEAHQKCPP
WWYKCAHKVL IWNCCAPWVK FKHIILLIVM DPFVDLGITI CIVLNTLFMA MEHYPMTEHF
DNVLSVGNLV FTGIFTAEMV LKLIAMDPYE YFQQGWNIFD SFIVTLSLVE LGLANVQGLS
VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKSY
KECVCKIASD CSLPRWHMHD FFHSFLIVFR ILCGEWIETM WDCMEVAGQA MCLTVFLMVM
VIGNLVVLNL FLALLLSSFS ADSLAASDED GEMNNLQIAI GRIKWGIAFA KTFLLGLLHG
KILSLKDIML SLGEPGGAGE NGESPPEDEK KEPPPEDGNK ELKDNHILNH VGLTDGPRSS
IEMDHLNFIN NPYLTIHVPI ASEESDLEMP TEEETDTFSE PEDIKKPLQP LYDGNSSVCS
TADYKPPEED PEEQAEENPE GELPEECFTE ACVKRCPCLY VDISQGRGKM WWTLRRACFK
IVEHNWFETF IVFMILLSSG ALAFEDIYIE QRRVIRTILE YADKVFTYIF ILEMLLKWVA
YGFKVYFTNA WCWLDFLIVD VSIISLVANW LGYSELGPIK SLRTLRALRP LRALSRFEGM
RVVVNALLGA IPSIMNVLLV CLIFWLIFSI MGVNLFAGKF YYCINTTTSE RFDISVVNNK
SECESLMYTG QVRWMNVKVN YDNVGLGYLS LLQVATFKGW MDIMYAAVDS REKEEQPDYE
VNLYMYLYFV IFIIFGSFFT LNLFIGVIID NFNQQKKKFG GKDIFMTEEQ KKYYNAMKKL
GSKKPQKPIP RPQNKIQGMV YDFVTKQVFD ISIMILICLN MVTMMVETDD QSQLKVDILY
NINMVFIIVF TGECVLKMFA LRHYYFTIGW NIFDFVVVIL SIVGLALSDL IQKYFVSPTL
FRVIRLARIG RVLRLIRGAK GIRTLLFALM MSLPALFNIG LLLFLVMFIY SIFGMSNFAY
VKKESGIDDM FNFETFGNSI ICLFEITTSA GWDGLLNPIL NSGPPDCDPT LENPGTNIKG
DCGNPSIGIC FFCSYIIISF LIVVNMYIAI ILENFNVATE ESSEPLCEDD FEMFYETWEK
FDPDATQFID YSRLSDFVDT LQEPLKIAKP NKIKLITLDL PMVPGDKIHC LDILFALTKE
VLGDSGEMDA LKQTMEEKFM AANPSKVSYE PITTTLKRKQ EEVCAIKIQR AYRRHLLQRS
VKQASYMYRH SQEGNGDGAP EKEGLLANTM NKMYGSEKED NGVQSQGEKE KDSTEDAGPT
TEVTAPSSSD TALTPPPPSP PPPSSPPQGQ TVRPGVKESL V
