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Database: UniProt
Entry: SCN4A_HORSE
LinkDB: SCN4A_HORSE
Original site: SCN4A_HORSE 
ID   SCN4A_HORSE             Reviewed;        1834 AA.
AC   Q28371;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   10-MAY-2017, entry version 96.
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   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skeletal muscle;
RA   Stephan D.A., Wang J., Spier S., Hoffman E.P.;
RL   Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   INVOLVEMENT IN HYPP, AND VARIANT HYPP LEU-1416.
RX   PubMed=1338908; DOI=10.1038/ng1092-144;
RA   Rudolph J.A., Spier S.J., Byrns G., Rojas C.V., Bernoco D.,
RA   Hoffman E.P.;
RT   "Periodic paralysis in quarter horses: a sodium channel mutation
RT   disseminated by selective breeding.";
RL   Nat. Genet. 2:144-147(1992).
CC   -!- FUNCTION: This protein mediates the voltage-dependent sodium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a sodium-selective channel through
CC       which Na(+) ions may pass in accordance with their electrochemical
CC       gradient. This sodium channel may be present in both denervated
CC       and innervated skeletal muscle.
CC   -!- SUBUNIT: Muscle sodium channels contain an alpha subunit and a
CC       smaller beta subunit. Heterooligomer with SCN2B or SCN4B;
CC       disulfide-linked. Interacts with the PDZ domain of the syntrophin
CC       SNTA1, SNTB1 and SNTB2. Interacts with the conotoxin GVIIJ.
CC       {ECO:0000250|UniProtKB:P04775, ECO:0000250|UniProtKB:P15390,
CC       ECO:0000250|UniProtKB:Q9JJV9}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P35499}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively
CC       charged segment (S4). Segments S4 are probably the voltage-sensors
CC       and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000305}.
CC   -!- PTM: Phosphorylation at Ser-1325 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 SCN4A are the cause of periodic paralysis
CC       hyperkalemic (HYPP). HYPP is an autosomal dominant channelopathy
CC       characterized by episodic flaccid generalized muscle weakness
CC       associated with high levels of serum potassium. HYPP is frequently
CC       found in Quarter Horses, the most popular equine breed in the
CC       United States. {ECO:0000269|PubMed:1338908}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.4/SCN4A subfamily. {ECO:0000305}.
DR   EMBL; U25990; AAA67366.1; -; mRNA.
DR   RefSeq; NP_001075230.1; NM_001081761.1.
DR   UniGene; Eca.13094; -.
DR   ProteinModelPortal; Q28371; -.
DR   PRIDE; Q28371; -.
DR   GeneID; 100049793; -.
DR   KEGG; ecb:100049793; -.
DR   CTD; 6329; -.
DR   InParanoid; Q28371; -.
DR   KO; K04837; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
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   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; IPR010526; Na_trans_assoc.
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; Complete proteome; Disease mutation; Disulfide bond;
KW   Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1834       Sodium channel protein type 4 subunit
FT                                alpha.
FT                                /FTId=PRO_0000371315.
FT   TOPO_DOM      1    131       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    132    150       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    151    157       Extracellular. {ECO:0000305}.
FT   TRANSMEM    158    178       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    179    192       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    193    210       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    211    216       Extracellular. {ECO:0000305}.
FT   TRANSMEM    217    233       Helical; Name=S4 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    234    252       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    253    272       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    273    385       Extracellular. {ECO:0000305}.
FT   INTRAMEM    386    410       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    411    417       Extracellular. {ECO:0000305}.
FT   TRANSMEM    418    438       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    439    572       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    573    591       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    592    602       Extracellular. {ECO:0000305}.
FT   TRANSMEM    603    622       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    623    636       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    637    656       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    657    658       Extracellular. {ECO:0000305}.
FT   TRANSMEM    659    676       Helical; Name=S4 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    677    692       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    693    711       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    712    740       Extracellular. {ECO:0000305}.
FT   INTRAMEM    741    761       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    762    774       Extracellular. {ECO:0000305}.
FT   TRANSMEM    775    795       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    796   1029       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1030   1047       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1048   1060       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1061   1079       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1080   1093       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1094   1112       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1113   1120       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1121   1139       Helical; Name=S4 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1140   1156       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1157   1176       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1177   1227       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1228   1249       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1250   1266       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1267   1288       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1289   1351       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1352   1369       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1370   1380       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1381   1399       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1400   1411       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1412   1429       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1430   1442       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1443   1459       Helical; Name=S4 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1460   1478       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1479   1496       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1497   1518       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1519   1541       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1542   1571       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1572   1594       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1595   1834       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      113    448       I. {ECO:0000305}.
FT   REPEAT      554    826       II. {ECO:0000305}.
FT   REPEAT     1010   1323       III. {ECO:0000305}.
FT   REPEAT     1332   1630       IV. {ECO:0000305}.
FT   DOMAIN     1724   1753       IQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00116}.
FT   MOD_RES    1325   1325       Phosphoserine; by PKC. {ECO:0000250}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    291    291       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    303    303       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    309    309       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    327    327       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    356    356       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1188   1188       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1202   1202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    280    363       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    723    723       Interchain; with SCN2B or SCN4B.
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   DISULFID    723    723       Interchain; with the conotoxin GVIIJ
FT                                (when the channel is not linked to SCN2B
FT                                or SCN4B; the bond to SCN2B or SCN4B
FT                                protects the channel from the inhibition
FT                                by toxin).
FT                                {ECO:0000250|UniProtKB:P04775}.
FT   VARIANT    1416   1416       F -> L (in HYPP; found in a Quarter Horse
FT                                lineage segregating the disease).
FT                                {ECO:0000269|PubMed:1338908}.
SQ   SEQUENCE   1834 AA;  207487 MW;  01D62B25CD577D97 CRC64;
     MASSSLPNLV PLGPESLRPF TRASLAAIER RALEEEARLQ RNKQMEIQET ERNARSDLEA
     GKNLPLIYGD PPPEVIGIPL EDLDPYYSNK KTFIVLNKGK AIFRFSATPA LYMLSPFSII
     RRSAIKVLIH SLFSMFIMIT ILPNCVVMTM SDPPPWPIHV ENTFTGINTF ESLIKMLARG
     FCIDDFTFLR DPWNWLDFSV IMMAYLTEFV DLGNISALRT FRVLRALKTI TVIPGLKTIV
     GALIQSVKKL SDVMILTVFC LSVFALVGLQ LFMGNLRQKC VRWPQPFNDT NTTWYGNDTW
     YSNDTWNSND TWSSNDMWNS HESMASNYTF DWDAYINDEG NFYFLEGAKD ALLCGNSSDA
     GHCPEGYKCI KTGRNPNYGY TSHDTFSWAF LALFRLMIQD YWENLFQLTL RAAGKTYMIF
     FVVIIFLGSF YLINLILAVV TMAYAEQNEA TLAEDQEKEE EFQQMMEKFQ KQQEELEKAK
     ADQALEGGEA GGDPAHSKDC NGSLDTSPGE KGPPRQSCSA DSGVSDAMEE LEEAHQKCPP
     WWYKCAHKVL IWNCCTPWVK FKNIIHLIVM DPFVDLGITI CIVLNTLFMA MEHYPMTEHF
     DKVLTVGNLV FTGIFTAEMV LKLIALDPYE YFQQGWNVFD SIIVTLSWVE LGLVNVKGLS
     VLRSFRLVRS LKLAKSWPTL NMFIRIIGNS GGGLGNLTLV LAIIVVNFSV VGMQLFGKNY
     KECVCKNASD CALPRWKMCD FFHSFLIVLR ILCGEWIEPM WGFMEVAGQA MFLTVLLMVM
     VNGNLVDLDL FLALLLNPLN SDNLSASDED GEMNNLQISS WPIKLGICFA NAFLLGLLHG
     KILSPKDIML SLGDPGEAGE AGEAEESAPE DEKKEPPPED DDKDLKKDNH ILNHMGLVDG
     TPTSIELDHL NFINNPYLTI HVPIASEESD LEMPTEEETD TFSEPEDGKK PLQPLDGNSS
     VCSTADYKPP EEDPEEQAEE NPEGEQPEEC FTEACVQRFP CLSVDISQGR GKMWWTLRRA
     CFKIVEHHWF KTFNSSLILL NSGTLAFEDI YIEQRRVIRT ILEYADKVFT YIFIMEMLLK
     WVAYGFKVYF TNAWCWLDFL IVDVSIISLV ANWLGYSELG PIKSLRTLRA LRPLRALSRF
     EGMRVVVNAL LGAIPSIMNV LLVCLIFWVI FSIMGVNLFA AKIYYFINTT TSERFDISGV
     NNKSECESLI HTGQVRWLNV KVNYDNVGLG YLSLLQVATF KGWMDIMYSA VDSREQEEQP
     QYEVNIYMYL YFVIFIIFGS FFTINSLIRL IIVNFNQQKK KLGGKDIFMT EEQKKYYNAM
     KKLGSKKPQK PIPRPQNKIQ GMVYDFVTKQ VFDITIMILI CLNMVTMMVE TDDQSQLKVD
     ILYNINMVFI IVFTGECVLK MFALRQNYFT VGWNIFDFVV VILSIVGLAL SDLIQKYFVS
     PTLFRVIRLA RIGRVLRLIR GAKGIRTLLF ALMMSLPALF NIGLLLILVM FIYSIFGMSN
     FAYVKKESGI DDMFNFETFG NSIICLFEIT TSAGWDGLLN PILNSGPPDC DPTLENPGTS
     VRGDCGNPSI GICFFCSYII ISFLIVVNMY IAIILENFNV ATEESSDPLG EDDFEIFFEK
     WEKFGPDATQ FIDYSRLSDF VDTLQEPLRI AKPNKIKLIT LDLPMVPGDK IHCLDILFAL
     TKEVLGDSGE MDALKETMEE KFMAANPSKV SYEPITTTLK RKQEEVCAIK IQRAYRRHLL
     QRSVKQASYM YRHSQDGSGD GAPEKEGLIA NTMSKMYGRE NGNSGVQNKG EERGSTGDAG
     PTMGLTPINP SDSALPPSPP PGLPLHPGVK ESLV
//
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