ID A0A286Y3I8_CAVPO Unreviewed; 2015 AA.
AC A0A286Y3I8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN5A {ECO:0000313|Ensembl:ENSCPOP00000032395.1};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000032395.1, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000032395.1}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000032395.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR EMBL; AAKN02049251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02049252; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005001164.1; XM_005001107.2.
DR STRING; 10141.ENSCPOP00000032395; -.
DR Ensembl; ENSCPOT00000044055.1; ENSCPOP00000032395.1; ENSCPOG00000005240.4.
DR GeneID; 100723340; -.
DR CTD; 6331; -.
DR VEuPathDB; HostDB:ENSCPOG00000005240; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000161691; -.
DR InParanoid; A0A286Y3I8; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000005240; Expressed in heart left ventricle and 4 other cell types or tissues.
DR GO; GO:0005901; C:caveola; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0030315; C:T-tubule; IEA:Ensembl.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0030506; F:ankyrin binding; IEA:Ensembl.
DR GO; GO:0005516; F:calmodulin binding; IEA:Ensembl.
DR GO; GO:0017134; F:fibroblast growth factor binding; IEA:Ensembl.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:0086060; F:voltage-gated sodium channel activity involved in AV node cell action potential; IEA:Ensembl.
DR GO; GO:0086061; F:voltage-gated sodium channel activity involved in bundle of His cell action potential; IEA:Ensembl.
DR GO; GO:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; IEA:Ensembl.
DR GO; GO:0086063; F:voltage-gated sodium channel activity involved in SA node cell action potential; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0098912; P:membrane depolarization during atrial cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IEA:Ensembl.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0060372; P:regulation of atrial cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0086004; P:regulation of cardiac muscle cell contraction; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:1902305; P:regulation of sodium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0060373; P:regulation of ventricular cardiac muscle cell membrane depolarization; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR008053; Na_channel_a5su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF206; SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PRINTS; PR01666; NACHANNEL5.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 230..247
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 388..416
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 714..732
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 744..765
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 777..794
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 834..857
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 877..894
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 914..937
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1203..1222
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1243..1259
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1271..1292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1320..1346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1442..1468
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1527..1545
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1557..1575
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1587..1607
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1644..1672
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1747..1770
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 130..422
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 512..663
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 714..943
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 951..1198
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1202..1477
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1526..1780
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 27..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2015
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 413..451
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 480..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1052..1066
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1993
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2015 AA; 227802 MW; 0E2DA7B464EEF1F0 CRC64;
MANFLLPRGT SSFRRFTRES LAAIEKRMAE KQARGSATSQ ESREGLPEEE APRPQLDLQA
SKKLPDLYGN PPRELIGEPL EDLDPFYSTQ KTFIVLNKGK TIFRFSATNA LYILSPFHPV
RRAAVKILVH SLFSMLIMCT ILTNCVFMAQ HDPPPWTKYV EYTFTAIYTF ESLVKILARG
FCLHAFTFLR DPWNWLDFSV IIMAYTTEFV DLGNVSALRT FRVLRALKTI SVISGLKTIV
GALIQSVKKL ADVMVLTVFC LSVFALIGLQ LFMGNLRHKC VRNFTALNDT NGSVEAEGLV
WKSLDLYLRD PVNYLLKNGT SDVLLCGNSS DAGTCPEGYR CLKAGDNPDH GYTSFDSFAW
AFLALFRLMT QDCWERLYQQ TLRSAGKIYM IFFMLVIFLG SFYLVNLILA VVAMAYEEQN
QATIAETEEK EKRFQEAMEM LKKEHEALTI RGVDTVSRSS LEMSPLAPVT NHERRSKRRK
RMSSGTEECG DERFPKSDSE DGPRAMNHRS LSRTSVKPRS SRGSIFTFRR RDLGSETDFA
DDENSTAGDS ESHRTSLLVP WPLHRPSAQG QPSPVASAPS HVFNSKRNST VDCNGVVSLL
GAGDTEAMSP GSRLLRPMML ERPPDTTTPS EEPGGPQMLT PQAPCADGFE EPGARQRALS
AVSVLTSVLE ELEESHRKCP PCWIRFAKRY LIWECCPLWI SIKQKVKFVV MDPFADLTIT
MCIVLNTLFM ALEHYNMTTE FEEMLQVGNL VFTGIFTAEM TFKIIALDPY YYFQQGWNIF
DSIIVILSLM ELGLSRMGNL SVLRSFRLLR VFKLAKSWPT LNTLIKIIGN SVGALGNLTL
VLAIIVFIFA VVGMQLFGKN YSELRHRISD SDLLPRWHMM DFFHAFLIIF RILCGEWIET
MWDCMEVSGQ SLCLLVFLLV MVIGNLVVLN LFLALLLSSF SADNLTAPDE DGEMNNLQLA
LARIQRGLHF LKRTTWDFCC GLLQQRPKKP AAPTAHSQLP SCMTSPRSPP PAEVEKAPPA
RKETRFEESK HPGQGTPGEP EPVCVPIAVA ESDTDDQEEE DENSLGTEEE SSKQQESQPV
SDGPEHPQEP RARSQGSETT TSEAETGVSQ ANWRQQRKAE PQAPGSSETH EDSYSEGSTA
DMTNTADLLE QIPDLGEDVK DPEDCFTEGC VQRCPCCAVD TTQAPGKVWW RLRKTCYRIV
EHSWFETFII FMILLSSGAL AFEDIYLEER KTIKVLLEYA DKMFTYVFVL EMLLKWVAYG
FKKYFTNAWC WLDFLIVDVS LVSLVANTLG FAEMGPIKSL RTLRALRPLR ALSRFEGMRV
VVNALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFGR CINQTEGDLP LNYTIVNNKS
ECKSFNMTGE LYWTKVKVNF DNVGAGYLAL LQVATFKGWM DIMYAAVDSR GYEEQPQWEY
NLYMYIYFVV FIIFGSFFTL NLFIGVIIDN FNQQKKKLGG QDIFMTEEQK KYYNAMKKLG
SKKPQKPIPR PVNKYQGFLF DIVTKQAFDV TIMFLICLNM VTMMVETDDQ SPEKVNILAK
INLLFVAIFT GECIVKMTAL RHYYFTNSWN IFDFVVVILS IVGTVLSDII QKYFFSPTLF
RVIRLARIGR ILRLIRGAKG IRTLLFALMM SLPALFNIGL LLFLVMFIYS IFGMANFAYV
KWEAGIDDMF NFQTFANSML CLFQITTSAG WDGLLSPILN TGPPYCDPNL PNNNGSRGNC
GSPAVGILFF TTYIIISFLI VVNMYIAIIL ENFSVATEES TEPLSEDDFD MFYEIWEKFD
PEATQFIEYS ALSDFADALS EPLRIAKPNQ ISLINMDLPM VSGDRIHCMD ILFAFTKRVL
GESGEMDALK IQMEEKFMAA NPSKISYEPI TTTLRRKHEE VSATVIQRAF RRHLLQRSMK
HASFLFRQQA GSGGLSEEDA PEREGLIAYM MNENFSRHDR PASSSSISST SFPPSYDSVT
RATSDNLQVR VSDYSHSEDL ADFPASPERD RESIV
//
