ID A0A3P8RB37_ASTCA Unreviewed; 2030 AA.
AC A0A3P8RB37;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000038191.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000038191.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000038191.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 STRING; 8154.ENSACLP00000038191; -.
DR Ensembl; ENSACLT00000039082.1; ENSACLP00000038191.1; ENSACLG00000025753.1.
DR GeneTree; ENSGT00940000163423; -.
DR OrthoDB; 1110761at2759; -.
DR Proteomes; UP000265100; Chromosome 23.
DR Bgee; ENSACLG00000025753; Expressed in brain and 2 other cell types or tissues.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
DR GO; GO:0006110; P:regulation of glycolytic process; IEA:Ensembl.
DR GO; GO:1904059; P:regulation of locomotor rhythm; IEA:Ensembl.
DR GO; GO:0002082; P:regulation of oxidative phosphorylation; IEA:Ensembl.
DR GO; GO:0036269; P:swimming behavior; IEA:Ensembl.
DR GO; GO:0099536; P:synaptic signaling; 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; IPR000048; IQ_motif_EF-hand-BS.
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:SF237; SODIUM CHANNEL PROTEIN TYPE 3 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 SMART; SM00015; IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|ARBA:ARBA00023303, 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 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 Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT TRANSMEM 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 224..245
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 414..441
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 769..787
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 799..822
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 879..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 969..992
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1238..1256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1277..1296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1308..1328
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1354..1380
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1476..1499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1558..1576
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1588..1606
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1618..1638
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1675..1703
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1779..1802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 128..447
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 568..718
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 768..998
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1006..1231
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1236..1508
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1557..1812
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 28..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..2004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2030 AA; 230103 MW; 1C6AC558DDF43748 CRC64;
MAQLLIPPGP DSFRPFVPES LAAIERRIAE EEAQRPRVER RSDSDDENGP KPNSDVEAGK
SLPFIYGDIP PGLVSTPLED IDPYYSSQKT FIVLNRGKAI FRFNATPALY ILSPFNPLRR
IAIKVLVHSM FSILIMFTIL TNCAFMTLSN PPDWAKNVEY TFTGIYTFES LIKILARGFC
VGKFTFLRDP WNWLDFSVIL MAYITEFVNL GNVSALRTFR VLRALKTISV IPGLKTIVGA
LIQSVKKLSD VMILTVFCLS VFALIGLQLF MGNLRQKCVR IPLGSNTTLN NTHESNNTLV
ENITLVENVT FMENITKNSF DWIEYINDER NYYYLPGRRD ALLCGNGSGA GSQVRLSRVC
PEGFSCLKAG RNPDYGYTSF DTFSWAFLSL FRLMTQDYWE NLYQQTLRAA GKPYMIFFVL
VIFLGSFYLV NLILAVVAMA YDEQNQATIE EAQQKEEEFQ AMLEQLKRQQ EEAQVAAAAA
TESGEYSGRG RPTSESSSGT SKLSSKSAKE RRNRRKKRKQ REEEEERGCR DKFHKSESED
SIKRSSFRFS IDANRLSYEK RCSSPNQSLL SIRGSIFSPR RNSRASLFSF RGRARDMGSE
NDFADDEHST FEESDSRRGS LFLPRRLERR CSAVSQTSLG APRIMLPANG KMHCAVDCNG
VVSLVGGTSV TTSPVGLLLP EGTTTDTELK KRRSGFHQPS MDYLNEPGGR QRAMSVASIL
TNTMEELEES RQKCPPCWYR FANTGLIWDC CPAWLKIKEI VSMVVMDPFV DLAITICIVL
NTLFMAMEHY PMTEEFDNVL SVGNLVFTGI FTAEMCFKII ALDPYYYFQE GWNIFDGIIV
SLSLMELGLA NVEGLSVLRS FRLLRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII
VFIFAVVGMQ MFGKNYKECV CKISEDCMLP RWHMHDFFHS FLIVFRVLCG EWIETMWDCM
EVAGQTMCLI VFMMVMVIGN LVVLNLFLAL LLSSFSADNL AATDEDSEMN NLQIAVGRIQ
RGIAFVKNAV RQFLQSLCFG RGGKGSGLAE ESKPLDELHS NGKGNCISNH TTVEITKDPS
GVYMREGNGR PGGLVVGVSV GRDSTGKYPV EDCDYMSFIH NPSLTVTVPI AVGESDFENL
NTEDFSSDSS DVEGSKEKLD VEPQPLSSSE GSTVDIRPPG DGVDSVELEP EESLDPEACF
TEGCVRRFQC CQISEEGDKF KSWWTLRKTC FIIVEHNWFE SFIIFMILLS SGALAFEDIY
IEQRRTIKTV LEYADKVFTY VFILEMLLKW VAYGFVKYFT NAWCWLDFLI VDVSLVSLVA
NALGYSELSA IKSLRTLRAL RPLRALSRFE GMRVVVNALL GAIPSIMNVL LVCLIFWLIF
SIMGVNLFAG KYYYCVNATT DEPFPSEVVN NKSDCLSLND SARWKNVKIN FDNVGAGYLA
LLQVATFKGW MDIMYAAVDS RDLEEQPKYE VNLYMYLYFV IFIIFGSFFT LNLFIGVIID
NFNQQKKKLG GQDIFMTEEQ KKYYNAMKKL GSKKPQKPIP RPTNAFQGCV FDFITKQAFD
IVIMILICLN MVTMMVETDA QTKEMDHILY WINLVFIVLF TGECVLKMIS LRHYYFTIGW
NIFDFVVVIL SIVGMFLSEV IEKYFVSPTL FRVIRLARIG RILRLIKGAK GIRTLLFALM
MSLPALFNIG LLLFLVMFIY AIFGMSNFAY VKREAGIDDM FNFETFGNSM ICLFQITTSA
GWDGLLAPIL NKRDPDCESQ LEHPGNSYKG NCGNPSVGIF FFVSYIIICF LIVVNMYIAV
ILENFSVATE ESAEPLSEDD FEMFYEVWER FDPDATQFVA YSKLSDFADA LDPPLRIPKP
NMIQLISMDL PMVSGERIHC LDILFAFTKR VLGEGGEMDM LRGQMEDRFM ASNPSKVSYE
PITTTLRRKQ EEMSAIIIQR AFRRYMIRLA MKKASALYKE QLKEGMHDPD KDVMVISKFN
ENSTSEKMDM TPSTASPPSY NSVTKSDKDK YEKENREREN KAKDLKDRKK
//