ID A0A3P8QTZ5_ASTCA Unreviewed; 1962 AA.
AC A0A3P8QTZ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSACLP00000032392.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000032392.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000032392.1}
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.ENSACLP00000032392; -.
DR Ensembl; ENSACLT00000033154.1; ENSACLP00000032392.1; ENSACLG00000019651.1.
DR GeneTree; ENSGT00940000154992; -.
DR OMA; FTEMEQD; -.
DR Proteomes; UP000265100; Chromosome 9.
DR Bgee; ENSACLG00000019651; Expressed in ovary and 2 other cell types or tissues.
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 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:SF295; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 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 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|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 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 188..207
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 386..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 698..716
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 728..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 808..836
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 866..884
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 896..921
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1137..1156
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1177..1195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1215..1237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1257..1283
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1371..1394
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1453..1471
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1483..1501
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1508..1533
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1570..1598
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1674..1697
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 125..419
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 517..597
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 697..928
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 935..1132
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1136..1402
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1452..1707
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1016..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1903..1962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1063
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1903..1929
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1962 AA; 223408 MW; AA8CAD7D96922F71 CRC64;
MAGCVFPMGP ESFQRFTPDS LAAIEQRIAQ EESRRNKHYQ EDLGDVELPR PRPDLEAGKQ
LPRIFADIPS HLVGVPLEDI DPYYFKDKRT FIVLNKGKAI FRFSATSALY IFSPFHPIRR
LAIKILVLFI MCTILTNCCF MAMSEPEYWA KYLEYTFTGI YTFESLIKIL ARGFCVGPFT
FLRDPWNWLD FSVIVMAYVT EFVDLGNVSA LRTFRVLRAL KTISVIPGLK TIVGALIQSV
KKLADVMILT VFCLSVFALI GLQLFMGNLR QKCVRSTAHC FNDTLPANTS FYCNNKTWAS
IKDFTEHEDN FYKVEGAKDA LICGNSSDAG KCPDGFVCLK AGRNPNYGYT SFDTFGWAFL
SLFRLMTQDY WENLYHQTLR SAGKTYMVFF VVVIFLGSFY LVNLILAVVA MAYEEQNQAT
IAEACQKERE FQQAMEILKK EQQGATQKAT DSDSLMSPDL SPFGQPMDSF EERRRSQALM
GVGDVEANLS EEKLLQVDLT DGGKPLHPLL ARSFSTRTRR SSQVSSIFNF RLRSRGSEGE
MADDEYSVPG TFSGILPQPW PKRRPSTYST ASRSSQVFYP TLNINGKLFV AMDQNGVSPP
PLQGQLPACT MEKVKEESVS SLSTMLLPRP SSMQDSERRG RAMSAASYLT DVMEELEESH
KKCHPCWYTF AHHYLVWECC PMWLKVKQLV KIMVMDPFLD LAITVCIVLN TLFMAMEHYP
MTDEFNGMLT IGNLVFSGIF TAEMVLKIIA LDPYYYFQTG WNIFDSIIVC LSLMELGLSD
VEGLSVLRSF RLLRVFKLAR SWPTLNTLIK IIGNSMGALG NLTLVLAIIV FIFAVVGMQL
FGKNYQECVC KISKDCTLPR WHMKDFFHSF LIVFRVLCGE WIETMWDCME VAGQPLCILV
FMLVMVIGNL VLLNLFLALL LSSFSSDNLS APDDDGEMNN LHIAIHRITR GLAWCRRQVV
DFFNGNLKRR RQKRKEAKAM MKLKRLSTIH TEANGAVIGR HVEKYVVPED DSYMTNPNLT
ISVPIAPGES DVEFPEEEED GEGEEEQTEG SEEEEEEERE EPKDDISLSE GSTVDLRKPG
EEEDEYSEMA EEAMDPDNCF PDMCVARFQC CDIDTTVGLG QMWWRTRKTC YQIVEHSWFE
TFIIFMILLS SGALAFEDIY IEQRRVIKVV LEYADKIFTY IFILEMLLKW LAYGFKKYFT
NYWCWLDFLI VDVMLGLMAH LVANTLGYSD LAAIKSLRTL RALRPLRALS RFEGMRVVVN
ALIGAIPSIM NVLLVCLIFW LIFSIMGVNL FAGKFGRCVN STGQVYDASA ITNKSQCETH
NDTSTHYWSK VKVNFDNVGA GYLALLQVKQ IRVFPEQVEE QPIKEINLYM YLYFVIFIIF
GSFFTLNLFI GVIIDNFNQQ KRKIRGQDIF MTEEQKKYYN AMKKLGSKKP QKPIPRPMNA
LQGFFFDLVG KQAFDIIIMV LILFNMITMM VETDEQPPQM EKILNNINLA FIIFFTAECL
IKIMALRCYF FTVGWNIFDF VVVILSIVGI VLADIIEKYF VSPTLFRVIR LARIGRILRL
IRGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIYAIFGM ANFAYVKRQG GIDDMFNFET
FGNSMICLFQ ITTSAGWDSL LNPILNNSPE ECDANIPHTG TTVRGNCGNP SVGITFFVTY
IIISFLIVVN MYIAIILENF SVATEESTEP LSEDDFEMFY EVWEKFDPEA TQFIEYSKLS
DFADSLLEPL RIAKPNKIKL ISMDLPMVSG DKIHCLDILF AFTKRVLGES GEMDALKQQM
EEKFMMANPS KISYEPITTT LRRKQEEVSA TIIQRCYRRH LVRRQLKAAS YMYRQITTPR
HAGGEGEQGG EVVFGEDAPE KEGLIATMMR ENYGSSMLGI ERSETISSTS SPPSYDSVTR
ATSEIFQPLA VKTETVADTA GSEQSEQSQS EITHDRQQEM TP
//
