ID H9G4U9_ANOCA Unreviewed; 1974 AA.
AC H9G4U9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 3.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=LOC100560075 {ECO:0000313|Ensembl:ENSACAP00000001152.4};
OS Anolis carolinensis (Green anole) (American chameleon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Iguania; Dactyloidae; Anolis.
OX NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000001152.4, ECO:0000313|Proteomes:UP000001646};
RN [1] {ECO:0000313|Ensembl:ENSACAP00000001152.4}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000001152.4};
RG The Genome Sequencing Platform;
RA Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACAP00000001152.4}
RP IDENTIFICATION.
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 RefSeq; XP_008113347.1; XM_008115140.2.
DR STRING; 28377.ENSACAP00000001152; -.
DR Ensembl; ENSACAT00000001184.4; ENSACAP00000001152.4; ENSACAG00000000353.4.
DR GeneID; 100560075; -.
DR KEGG; acs:100560075; -.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000157130; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; H9G4U9; -.
DR OrthoDB; 1110761at2759; -.
DR TreeFam; TF323985; -.
DR Proteomes; UP000001646; Unplaced.
DR Bgee; ENSACAG00000000353; Expressed in ovary and 4 other cell types or tissues.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
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:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
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 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 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:UP000001646};
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 127..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 194..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 225..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 390..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 855..883
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 942..968
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1184..1203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1224..1246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1301..1327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1420..1446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1505..1523
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1535..1553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1560..1585
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1622..1650
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1726..1749
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 546..694
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 744..973
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 983..1179
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1183..1455
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1504..1759
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 36..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1929..1974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 414..462
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 36..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..516
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1949..1974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1974 AA; 224936 MW; 524716A4025D9686 CRC64;
MAQALLSPPG PNCFFRFTHE SLAAIEKRIA DERKRVKVEQ DQWEEGSDDA KPKPNRDLEA
GKSLPFIYGD IPPGMVSEPL EDLDPYYANK KTFIVLNKGK TIFRFSATPS LYLLSPFSIL
RRISIKIFVH SLFSMFIMLT ILANCVVMTQ TEPKWGKSVE YTFTAIYTFE SLVKIFARGF
CIDDFTFLRD PWNWLDFLVI SFAYITEFVN LGNVSALRTF RVLRALKTIS VIPGLKTIVG
ALIQSVKKLS DVMILTVFCL SVFALIGLQL FMGNLRHKCL LWPHNNSSYL DPRFREYYNE
TKLLWSKYIE SSENFYTLDP TKDPLICGNS SDAGQCPEGY TCVKAGRNPN YGYTSFDTFS
WAFLTLFRLM TQDYWENLYQ LTLRAAGKGY MVFFVLVIFL GSFYLVNLIL AVVAMAYEEQ
NQANIEEAER KEAEYQQMLE QLKRQQEEAQ AIAAACRDAR DDVALGRLSE TSSQLSRLSS
KSAKERRNRR KKRRQRELSL GDEKVDSKKI PKSESDGSIK KKAFRFSLEG NRLTYDTRTI
SPYQSMLFPT RRSSRASFSS FKGPTTEGGS DADSEHSTFE DNASRNGSFF VIRRPSERRS
SNISQTMLPV FSMNGKMHSS VDCNGVVSLV GGPPALLSPI GQLLPEVIVD KATTDDSSTA
SETGSRKRRS SSFQIPMDLL EDPTVRERAM SIASIITNTM EELEESRQKC PPCWYKFAHT
CLIWDCSSAW IEVKKVVYFI VMDPFVDLGI TICIVANTVF MALEHYPSDK AFSDVLKNGN
LVFTGIFTAE MVLKIIAMDP YYYFQVGWNI FDSIIVSLSL MELGLSNIDG LSVLRSFRLL
RVFKLAKSWP TLNMLIKIIG NSVGALGNLT LVLAIIVFIF AVVGMQLFGK QYEACKCKIS
NDCTLPRWHM NDFYHSFLIV FRVLCGEWIE TMWDCMEVAG QAMCLVVFMM VMVIGNLVVL
NLFLALLLSS FSSDSLAAPE QETEVNNLQI AVARIRRGIS IVKRKIIEFI QITILQKCRP
STGVDSTDKQ NNMQGGCIPN HTVAEINKAL DYCIEKTASS IIYMDSADQM SFINNPNLTV
TVPIAVGESD FEHINTEELS SISELEESKE MLSICSSTEA STVNLAIAGE NKDESSEEDT
SQPKPCFTEG CVRKFKCCQV SIESGKGKFW WNLRKTCYRI VEHSWFETFI VFMILLSSGA
LAFEDIYIEQ RKTIKIILEY ADKVFTYIFI LEMLLKWVSY GFQVYFTNAW CWLDFLIVDV
SIVSLIANAL DYAELGPIKS LRTLRALRPL RALSRFEGMK VVVNALIGAI PSIMNVLLVC
LIFWLIFSIM GVNLFAGTFY HCVNKTDGAM LSHKEFPFKN VCESMSDVAR WKNVKVNYDN
VGAGYLSLLQ VATFKGWMDI MYAAVDSTGV EKQPEYEASW FMYMYFVVFI IFGSFFTLNL
FIGVIIDNFN QQKKKLGGQD IFMTEEQKKY YNAMKKLGNK KPQKPIPRPA NKVQGFIFDF
VTRQAFDIGI MSLICLNMVT MMVETDDEDE SKKKILYWIN VIFIILFTGE FLLKLIALRY
YYFTIGWNIF DFVVVILSFI GMFLSELIEK YFVSPTLFRV IRLARIGRIL RLIKGAKGIR
TLLFALMMSL PALFNIGLLL FLVMFIYAIF GMSQFAYVKK EVGIDDMFNF ETFPNSMICL
FQITTSAGWA ELLSPILNSG PPDCDPNMVH TGSLVRGDCG NPSVGIFFFV SYIIISFLVV
VNMYIAVILE NFSVATEESA EPLDEDDFER FYEVWEKFDP DATQFIEYHQ LFDFAASLDP
PLLIPKPNHV QLISMDLPMV SGDRIHCLDI LFAFTKRVLG ESEEMDLLRV QMEERFMKAN
PSKKSYEPIT TTMKRKLEED SAKVIQRAFR GYRLRKPVHN TTFIYDNDDD FPARKNMLAD
KFSLNLALEK AEQSSSSTTS PPSYDSVTKT DKYEQEKSEK EEKDKDGKYS RNYK
//
