ID H2NHB7_PONAB Unreviewed; 1980 AA.
AC H2NHB7; A0A2J8SXQ4;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN8A {ECO:0000313|Ensembl:ENSPPYP00000005169.2};
GN ORFNames=CR201_G0039418 {ECO:0000313|EMBL:PNJ25549.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000005169.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000005169.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ25549.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ25549.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000005169.2}
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 EMBL; NDHI03003535; PNJ25549.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000005169; -.
DR Ensembl; ENSPPYT00000005370.2; ENSPPYP00000005169.2; ENSPPYG00000004530.3.
DR eggNOG; KOG2301; Eukaryota.
DR GeneTree; ENSGT00940000156263; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR TreeFam; TF323985; -.
DR Proteomes; UP000001595; Chromosome 12.
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; IPR008054; Na_channel_a8su.
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:SF23; SODIUM CHANNEL PROTEIN TYPE 8 SUBUNIT ALPHA; 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 PRINTS; PR01667; NACHANNEL8.
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 Reference proteome {ECO:0000313|Proteomes:UP000001595};
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 128..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 387..414
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 754..772
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 784..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 864..892
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 951..977
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1199..1217
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1238..1257
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1269..1292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1313..1341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1438..1464
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1523..1541
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1553..1571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1583..1603
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1640..1668
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1743..1766
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 131..420
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 546..702
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 753..983
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 991..1192
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1197..1473
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1522..1776
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 28..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1107..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1922..1980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..530
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..602
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1980
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1980 AA; 225239 MW; 0510CF3CDC2592F0 CRC64;
MAARLLAPPG PDSFKPFTPE SLANIERRIA ESKLKKPPKA DGSHREDDED SKPKPNSDLE
AGKSLPFIYG DIPQGLVAVP LEDFDPYYLT QKTFVVLNRG KTLFRFSATP ALYILSPFNL
IRRIAIKILI HSVFSMIIMC TILTNCVFMT FSNPPDWSKN VEYTFTGIYT FESLVKIIAR
GFCIDGFTFL RDPWNWLDFS VIMMAYVTEF VDLGNVSALR TFRVLRALKT ISVIPGLKTI
VGALIQSVKK LSDVMILTVF CLSVFALIGL QLFMGNLRNK CVVWPINFNE SYLENGTKGF
DWEEYINNKT NFYTVPGMLE PLLCGNSSDA GQCPEGYQCM KAGRNPNYGY TSFDTFSWAF
LALFRLMTQD YWENLYQLTL RAAGKTYMIF FVLVIFVGSF YLVNLILAVV AMAYEEQNQA
TLEEAEQKEA EFKAMLEQLK KQQEEAQAAA MATSAGTVSE DAIEEEGEEG GGSPRSSSEI
SKLSSKSAKE RRNRRKKRKQ KELSEGEEKG DPEKVFKSES EDGMRRKAFR LPDNRIGRKF
SIMNQSLLSI PGSPFLSRHN SKSSIFSFRG PGRFRDPGSE NEFADDEHST VEESEGRRDS
LFIPIRARER RSSYSGYSGY SQGSRSSRIF PSLRRSVKRN STVDCNGVVS LIGGPGSHIG
GRLLPEATTE VEIKKKGPGS LLVSMDQLAS YGRKDRINSI MSVVTNTLVE ELEESQRKCP
PCWYKFANTF LIWECHPYWI KLKEIVNLIV MDPFVDLAIT ICIVLNTLFM AMEHHPMTPQ
FEHVLAVGNL VFTGIFTAEM FLKLIAMDPY YYFQEGWNIF DGFIVSLSLM ELSLADVEGL
SVLRSFRLLR VFKLAKSWPT LNMLIKIIGN SVGALGNLTL VLAIIVFIFA VVGMQLFGKS
YKECVCKINQ DCELPRWHMH DFFHSFLIVF RVLCGEWIET MWDCMEVAGQ AMCLIVFMMV
MVIGNLVVLN LFLALLLSSF SADNLAATDD DGEMNNLQIS VIRIKKGVAW TKLKVHAFMQ
AHFKQREADE VKPLDELYEK KANCIANHTG ADIHRNGDFQ KNGNGTTSGI GSSVEKYIID
EDHMSFINNP NLTVRVPIAV GESDFENLNT EDVSSESDPE GSKDKLDDTS SSEGSTIDIK
PEVEEVPVEQ PEEYLDPDAC FTEGCVQRFK CCQVNIEEGL GKSWWILRKT CFLIVEHNWF
ETFIIFMILL SSGALAFEDI YIEQRKTIRT ILEYADKVFT YIFILEMLLK WTAYGFVKFF
TNAWCWLDFL IVAVSLVSLI ANALGYSELG AIKSLRTLRA LRPLRALSRF EGMRVVVNAL
VGAIPSIMNV LLVCLIFWLI FSIMGVNLFA GKYHYCFNET SEIRFEIEDV NNKTECEKLM
EGNNTEIRWK NVKINFDNVG AGYLALLQVA TFKGWMDIMY AAVDSRKPDE QPKYEDNIYM
YIYFVIFIIF GSFFTLNLFI GVIIDNFNQQ KKKFGGQDIF MTEEQKKYYN AMKKLGSKKP
QKPIPRPLNK IQGIVFDFVT QQAFDIVIMM LICLNMVTMM VETDTQSKQM ENILYWINLV
FVIFFTCECV LKMFALRHYY FTIGWNIFDF VVVILSIVGM FLADIIEKYF VSPTLFRVIR
LARIGRILRL IKGAKGIRTL LFALMMSLPA LFNIGLLLFL VMFIFSIFGM SNFAYVKHEA
GIDDMFNFET FGNSMICLFQ ITTSAGWDGL LLPILNRPPD CSLDKEHPGS GFKGDCGNPS
VGIFFFVSYI IISFLIVVNM YIAIILENFS VATEESADPL SEDDFETFYE IWEKFDPDAT
QFIEYCKLAD FADALEHPLR VPKPNTIELI AMDLPMVSGD RIHCLDILFA FTKRVLGDSG
ELDILRQQME ERFVASNPSK VSYEPITTTL RRKQEEVSAV VLQRAYRGHL ARRGFICKKT
TSNKLENGGT HREKKESTPS TASLPSYDSV TKPEKEKQQR AEEGRREKAK RQKEVRESKC
//
