ID S4RRT3_PETMA Unreviewed; 1955 AA.
AC S4RRT3;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000007920.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|EMBL:QBP05222.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30878501;
RA Northcutt A.J., Hough R.A., Frese A.N., McClellan A.D., Schulz D.J.;
RT "Genomic discovery of ion channel genes in the central nervous system of
RT the lamprey Petromyzon marinus.";
RL Mar. Genomics 0:0-0(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMAP00000007920.1}
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; MH726126; QBP05222.1; -; mRNA.
DR STRING; 7757.ENSPMAP00000007920; -.
DR Ensembl; ENSPMAT00000007955.1; ENSPMAP00000007920.1; ENSPMAG00000007100.1.
DR GeneTree; ENSGT00940000163423; -.
DR HOGENOM; CLU_000540_5_0_1; -.
DR OMA; NYANENT; -.
DR Proteomes; UP000245300; Unplaced.
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 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; 3.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR010526; Na_trans_assoc_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR013122; PKD1_2_channel.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF298; SODIUM CHANNEL PROTEIN; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 3.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR Pfam; PF08016; PKD_channel; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
PE 2: Evidence at transcript level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132, ECO:0000313|EMBL:QBP05222.1};
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:UP000245300};
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 130..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 387..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 748..771
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 783..801
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 862..891
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 950..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1203..1221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1242..1261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1267..1290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1334..1353
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1403..1426
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1438..1457
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1496..1516
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1597..1625
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1698..1724
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 130..416
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 539..701
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 752..981
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 990..1197
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1201..1457
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1583..1728
FT /note="Polycystin cation channel PKD1/PKD2"
FT /evidence="ECO:0000259|Pfam:PF08016"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1106..1137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1912..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 467..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1912..1933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1938..1955
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1955 AA; 221189 MW; 251832CB19531475 CRC64;
MAAPVLLPPG PHSLRRFTPE SLAAIEQRAA HEQAKKAKGF ESEDDQPKPS SDLEVGKSLP
FMYGDMPPEC VAEPLEDLDP FYSTQKTFIV LNSGKAIFRF SATPALYILT PFNPVRRYAI
KILTHSWQRT LFSIFIMFTI LTNCVFMTMS EPPTWTKNVE YTFTGIYTFE SMVKILARGF
CLHPFTFLRD PWNWLDFCVI VMAYVTEFID LGNVSALRTF RVLRALKTIS VIPGLKTIVG
ALIQAVKQLS DVMILTVFCL SVFALIGLQL FMGNLRHKCI LWPIANQTNV TEFNETAEPF
NWENYVNNED NQYKLEGSKD ALLCGNGSDA GSCPEKFVCV KGGRNPNYGY TSFDTFSWAF
LSLFRLMTQD YWENLYQLTL RAAGKPYIFF MVVIFLGSFY LINLILAVVA MAYEKANCLV
YCIALCKMQL CCVLHSELLG CGLPRQGGTA DSEPLSRSSS EESRLSSKSA NESRNQRKKQ
RQKSDSEEGE EKRDDEKIPK SVSEESMLRK PGSLRGSRKY STHRESTPQV SLISMYYKPK
RKSSRTSLLS FREKVRDHNS DNDFADDEQS ELQSMAGEAG SRRNSLFVPQ RGHGERRNSQ
GSKLSWAGPN PPILPPLNGK MNVSVDCNGV VSLVDRPAGT SVPNSPPGLL LPEVVIDKAV
TDDNATTETE LLKKRRRGSQ HTSMDLLEEP VIIRNRAYSA ISVLTNTMEE LEESRQNCPP
CWYKFANKYL IWECCSLWMK VKEILKMIVM DPFVDLSITI CIILNTLFMA LEHYPMTPEF
DNALFVGNLV FTGIFTAEMV LKIAAQDPYY YFQQGWNIFD SIIVSLSLME LGLSSVDGLS
VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV VGMQLFGKMY
KECVCKISEN CTLPRWHMHD FFHSFLIVFR VLCGEWIETM WDCMEVAGQA MCLIVFMMVM
VIGNLVVLNL FLALLLSSFS GDNLSATDDD GEMNNLQVAI GRIERGVSFI KRSICDVFRK
ALKRSCDNEE MKALDDLGGL DKMEIYVGNH TGVQGESIVK DGNGVASGAA GVGNSLKNHH
VLDVDRLGFL TNPNLGVRVP IAVGESDFEN RDEEDEKTQK QIGKSEQKLD TVSSSEGSTV
DIQKEGVVEV PVELVEEMME PEECFTEGCL HRFPYCRLDV GTDRGRSWWN LRRACYRIVE
HNWFESVIVF MILLSSGALA FEDIYIEQRK TIKTVLEYAD KVFTYVFILE MLLKWVAYGF
QKYFTNAWCW LDFLIVDISI VSLMATALGY DQLSAIKSLR TLRALRPLRA LSRFEGMRVV
VNALVGAIPS IMNVLLVCLI FWLIFSIMGV NLFSGKYYYC LNKTDGQRLP ISIVDNYSMC
IALNDTTNET LWKNVKVNFD NVGIGYLALL QVATFKGWMD IMYAAVDSRD TRVNVLVVPH
YSTAALIYEM FILACFFHSS LKAHLYRPFS SSTFNSLLSF RKLREPIHSH HNMNNFIVHI
IFFILIAANY TTGAFVSTLN ADHLAVHLPR NYGNAMPGIN IKPVTSMNTR DLCVVRIMLA
DMIQKYFVSP TLFRVIRLAR IGRILRLIRG AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
IYSIFGMSNF AYVKKESGID DMFNFETFGN SMICLFQITT SAGWDGLLAP ILNSGVPDCD
PEIEHPGSLV KGDCGNPMVG IIFFVSYIII SFLVVVNMYI AIILENFSVA TEESSEPLSE
DDFEMFYEIW EKFDPDATQF IAWERLPDFA DALDEPLRVP KPNKIKLIAM DLPMVINDRI
HCLDILFAFT KRVLGEGAGM DALKTQMEDR FMAANPSKTS YEPITTTLRR KQEEVAVRVI
QRAYRRHILH RSLKQASYIY RHRKSDGNIL EEEAPEKDGL IARNMRANFS TDCEYGDSST
ITPPPSFESL ELMDNTNKHG GYNDEDPKER DIEGK
//
