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Database: UniProt
Entry: SCNAA_CANLF
LinkDB: SCNAA_CANLF
Original site: SCNAA_CANLF 
ID   SCNAA_CANLF             Reviewed;        1962 AA.
AC   O46669;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-OCT-2017, entry version 103.
DE   RecName: Full=Sodium channel protein type 10 subunit alpha;
DE   AltName: Full=NaNG;
DE   AltName: Full=Sodium channel protein type X subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.8;
GN   Name=SCN10A;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=Mongrel; TISSUE=Nodose ganglion;
RX   PubMed=9427539; DOI=10.1016/S0378-1119(97)00433-2;
RA   Chen J., Ikeda S.R., Lang W., Isales C.M., Wei X.;
RT   "Molecular cloning of a putative tetrodotoxin-resistant sodium channel
RT   from dog nodose ganglion neurons.";
RL   Gene 202:7-14(1997).
CC   -!- FUNCTION: Tetrodotoxin-resistant channel that mediates the
CC       voltage-dependent sodium ion permeability of excitable membranes.
CC       Assuming opened or closed conformations in response to the voltage
CC       difference across the membrane, the protein forms a sodium-
CC       selective channel through which sodium ions may pass in accordance
CC       with their electrochemical gradient. Plays a role in neuropathic
CC       pain mechanisms (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The channel consists of an ion conducting pore forming
CC       alpha-subunit regulated by one or more associated auxiliary
CC       subunits SCN1B, SCN2B and SCN3B; electrophysiological properties
CC       may vary depending on the type of the associated beta subunits.
CC       Found in a number of complexes with PRX, DYNLT1 and PDZD2.
CC       Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10
CC       and many others (By similarity). Interacts with NEDD4 and NEDD4L.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the
CC       cell membrane through association with S100A10. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in nodose ganglia, but not in
CC       cortex, hippocampus, cerebellum, liver, heart and skeletal muscle.
CC       {ECO:0000269|PubMed:9427539}.
CC   -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC       hydrophobic segments (S1, S2, S3, S5, S6) and one positively
CC       charged segment (S4). Segments S4 are probably the voltage-sensors
CC       and are characterized by a series of positively charged amino
CC       acids at every third position. {ECO:0000305}.
CC   -!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis.
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-1458 by PKC in a highly conserved
CC       cytoplasmic loop slows inactivation of the sodium channel and
CC       reduces peak sodium currents. {ECO:0000250}.
CC   -!- PTM: Lacks the cysteine which covalently binds the conotoxin
CC       GVIIJ. This cysteine (position 825) is speculated in other sodium
CC       channel subunits alpha to be implied in covalent binding with the
CC       sodium channel subunit beta-2 or beta-4.
CC       {ECO:0000250|UniProtKB:P15389}.
CC   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.8/SCN10A subfamily. {ECO:0000305}.
DR   EMBL; U60590; AAC39164.1; -; mRNA.
DR   RefSeq; NP_001003203.1; NM_001003203.1.
DR   UniGene; Cfa.3714; -.
DR   ProteinModelPortal; O46669; -.
DR   SMR; O46669; -.
DR   STRING; 9615.ENSCAFP00000011447; -.
DR   PaxDb; O46669; -.
DR   PRIDE; O46669; -.
DR   GeneID; 477026; -.
DR   KEGG; cfa:477026; -.
DR   CTD; 6336; -.
DR   eggNOG; KOG2301; Eukaryota.
DR   eggNOG; ENOG410XNP6; LUCA.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; O46669; -.
DR   KO; K04842; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; IBA:GO_Central.
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:0019233; P:sensory perception of pain; IEA:InterPro.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028809; Na_channel_a10su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF208; PTHR10037:SF208; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
PE   2: Evidence at transcript level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Phosphoprotein;
KW   Reference proteome; Repeat; Sodium; Sodium channel; Sodium transport;
KW   Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW   Voltage-gated channel.
FT   CHAIN         1   1962       Sodium channel protein type 10 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048506.
FT   TOPO_DOM      1    125       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    126    149       Helical; Name=S1 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    150    154       Extracellular. {ECO:0000305}.
FT   TRANSMEM    155    174       Helical; Name=S2 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    175    187       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    188    206       Helical; Name=S3 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    207    212       Extracellular. {ECO:0000305}.
FT   TRANSMEM    213    232       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000255}.
FT   TOPO_DOM    233    248       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    249    272       Helical; Name=S5 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    273    350       Extracellular. {ECO:0000305}.
FT   INTRAMEM    351    375       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    376    382       Extracellular. {ECO:0000305}.
FT   TRANSMEM    383    408       Helical; Name=S6 of repeat I.
FT                                {ECO:0000255}.
FT   TOPO_DOM    409    668       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    669    693       Helical; Name=S1 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    694    704       Extracellular. {ECO:0000305}.
FT   TRANSMEM    705    728       Helical; Name=S2 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    729    736       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    737    756       Helical; Name=S3 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    757    762       Extracellular. {ECO:0000305}.
FT   TRANSMEM    763    782       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000255}.
FT   TOPO_DOM    783    798       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    799    819       Helical; Name=S5 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    820    843       Extracellular. {ECO:0000305}.
FT   INTRAMEM    844    864       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    865    873       Extracellular. {ECO:0000305}.
FT   TRANSMEM    874    899       Helical; Name=S6 of repeat II.
FT                                {ECO:0000255}.
FT   TOPO_DOM    900   1154       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1155   1178       Helical; Name=S1 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1179   1191       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1192   1217       Helical; Name=S2 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1218   1223       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1224   1245       Helical; Name=S3 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1246   1249       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1250   1271       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000255}.
FT   TOPO_DOM   1272   1290       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1291   1318       Helical; Name=S5 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1319   1360       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1361   1382       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1383   1398       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1399   1425       Helical; Name=S6 of repeat III.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1426   1478       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1479   1502       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1503   1513       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1514   1537       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1538   1543       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1544   1567       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1568   1579       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1580   1601       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000255}.
FT   TOPO_DOM   1602   1616       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1617   1639       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1640   1653       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1654   1676       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1677   1704       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1705   1729       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000255}.
FT   TOPO_DOM   1730   1962       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      116    414       I. {ECO:0000305}.
FT   REPEAT      656    920       II. {ECO:0000305}.
FT   REPEAT     1147   1456       III. {ECO:0000305}.
FT   REPEAT     1465   1764       IV. {ECO:0000305}.
FT   DOMAIN     1858   1887       IQ.
FT   MOD_RES     450    450       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     453    453       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     476    476       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     488    488       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     621    621       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES     624    624       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q14524}.
FT   MOD_RES    1458   1458       Phosphoserine; by PKC. {ECO:0000250}.
FT   CARBOHYD    284    284       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    288    288       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    321    321       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    344    344       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    828    828       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1319   1319       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1335   1335       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1343   1343       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1693   1693       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    276    328       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    866    875       {ECO:0000250|UniProtKB:D0E0C2}.
SQ   SEQUENCE   1962 AA;  220702 MW;  5D32D20D4AF47A68 CRC64;
     MEFPFGSLET TNFRRFTPES LVEIEKRIAA KQAAKKAKGK HREQKDQEEK PRPQLDLKAC
     NQPPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLDKGRT ISRFSATRAL WLFSPFNLIR
     RTAIKVSVHS WFSLFITVTI LVNCVGMTQT ELPDRIEYVF TVIYTFEALI KILARGFCLN
     EFAYLRDPWD WLDFSVITLA YIGEATALRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
     HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCVKNC AALNETGNYS SYGKQEWNFC
     HRDEDFYYNK PGTSDPLLCG NGSDAGHCPK GYLCLKTSDN PDFNYTSFDS FAWAFLSLFR
     LMTQDSWERL YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQNQATIDEI
     EAKEKTFQET LEMPRKEQEV LAALGIDTAS LHSCNGSPLP SKNASERMRR MKPRVSEGST
     DDNKSPQSDP YNQRRMSFLG LTSGRRRASH GSVFHFRTPC LDTSFPDGVT DDGVFPGDRE
     SHRGSLLLGG GTSQQGPLLR SPLPQPPNPG SGHGEDGHST LPTGELAPGG IEVSAFDAGQ
     KKTFLSAEYL NEPFRAQRAM SVVSIMTSVL EELEESERRC PPCLTSFAQK YLIWECCPTW
     VKLKTVLFGI VTDPFAELTT TLCIVVNTVF MAMEHHGMSS AFEAMLQIGN IVFTVFFTAE
     MVFKIIAFDP YYYFQKRWNI FDCIIVTVSL IELGAARKGS LSVLRTFRLL RVFKLAKSWP
     TLNTLIKIIG NSVGALGNLT IILAIIVFVF ALVGKQLLGE NYRDNRRNIS APNEEWPRWH
     MHDFFHSFLI VFRILCGEWI ENMWACMEVG QKSICLILFL TVMVLGNLVV LNLFTALLLN
     SFSADNLATP DEDGEVNNLQ VALARIQAFG HRTKKAICNF FTRPCLLPWP KAEPQLVVKL
     PLSSSKAENH IAANAAVGSP GGLSVSRGLR DDHSDFITNP NIWVSVPIAE GESDLDDLEE
     DGEEDSQSSQ QEVILQGQEQ LQVETCEGHT APRSPGSGMS SEDLASYVDE KWKDEAVAQA
     PAEGGDDSSS SGGSTVDCLD PEEILRKIPE LADDLEEPDD CFTEGCLRRC PCCKVDISKF
     PWTVGWQVRK TCYRIVEHSW FESFIIFMIL LSSGSLAFED YHLDQKPTVK ALLEYTDRMF
     TFIFVLEMLL KWVAYGFKKY FTNAWCWLDF LIVNISLISL IAKILQYSDV ASIKALRTLR
     ALRPLRALSR FEGMRVVVDA LVGAIPSIMN VLLVCLIFWL IFSTMGVNFF AGKFGRCINK
     TNEYFSLVPL SIVNNISDCK YQNHTGSFFW VNVKVNFDNV AMGYLALLQV ATFKGWMDIM
     YAAVDARDVN LQPKWEDNVY MYLYFVIFII FGGFFTLNLF VGVIIDNFNQ QKKKLGGQDI
     FMTEEQKKYY NAMKKLGSKK PQKPIPRPLN KYQGFVFDIV TKQAFDIVIM VLICLNMITM
     MVETDEQSAE KTKILNKINQ FFVAVFTGEC VMKMFALRHY YFTNGWNVFD FIVVVLSIGS
     LVFSVILTSL ENYFSPTLFR VIRLARIGRI LRLIRAAKGI RTLLFALMMS LPALFNIGLL
     LFLVMFIYSI FGMASFPHVS WEAGIDDMFN FQTFANSMLC LFQITTSAGW DGLLSPILNT
     GPPYCDPNLP NSNGSRGNCG SPAVGILFFT TYIIISFLIV VNMYIAVILE NFNVATQESS
     EPLSEDDFDM FYETWEKFDP EATQFITFSA LSDFADTLSG PLRIPKPNQN ILIQMDLPLV
     PGDKIHCLDI LFAFTKNVLG ESGELDSLKA NIEEKFMATN VSKASYEPIA TTLRWKQEDI
     SATVIQKAYR SYVLHRSMTI SNPPAVPRAE EAVPPPDEAF VEFMVNENCA LPDKSETASA
     ASFPPSYDSV TRGLSDQINM STSSSMQNED EGTSKKVTAP GP
//
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