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Database: UniProt
Entry: SCNBA_RAT
LinkDB: SCNBA_RAT
Original site: SCNBA_RAT 
ID   SCNBA_RAT               Reviewed;        1765 AA.
AC   O88457;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   22-NOV-2017, entry version 114.
DE   RecName: Full=Sodium channel protein type 11 subunit alpha;
DE   AltName: Full=NaN;
DE   AltName: Full=Sensory neuron sodium channel 2;
DE   AltName: Full=Sodium channel protein type XI subunit alpha;
DE   AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.9;
GN   Name=Scn11a; Synonyms=Nan, Sns2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX   PubMed=9671787; DOI=10.1073/pnas.95.15.8963;
RA   Dib-Hajj S.D., Tyrrell L., Black J.A., Waxman S.G.;
RT   "NaN, a novel voltage-gated Na channel, is expressed preferentially in
RT   peripheral sensory neurons and down-regulated after axotomy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 95:8963-8968(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION,
RP   TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
RX   PubMed=10196578; DOI=10.1038/3652;
RA   Tate S.N., Benn S.C., Hick C.A., Trezise D., John V.H., Mannion R.J.,
RA   Costigan M., Plumpton C., Grose D., Gladwell Z., Kendall G., Dale K.,
RA   Bountra C., Woolf C.J.;
RT   "Two sodium channels contribute to the TTX-R sodium current in primary
RT   sensory neurons.";
RL   Nat. Neurosci. 1:653-655(1998).
RN   [3]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=11487631;
RA   Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.;
RT   "Developmental expression of the TTX-resistant voltage-gated sodium
RT   channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons.";
RL   J. Neurosci. 21:6077-6085(2001).
RN   [4]
RP   REVIEW.
RX   PubMed=12536125; DOI=10.1016/S0166-2236(02)00030-9;
RA   Delmas P., Coste B.;
RT   "Na+ channel Nav1.9: in search of a gating mechanism.";
RL   Trends Neurosci. 26:55-57(2003).
CC   -!- FUNCTION: This protein mediates the voltage-dependent sodium ion
CC       permeability of excitable membranes. Assuming opened or closed
CC       conformations in response to the voltage difference across the
CC       membrane, the protein forms a sodium-selective channel through
CC       which sodium ions may pass in accordance with their
CC       electrochemical gradient. It is a tetrodotoxin-resistant sodium
CC       channel isoform. Also involved, with the contribution of the
CC       receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal
CC       depolarization (By similarity). {ECO:0000250,
CC       ECO:0000269|PubMed:10196578}.
CC   -!- SUBUNIT: The voltage-resistant sodium channel consists of an ion
CC       conducting pore forming alpha-subunit regulated by one or more
CC       auxiliary subunits SCN1B, SCN2B and SCN3B.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein
CC       {ECO:0000250|UniProtKB:D0E0C2}.
CC   -!- TISSUE SPECIFICITY: Expressed (at protein level) in myenteric
CC       sensory neurons. Expressed in small sensory neurons of the dorsal
CC       root ganglia (C-fiber neurons) and trigeminal ganglia.
CC       {ECO:0000269|PubMed:10196578, ECO:0000269|PubMed:11487631,
CC       ECO:0000269|PubMed:9671787}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in dorsal root ganglia at 17 dpc
CC       onwards. {ECO:0000269|PubMed:11487631}.
CC   -!- INDUCTION: Down-regulated after axotomy and up-regulated following
CC       hind paw inflammation. Down-regulated in vitro by electrical
CC       stimulation and by deprivation of NGF.
CC       {ECO:0000269|PubMed:10196578, ECO:0000269|PubMed:9671787}.
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   -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC       Nav1.9/SCN11A subfamily. {ECO:0000305}.
DR   EMBL; AF059030; AAC40199.1; -; mRNA.
DR   EMBL; AJ237852; CAB41850.1; -; mRNA.
DR   PIR; T42388; T42388.
DR   RefSeq; NP_062138.1; NM_019265.2.
DR   UniGene; Rn.30023; -.
DR   ProteinModelPortal; O88457; -.
DR   CORUM; O88457; -.
DR   STRING; 10116.ENSRNOP00000033224; -.
DR   GuidetoPHARMACOLOGY; 586; -.
DR   iPTMnet; O88457; -.
DR   PhosphoSitePlus; O88457; -.
DR   PaxDb; O88457; -.
DR   PRIDE; O88457; -.
DR   GeneID; 29701; -.
DR   KEGG; rno:29701; -.
DR   UCSC; RGD:3630; rat.
DR   CTD; 11280; -.
DR   RGD; 3630; Scn11a.
DR   eggNOG; ENOG410KCTY; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   HOGENOM; HOG000231755; -.
DR   HOVERGEN; HBG053100; -.
DR   InParanoid; O88457; -.
DR   KO; K04843; -.
DR   PhylomeDB; O88457; -.
DR   PRO; PR:O88457; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0030424; C:axon; ISO:RGD.
DR   GO; GO:0044299; C:C-fiber; ISO:RGD.
DR   GO; GO:0070062; C:extracellular exosome; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005248; F:voltage-gated sodium channel activity; ISO:RGD.
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:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR   GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR028821; Na_channel_a11su.
DR   InterPro; IPR001696; Na_channel_asu.
DR   InterPro; IPR010526; Na_trans_assoc.
DR   PANTHER; PTHR10037:SF210; PTHR10037:SF210; 1.
DR   Pfam; PF00520; Ion_trans; 4.
DR   Pfam; PF06512; Na_trans_assoc; 1.
DR   PRINTS; PR00170; NACHANNEL.
PE   1: Evidence at protein level;
KW   Cell membrane; Complete proteome; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Membrane; Reference proteome; Repeat;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1765       Sodium channel protein type 11 subunit
FT                                alpha.
FT                                /FTId=PRO_0000048512.
FT   TOPO_DOM      1    126       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    127    148       Helical; Name=S1 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    149    157       Extracellular. {ECO:0000305}.
FT   TRANSMEM    158    177       Helical; Name=S2 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    178    189       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    190    209       Helical; Name=S3 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    210    216       Extracellular. {ECO:0000305}.
FT   TRANSMEM    217    236       Helical; Voltage-sensor; Name=S4 of
FT                                repeat I. {ECO:0000250}.
FT   TOPO_DOM    237    252       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    253    266       Helical; Name=S5 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    267    339       Extracellular. {ECO:0000305}.
FT   INTRAMEM    340    364       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    365    371       Extracellular. {ECO:0000305}.
FT   TRANSMEM    372    397       Helical; Name=S6 of repeat I.
FT                                {ECO:0000250}.
FT   TOPO_DOM    398    567       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    568    591       Helical; Name=S1 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    592    602       Extracellular. {ECO:0000305}.
FT   TRANSMEM    603    626       Helical; Name=S2 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    627    634       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    635    656       Helical; Name=S3 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    657    662       Extracellular. {ECO:0000305}.
FT   TRANSMEM    663    682       Helical; Voltage-sensor; Name=S4 of
FT                                repeat II. {ECO:0000250}.
FT   TOPO_DOM    683    697       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM    698    720       Helical; Name=S5 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    721    741       Extracellular. {ECO:0000305}.
FT   INTRAMEM    742    762       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM    763    772       Extracellular. {ECO:0000305}.
FT   TRANSMEM    773    798       Helical; Name=S6 of repeat II.
FT                                {ECO:0000250}.
FT   TOPO_DOM    799   1029       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1030   1052       Helical; Name=S1 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1053   1066       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1067   1092       Helical; Name=S2 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1093   1098       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1099   1116       Helical; Name=S3 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1117   1117       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1118   1139       Helical; Voltage-sensor; Name=S4 of
FT                                repeat III. {ECO:0000250}.
FT   TOPO_DOM   1140   1158       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1159   1180       Helical; Name=S5 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1181   1223       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1224   1245       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1246   1261       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1262   1288       Helical; Name=S6 of repeat III.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1289   1341       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1342   1365       Helical; Name=S1 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1366   1376       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1377   1400       Helical; Name=S2 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1401   1406       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1407   1430       Helical; Name=S3 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1431   1440       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1441   1463       Helical; Voltage-sensor; Name=S4 of
FT                                repeat IV. {ECO:0000250}.
FT   TOPO_DOM   1464   1478       Cytoplasmic. {ECO:0000305}.
FT   TRANSMEM   1479   1501       Helical; Name=S5 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1502   1515       Extracellular. {ECO:0000305}.
FT   INTRAMEM   1516   1538       Pore-forming.
FT                                {ECO:0000250|UniProtKB:D0E0C2}.
FT   TOPO_DOM   1539   1559       Extracellular. {ECO:0000305}.
FT   TRANSMEM   1560   1584       Helical; Name=S6 of repeat IV.
FT                                {ECO:0000250}.
FT   TOPO_DOM   1585   1765       Cytoplasmic. {ECO:0000305}.
FT   REPEAT      115    403       I. {ECO:0000305}.
FT   REPEAT      554    820       II. {ECO:0000305}.
FT   REPEAT     1022   1319       III. {ECO:0000305}.
FT   REPEAT     1328   1619       IV. {ECO:0000305}.
FT   CARBOHYD    214    214       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    319    319       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    333    333       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    660    660       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    723    723       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1187   1187       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1202   1202       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1207   1207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1210   1210       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1547   1547       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    280    317       {ECO:0000250|UniProtKB:D0E0C2}.
FT   DISULFID    764    774       {ECO:0000250|UniProtKB:D0E0C2}.
SQ   SEQUENCE   1765 AA;  201845 MW;  AE8C67397CC60BD9 CRC64;
     MEERYYPVIF PDERNFRPFT SDSLAAIEKR IAIQKERKKS KDKAAAEPQP RPQLDLKASR
     KLPKLYGDIP PELVAKPLED LDPFYKDHKT FMVLNKKRTI YRFSAKRALF ILGPFNPLRS
     LMIRISVHSV FSMFIICTVI INCMFMANSM ERSFDNDIPE YVFIGIYILE AVIKILARGF
     IVDEFSFLRD PWNWLDFIVI GTAIATCFPG SQVNLSALRT FRVFRALKAI SVISGLKVIV
     GALLRSVKKL VDVMVLTLFC LSIFALVGQQ LFMGILNQKC IKHNCGPNPA SNKDCFEKEK
     DSEDFIMCGT WLGSRPCPNG STCDKTTLNP DNNYTKFDNF GWSFLAMFRV MTQDSWERLY
     RQILRTSGIY FVFFFVVVIF LGSFYLLNLT LAVVTMAYEE QNRNVAAETE AKEKMFQEAQ
     QLLREEKEAL VAMGIDRSSL NSLQASSFSP KKRKFFGSKT RKSFFMRGSK TAQASASDSE
     DDASKNPQLL EQTKRLSQNL PVDLFDEHVD PLHRQRALSA VSILTITMQE QEKFQEPCFP
     CGKNLASKYL VWDCSPQWLC IKKVLRTIMT DPFTELAITI CIIINTVFLA VEHHNMDDNL
     KTILKIGNWV FTGIFIAEMC LKIIALDPYH YFRHGWNVFD SIVALLSLAD VLYNTLSDNN
     RSFLASLRVL RVFKLAKSWP TLNTLIKIIG HSVGALGNLT VVLTIVVFIF SVVGMRLFGT
     KFNKTAYATQ ERPRRRWHMD NFYHSFLVVF RILCGEWIEN MWGCMQDMDG SPLCIIVFVL
     IMVIGKLVVL NLFIALLLNS FSNEEKDGSL EGETRKTKVQ LALDRFRRAF SFMLHALQSF
     CCKKCRRKNS PKPKETTESF AGENKDSILP DARPWKEYDT DMALYTGQAG APLAPLAEVE
     DDVEYCGEGG ALPTSQHSAG VQAGDLPPET KQLTSPDDQG VEMEVFSEED LHLSIQSPRK
     KSDAVSMLSE CSTIDLNDIF RNLQKTVSPK KQPDRCFPKG LSCHFLCHKT DKRKSPWVLW
     WNIRKTCYQI VKHSWFESFI IFVILLSSGA LIFEDVNLPS RPQVEKLLRC TDNIFTFIFL
     LEMILKWVAF GFRRYFTSAW CWLDFLIVVV SVLSLMNLPS LKSFRTLRAL RPLRALSQFE
     GMKVVVYALI SAIPAILNVL LVCLIFWLVF CILGVNLFSG KFGRCINGTD INMYLDFTEV
     PNRSQCNISN YSWKVPQVNF DNVGNAYLAL LQVATYKGWL EIMNAAVDSR EKDEQPDFEA
     NLYAYLYFVV FIIFGSFFTL NLFIGVIIDN FNQQQKKLGG QDIFMTEEQK KYYNAMKKLG
     TKKPQKPIPR PLNKCQAFVF DLVTSQVFDV IILGLIVLNM IIMMAESADQ PKDVKKTFDI
     LNIAFVVIFT IECLIKVFAL RQHYFTNGWN LFDCVVVVLS IISTLVSRLE DSDISFPPTL
     FRVVRLARIG RILRLVRAAR GIRTLLFALM MSLPSLFNIG LLLFLVMFIY AIFGMSWFSK
     VKKGSGIDDI FNFETFTGSM LCLFQITTSA GWDTLLNPML EAKEHCNSSS QDSCQQPQIA
     VVYFVSYIII SFLIVVNMYI AVILENFNTA TEESEDPLGE DDFEIFYEVW EKFDPEASQF
     IQYSALSDFA DALPEPLRVA KPNKFQFLVM DLPMVMGDRL HCMDVLFAFT TRVLGDSSGL
     DTMKTMMEEK FMEANPFKKL YEPIVTTTKR KEEEQGAAVI QRAYRKHMEK MVKLRLKDRS
     SSSHQVFCNG DLSSLDVAKV KVHND
//
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