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 03-AUG-2022, entry version 134.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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; DOI=10.1523/jneurosci.21-16-06077.2001;
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 which
CC sodium ions may pass in accordance with their electrochemical gradient.
CC It is a tetrodotoxin-resistant sodium channel isoform. Also involved,
CC with the contribution of the receptor tyrosine kinase NTRK2, in rapid
CC BDNF-evoked neuronal 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 {ECO:0000250|UniProtKB:D0E0C2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}.
CC -!- TISSUE SPECIFICITY: Expressed (at protein level) in myenteric sensory
CC neurons. Expressed in small sensory neurons of the dorsal root ganglia
CC (C-fiber neurons) and trigeminal ganglia. {ECO:0000269|PubMed:10196578,
CC ECO:0000269|PubMed:11487631, 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 hind
CC paw inflammation. Down-regulated in vitro by electrical stimulation and
CC by deprivation of NGF. {ECO:0000269|PubMed:10196578,
CC 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 charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.9/SCN11A subfamily. {ECO:0000305}.
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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 AlphaFoldDB; O88457; -.
DR SMR; O88457; -.
DR CORUM; O88457; -.
DR STRING; 10116.ENSRNOP00000033224; -.
DR BindingDB; O88457; -.
DR ChEMBL; CHEMBL2629; -.
DR GuidetoPHARMACOLOGY; 586; -.
DR GlyGen; O88457; 10 sites.
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; KOG2301; Eukaryota.
DR InParanoid; O88457; -.
DR OrthoDB; 172471at2759; -.
DR PhylomeDB; O88457; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:O88457; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0044299; C:C-fiber; ISO:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0051930; P:regulation of sensory perception of pain; ISS:UniProtKB.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR028821; Na_channel_a11su.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
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; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1765
FT /note="Sodium channel protein type 11 subunit alpha"
FT /id="PRO_0000048512"
FT TOPO_DOM 1..126
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 127..148
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..157
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 158..177
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 178..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 190..209
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 210..216
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 217..236
FT /note="Helical; Voltage-sensor; Name=S4 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 237..252
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 253..266
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 267..339
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 340..364
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 365..371
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 372..397
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250"
FT TOPO_DOM 398..567
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 568..591
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 592..602
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 603..626
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 627..634
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 635..656
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 657..662
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 663..682
FT /note="Helical; Voltage-sensor; Name=S4 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 683..697
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 698..720
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 721..741
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 742..762
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 763..772
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 773..798
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250"
FT TOPO_DOM 799..1029
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1030..1052
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1053..1066
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1067..1092
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1093..1098
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1099..1116
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1117
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1118..1139
FT /note="Helical; Voltage-sensor; Name=S4 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1140..1158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1159..1180
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1181..1223
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1224..1245
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1246..1261
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1262..1288
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1289..1341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1342..1365
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1366..1376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1377..1400
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1401..1406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1407..1430
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1431..1440
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1441..1463
FT /note="Helical; Voltage-sensor; Name=S4 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1464..1478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1479..1501
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1502..1515
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1516..1538
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT TOPO_DOM 1539..1559
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1560..1584
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250"
FT TOPO_DOM 1585..1765
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 115..403
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 554..820
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 1022..1319
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1328..1619
FT /note="IV"
FT /evidence="ECO:0000305"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 319
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 660
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 723
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 280..317
FT /evidence="ECO:0000250|UniProtKB:D0E0C2"
FT DISULFID 764..774
FT /evidence="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
