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O88457

- SCNBA_RAT

UniProt

O88457 - SCNBA_RAT

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Protein
Sodium channel protein type 11 subunit alpha
Gene
Scn11a, Nan, Sns2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which sodium ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-resistant sodium channel isoform. Also involved, with the contribution of the receptor tyrosine kinase NTRK2, in rapid BDNF-evoked neuronal depolarization By similarity.1 Publication

GO - Molecular functioni

  1. protein binding Source: BHF-UCL
  2. voltage-gated sodium channel activity Source: RefGenome

GO - Biological processi

  1. membrane depolarization during action potential Source: RefGenome
  2. neuronal action potential Source: RefGenome
  3. regulation of sensory perception of pain Source: UniProtKB
  4. sodium ion transmembrane transport Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Sodium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Sodium transport, Transport

Keywords - Ligandi

Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium channel protein type 11 subunit alpha
Alternative name(s):
NaN
Sensory neuron sodium channel 2
Sodium channel protein type XI subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.9
Gene namesi
Name:Scn11a
Synonyms:Nan, Sns2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi3630. Scn11a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei127 – 14822Helical; Name=S1 of repeat I; By similarity
Add
BLAST
Transmembranei158 – 17720Helical; Name=S2 of repeat I; By similarity
Add
BLAST
Transmembranei190 – 20920Helical; Name=S3 of repeat I; By similarity
Add
BLAST
Transmembranei217 – 23620Helical; Voltage-sensor; Name=S4 of repeat I; By similarity
Add
BLAST
Transmembranei253 – 26614Helical; Name=S5 of repeat I; By similarity
Add
BLAST
Transmembranei372 – 39726Helical; Name=S6 of repeat I; By similarity
Add
BLAST
Transmembranei568 – 59124Helical; Name=S1 of repeat II; By similarity
Add
BLAST
Transmembranei603 – 62624Helical; Name=S2 of repeat II; By similarity
Add
BLAST
Transmembranei635 – 65622Helical; Name=S3 of repeat II; By similarity
Add
BLAST
Transmembranei663 – 68220Helical; Voltage-sensor; Name=S4 of repeat II; By similarity
Add
BLAST
Transmembranei698 – 72023Helical; Name=S5 of repeat II; By similarity
Add
BLAST
Transmembranei773 – 79826Helical; Name=S6 of repeat II; By similarity
Add
BLAST
Transmembranei1030 – 105223Helical; Name=S1 of repeat III; By similarity
Add
BLAST
Transmembranei1067 – 109226Helical; Name=S2 of repeat III; By similarity
Add
BLAST
Transmembranei1099 – 111618Helical; Name=S3 of repeat III; By similarity
Add
BLAST
Transmembranei1118 – 113922Helical; Voltage-sensor; Name=S4 of repeat III; By similarity
Add
BLAST
Transmembranei1159 – 118022Helical; Name=S5 of repeat III; By similarity
Add
BLAST
Transmembranei1262 – 128827Helical; Name=S6 of repeat III; By similarity
Add
BLAST
Transmembranei1342 – 136524Helical; Name=S1 of repeat IV; By similarity
Add
BLAST
Transmembranei1377 – 140024Helical; Name=S2 of repeat IV; By similarity
Add
BLAST
Transmembranei1407 – 143024Helical; Name=S3 of repeat IV; By similarity
Add
BLAST
Transmembranei1441 – 146323Helical; Voltage-sensor; Name=S4 of repeat IV; By similarity
Add
BLAST
Transmembranei1479 – 150123Helical; Name=S5 of repeat IV; By similarity
Add
BLAST
Transmembranei1560 – 158425Helical; Name=S6 of repeat IV; By similarity
Add
BLAST

GO - Cellular componenti

  1. plasma membrane Source: RefGenome
  2. voltage-gated sodium channel complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17651765Sodium channel protein type 11 subunit alpha
PRO_0000048512Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi214 – 2141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi319 – 3191N-linked (GlcNAc...) Reviewed prediction
Glycosylationi333 – 3331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi660 – 6601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi723 – 7231N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1187 – 11871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1202 – 12021N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1207 – 12071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1210 – 12101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1547 – 15471N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiO88457.
PRIDEiO88457.

PTM databases

PhosphoSiteiO88457.

Expressioni

Tissue specificityi

Expressed (at protein level) in myenteric sensory neurons. Expressed in small sensory neurons of the dorsal root ganglia (C-fiber neurons) and trigeminal ganglia.3 Publications

Developmental stagei

Expressed in dorsal root ganglia at 17 dpc onwards.1 Publication

Inductioni

Down-regulated after axotomy and up-regulated following hind paw inflammation. Down-regulated in vitro by electrical stimulation and by deprivation of NGF.2 Publications

Gene expression databases

GenevestigatoriO88457.

Interactioni

Subunit structurei

The voltage-resistant sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more auxiliary subunits SCN1B, SCN2B and SCN3B.

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000033224.

Structurei

3D structure databases

ProteinModelPortaliO88457.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 398273I
Add
BLAST
Repeati567 – 799233II
Add
BLAST
Repeati1029 – 1289261III
Add
BLAST
Repeati1341 – 1585245IV
Add
BLAST

Domaini

The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position.

Sequence similaritiesi

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
HOGENOMiHOG000231755.
HOVERGENiHBG053100.
InParanoidiO88457.
KOiK04843.
PhylomeDBiO88457.

Family and domain databases

Gene3Di1.20.120.350. 4 hits.
InterProiIPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028821. Na_channel_a11su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view]
PANTHERiPTHR10037:SF22. PTHR10037:SF22. 1 hit.
PfamiPF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view]
PRINTSiPR00170. NACHANNEL.

Sequencei

Sequence statusi: Complete.

O88457-1 [UniParc]FASTAAdd to Basket

« Hide

MEERYYPVIF PDERNFRPFT SDSLAAIEKR IAIQKERKKS KDKAAAEPQP     50
RPQLDLKASR KLPKLYGDIP PELVAKPLED LDPFYKDHKT FMVLNKKRTI 100
YRFSAKRALF ILGPFNPLRS LMIRISVHSV FSMFIICTVI INCMFMANSM 150
ERSFDNDIPE YVFIGIYILE AVIKILARGF IVDEFSFLRD PWNWLDFIVI 200
GTAIATCFPG SQVNLSALRT FRVFRALKAI SVISGLKVIV GALLRSVKKL 250
VDVMVLTLFC LSIFALVGQQ LFMGILNQKC IKHNCGPNPA SNKDCFEKEK 300
DSEDFIMCGT WLGSRPCPNG STCDKTTLNP DNNYTKFDNF GWSFLAMFRV 350
MTQDSWERLY RQILRTSGIY FVFFFVVVIF LGSFYLLNLT LAVVTMAYEE 400
QNRNVAAETE AKEKMFQEAQ QLLREEKEAL VAMGIDRSSL NSLQASSFSP 450
KKRKFFGSKT RKSFFMRGSK TAQASASDSE DDASKNPQLL EQTKRLSQNL 500
PVDLFDEHVD PLHRQRALSA VSILTITMQE QEKFQEPCFP CGKNLASKYL 550
VWDCSPQWLC IKKVLRTIMT DPFTELAITI CIIINTVFLA VEHHNMDDNL 600
KTILKIGNWV FTGIFIAEMC LKIIALDPYH YFRHGWNVFD SIVALLSLAD 650
VLYNTLSDNN RSFLASLRVL RVFKLAKSWP TLNTLIKIIG HSVGALGNLT 700
VVLTIVVFIF SVVGMRLFGT KFNKTAYATQ ERPRRRWHMD NFYHSFLVVF 750
RILCGEWIEN MWGCMQDMDG SPLCIIVFVL IMVIGKLVVL NLFIALLLNS 800
FSNEEKDGSL EGETRKTKVQ LALDRFRRAF SFMLHALQSF CCKKCRRKNS 850
PKPKETTESF AGENKDSILP DARPWKEYDT DMALYTGQAG APLAPLAEVE 900
DDVEYCGEGG ALPTSQHSAG VQAGDLPPET KQLTSPDDQG VEMEVFSEED 950
LHLSIQSPRK KSDAVSMLSE CSTIDLNDIF RNLQKTVSPK KQPDRCFPKG 1000
LSCHFLCHKT DKRKSPWVLW WNIRKTCYQI VKHSWFESFI IFVILLSSGA 1050
LIFEDVNLPS RPQVEKLLRC TDNIFTFIFL LEMILKWVAF GFRRYFTSAW 1100
CWLDFLIVVV SVLSLMNLPS LKSFRTLRAL RPLRALSQFE GMKVVVYALI 1150
SAIPAILNVL LVCLIFWLVF CILGVNLFSG KFGRCINGTD INMYLDFTEV 1200
PNRSQCNISN YSWKVPQVNF DNVGNAYLAL LQVATYKGWL EIMNAAVDSR 1250
EKDEQPDFEA NLYAYLYFVV FIIFGSFFTL NLFIGVIIDN FNQQQKKLGG 1300
QDIFMTEEQK KYYNAMKKLG TKKPQKPIPR PLNKCQAFVF DLVTSQVFDV 1350
IILGLIVLNM IIMMAESADQ PKDVKKTFDI LNIAFVVIFT IECLIKVFAL 1400
RQHYFTNGWN LFDCVVVVLS IISTLVSRLE DSDISFPPTL FRVVRLARIG 1450
RILRLVRAAR GIRTLLFALM MSLPSLFNIG LLLFLVMFIY AIFGMSWFSK 1500
VKKGSGIDDI FNFETFTGSM LCLFQITTSA GWDTLLNPML EAKEHCNSSS 1550
QDSCQQPQIA VVYFVSYIII SFLIVVNMYI AVILENFNTA TEESEDPLGE 1600
DDFEIFYEVW EKFDPEASQF IQYSALSDFA DALPEPLRVA KPNKFQFLVM 1650
DLPMVMGDRL HCMDVLFAFT TRVLGDSSGL DTMKTMMEEK FMEANPFKKL 1700
YEPIVTTTKR KEEEQGAAVI QRAYRKHMEK MVKLRLKDRS SSSHQVFCNG 1750
DLSSLDVAKV KVHND 1765
Length:1,765
Mass (Da):201,845
Last modified:November 1, 1998 - v1
Checksum:iAE8C67397CC60BD9
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059030 mRNA. Translation: AAC40199.1.
AJ237852 mRNA. Translation: CAB41850.1.
PIRiT42388.
RefSeqiNP_062138.1. NM_019265.2.
UniGeneiRn.30023.

Genome annotation databases

GeneIDi29701.
KEGGirno:29701.
UCSCiRGD:3630. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF059030 mRNA. Translation: AAC40199.1 .
AJ237852 mRNA. Translation: CAB41850.1 .
PIRi T42388.
RefSeqi NP_062138.1. NM_019265.2.
UniGenei Rn.30023.

3D structure databases

ProteinModelPortali O88457.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000033224.

Chemistry

BindingDBi O88457.
GuidetoPHARMACOLOGYi 586.

PTM databases

PhosphoSitei O88457.

Proteomic databases

PaxDbi O88457.
PRIDEi O88457.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 29701.
KEGGi rno:29701.
UCSCi RGD:3630. rat.

Organism-specific databases

CTDi 11280.
RGDi 3630. Scn11a.

Phylogenomic databases

eggNOGi COG1226.
HOGENOMi HOG000231755.
HOVERGENi HBG053100.
InParanoidi O88457.
KOi K04843.
PhylomeDBi O88457.

Miscellaneous databases

NextBioi 610107.
PROi O88457.

Gene expression databases

Genevestigatori O88457.

Family and domain databases

Gene3Di 1.20.120.350. 4 hits.
InterProi IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR028821. Na_channel_a11su.
IPR001696. Na_channel_asu.
IPR010526. Na_trans_assoc.
[Graphical view ]
PANTHERi PTHR10037:SF22. PTHR10037:SF22. 1 hit.
Pfami PF00520. Ion_trans. 4 hits.
PF06512. Na_trans_assoc. 1 hit.
[Graphical view ]
PRINTSi PR00170. NACHANNEL.
ProtoNeti Search...

Publicationsi

  1. "NaN, a novel voltage-gated Na channel, is expressed preferentially in peripheral sensory neurons and down-regulated after axotomy."
    Dib-Hajj S.D., Tyrrell L., Black J.A., Waxman S.G.
    Proc. Natl. Acad. Sci. U.S.A. 95:8963-8968(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.
    Tissue: Spinal ganglion.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION, TISSUE SPECIFICITY, INDUCTION.
    Strain: Sprague-Dawley.
    Tissue: Spinal ganglion.
  3. "Developmental expression of the TTX-resistant voltage-gated sodium channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons."
    Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.
    J. Neurosci. 21:6077-6085(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "Na+ channel Nav1.9: in search of a gating mechanism."
    Delmas P., Coste B.
    Trends Neurosci. 26:55-57(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.

Entry informationi

Entry nameiSCNBA_RAT
AccessioniPrimary (citable) accession number: O88457
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: November 1, 1998
Last modified: June 11, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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