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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

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.By similarity

GO - Molecular functioni

  1. 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

Membrane By similarity; Multi-pass membrane protein By similarity

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 alphaPRO_0000048512Add
BLAST

Amino acid modifications

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

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.
ModBaseiSearch...
MobiDBiSearch...

Transmembrane

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati126 – 398273IAdd
BLAST
Repeati567 – 799233IIAdd
BLAST
Repeati1029 – 1289261IIIAdd
BLAST
Repeati1341 – 1585245IVAdd
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

        10         20         30         40         50
MEERYYPVIF PDERNFRPFT SDSLAAIEKR IAIQKERKKS KDKAAAEPQP
60 70 80 90 100
RPQLDLKASR KLPKLYGDIP PELVAKPLED LDPFYKDHKT FMVLNKKRTI
110 120 130 140 150
YRFSAKRALF ILGPFNPLRS LMIRISVHSV FSMFIICTVI INCMFMANSM
160 170 180 190 200
ERSFDNDIPE YVFIGIYILE AVIKILARGF IVDEFSFLRD PWNWLDFIVI
210 220 230 240 250
GTAIATCFPG SQVNLSALRT FRVFRALKAI SVISGLKVIV GALLRSVKKL
260 270 280 290 300
VDVMVLTLFC LSIFALVGQQ LFMGILNQKC IKHNCGPNPA SNKDCFEKEK
310 320 330 340 350
DSEDFIMCGT WLGSRPCPNG STCDKTTLNP DNNYTKFDNF GWSFLAMFRV
360 370 380 390 400
MTQDSWERLY RQILRTSGIY FVFFFVVVIF LGSFYLLNLT LAVVTMAYEE
410 420 430 440 450
QNRNVAAETE AKEKMFQEAQ QLLREEKEAL VAMGIDRSSL NSLQASSFSP
460 470 480 490 500
KKRKFFGSKT RKSFFMRGSK TAQASASDSE DDASKNPQLL EQTKRLSQNL
510 520 530 540 550
PVDLFDEHVD PLHRQRALSA VSILTITMQE QEKFQEPCFP CGKNLASKYL
560 570 580 590 600
VWDCSPQWLC IKKVLRTIMT DPFTELAITI CIIINTVFLA VEHHNMDDNL
610 620 630 640 650
KTILKIGNWV FTGIFIAEMC LKIIALDPYH YFRHGWNVFD SIVALLSLAD
660 670 680 690 700
VLYNTLSDNN RSFLASLRVL RVFKLAKSWP TLNTLIKIIG HSVGALGNLT
710 720 730 740 750
VVLTIVVFIF SVVGMRLFGT KFNKTAYATQ ERPRRRWHMD NFYHSFLVVF
760 770 780 790 800
RILCGEWIEN MWGCMQDMDG SPLCIIVFVL IMVIGKLVVL NLFIALLLNS
810 820 830 840 850
FSNEEKDGSL EGETRKTKVQ LALDRFRRAF SFMLHALQSF CCKKCRRKNS
860 870 880 890 900
PKPKETTESF AGENKDSILP DARPWKEYDT DMALYTGQAG APLAPLAEVE
910 920 930 940 950
DDVEYCGEGG ALPTSQHSAG VQAGDLPPET KQLTSPDDQG VEMEVFSEED
960 970 980 990 1000
LHLSIQSPRK KSDAVSMLSE CSTIDLNDIF RNLQKTVSPK KQPDRCFPKG
1010 1020 1030 1040 1050
LSCHFLCHKT DKRKSPWVLW WNIRKTCYQI VKHSWFESFI IFVILLSSGA
1060 1070 1080 1090 1100
LIFEDVNLPS RPQVEKLLRC TDNIFTFIFL LEMILKWVAF GFRRYFTSAW
1110 1120 1130 1140 1150
CWLDFLIVVV SVLSLMNLPS LKSFRTLRAL RPLRALSQFE GMKVVVYALI
1160 1170 1180 1190 1200
SAIPAILNVL LVCLIFWLVF CILGVNLFSG KFGRCINGTD INMYLDFTEV
1210 1220 1230 1240 1250
PNRSQCNISN YSWKVPQVNF DNVGNAYLAL LQVATYKGWL EIMNAAVDSR
1260 1270 1280 1290 1300
EKDEQPDFEA NLYAYLYFVV FIIFGSFFTL NLFIGVIIDN FNQQQKKLGG
1310 1320 1330 1340 1350
QDIFMTEEQK KYYNAMKKLG TKKPQKPIPR PLNKCQAFVF DLVTSQVFDV
1360 1370 1380 1390 1400
IILGLIVLNM IIMMAESADQ PKDVKKTFDI LNIAFVVIFT IECLIKVFAL
1410 1420 1430 1440 1450
RQHYFTNGWN LFDCVVVVLS IISTLVSRLE DSDISFPPTL FRVVRLARIG
1460 1470 1480 1490 1500
RILRLVRAAR GIRTLLFALM MSLPSLFNIG LLLFLVMFIY AIFGMSWFSK
1510 1520 1530 1540 1550
VKKGSGIDDI FNFETFTGSM LCLFQITTSA GWDTLLNPML EAKEHCNSSS
1560 1570 1580 1590 1600
QDSCQQPQIA VVYFVSYIII SFLIVVNMYI AVILENFNTA TEESEDPLGE
1610 1620 1630 1640 1650
DDFEIFYEVW EKFDPEASQF IQYSALSDFA DALPEPLRVA KPNKFQFLVM
1660 1670 1680 1690 1700
DLPMVMGDRL HCMDVLFAFT TRVLGDSSGL DTMKTMMEEK FMEANPFKKL
1710 1720 1730 1740 1750
YEPIVTTTKR KEEEQGAAVI QRAYRKHMEK MVKLRLKDRS SSSHQVFCNG
1760
DLSSLDVAKV KVHND
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: October 29, 2014
This is version 97 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