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Q8BHK2 (SCN3B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sodium channel subunit beta-3
Gene names
Name:Scn3b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Modulates channel gating kinetics. Causes unique persistent sodium currents. Inactivates the sodium channel opening more slowly than the subunit beta-1. Its association with neurofascin may target the sodium channels to the nodes of Ranvier of developing axons and retain these channels at the nodes in mature myelinated axons By similarity.

Subunit structure

The voltage-sensitive sodium channel consists of an ion conducting pore forming alpha-subunit regulated by one or more beta-1, beta-2, beta-3 and/or beta-4 subunits. Beta-1 and beta-3 are non-covalently associated with alpha, while beta-2 and beta-4 are covalently linked by disulfide bonds By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein By similarity.

Sequence similarities

Belongs to the sodium channel auxiliary subunit SCN3B (TC 8.A.17) family. [View classification]

Contains 1 Ig-like C2-type (immunoglobulin-like) domain.

Ontologies

Keywords
   Biological processIon transport
Sodium transport
Transport
   Cellular componentMembrane
   DomainImmunoglobulin domain
Signal
Transmembrane
Transmembrane helix
   LigandSodium
   Molecular functionIon channel
Sodium channel
Voltage-gated channel
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSA node cell to atrial cardiac muscle cell communication

Inferred from mutant phenotype PubMed 19796257. Source: BHF-UCL

atrial cardiac muscle cell action potential

Inferred from electronic annotation. Source: Ensembl

cardiac conduction

Inferred from mutant phenotype PubMed 19351516. Source: MGI

cardiac muscle contraction

Inferred from electronic annotation. Source: Ensembl

nervous system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of heart rate

Inferred from mutant phenotype PubMed 19796257. Source: BHF-UCL

positive regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

regulation of atrial cardiac muscle cell membrane depolarization

Inferred from mutant phenotype PubMed 19796257. Source: BHF-UCL

regulation of heart rate by cardiac conduction

Inferred from electronic annotation. Source: Ensembl

regulation of sodium ion transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

regulation of ventricular cardiac muscle cell membrane depolarization

Inferred from electronic annotation. Source: Ensembl

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

ventricular cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 19351516. Source: MGI

   Cellular_componentZ disc

Inferred from direct assay PubMed 17884088. Source: BHF-UCL

voltage-gated sodium channel complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionion channel binding

Inferred from physical interaction PubMed 20042427. Source: BHF-UCL

sodium channel regulator activity

Inferred from electronic annotation. Source: InterPro

voltage-gated sodium channel activity involved in cardiac muscle cell action potential

Inferred from mutant phenotype PubMed 19351516. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 215191Sodium channel subunit beta-3
PRO_0000014935

Regions

Topological domain25 – 159135Extracellular Potential
Transmembrane160 – 18021Helical; Potential
Topological domain181 – 21535Cytoplasmic Potential
Domain25 – 138114Ig-like C2-type

Amino acid modifications

Glycosylation951N-linked (GlcNAc...) Potential
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation1131N-linked (GlcNAc...) Potential
Glycosylation1211N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 48 Potential
Disulfide bond45 ↔ 120 Potential

Sequences

Sequence LengthMass (Da)Tools
Q8BHK2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 0E07B4704178A423

FASTA21524,789
        10         20         30         40         50         60 
MPAFNRLLPL ASLVLIYWVR VCFPVCVEVP SETEAVQGNS MKLRCISCMK REEVEATTVV 

        70         80         90        100        110        120 
EWFYRPEGGK DFLIYEYRNG HQEVESPFQG RLQWNGSKDL QDVSITVLNV TLNDSGLYTC 

       130        140        150        160        170        180 
NVSREFEFEA HRPFVKTTRL IPLRVTEEAG EDFTSVVSEI MMYILLVFLT LWLFIEMIYC 

       190        200        210 
YRKVSKAEEA AQENASDYLA IPSENKENSV VPVEE 

« Hide

References

« Hide 'large scale' references
[1]"Mouse brain and heart beta 3 sodium channel cDNA."
Chen C., Avery C., Kazen-Gillespie K., Isom L.L.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head and Spinal cord.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Olfactory epithelium.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY049036 mRNA. Translation: AAL07512.1.
AK049747 mRNA. Translation: BAC33901.1.
AK076466 mRNA. Translation: BAC36356.1.
BC053919 mRNA. Translation: AAH53919.1.
BC058636 mRNA. Translation: AAH58636.1.
RefSeqNP_001077386.1. NM_001083917.1.
NP_001273543.1. NM_001286614.1.
NP_839941.1. NM_178227.4.
XP_006510297.1. XM_006510234.1.
UniGeneMm.290083.

3D structure databases

ProteinModelPortalQ8BHK2.
SMRQ8BHK2. Positions 25-122.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BHK2.

Proteomic databases

PaxDbQ8BHK2.
PRIDEQ8BHK2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049941; ENSMUSP00000051627; ENSMUSG00000049281.
ENSMUST00000114956; ENSMUSP00000110606; ENSMUSG00000049281.
ENSMUST00000171835; ENSMUSP00000132933; ENSMUSG00000049281.
GeneID235281.
KEGGmmu:235281.
UCSCuc009ozj.1. mouse.

Organism-specific databases

CTD55800.
MGIMGI:1918882. Scn3b.

Phylogenomic databases

eggNOGNOG40812.
GeneTreeENSGT00390000018560.
HOGENOMHOG000276881.
HOVERGENHBG056582.
InParanoidQ8BHK2.
KOK04847.
OMALLIEMVY.
OrthoDBEOG7M3J19.
TreeFamTF332097.

Gene expression databases

ArrayExpressQ8BHK2.
BgeeQ8BHK2.
CleanExMM_SCN3B.
GenevestigatorQ8BHK2.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR013106. Ig_V-set.
IPR027098. Na_channel_b1/b3.
IPR027096. Na_channel_b3.
[Graphical view]
PANTHERPTHR10546. PTHR10546. 1 hit.
PTHR10546:SF1. PTHR10546:SF1. 1 hit.
PfamPF07686. V-set. 1 hit.
[Graphical view]
SMARTSM00409. IG. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio382555.
PROQ8BHK2.
SOURCESearch...

Entry information

Entry nameSCN3B_MOUSE
AccessionPrimary (citable) accession number: Q8BHK2
Secondary accession number(s): Q91Z99
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot