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SCN2A Membrane Protein Introduction

Introduction of SCN2A

Sodium channel protein type 2 subunit alpha (SCN2A) encoded by the SCN2A gene is a member of the sodium channel alpha subunit gene family. This protein has 2005 amino acids and the molecular mass is 227 kDa. It contains 4 internal repeats, each with 5 hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged segment (S4). Segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. The protein heterooligomers with SCN2B or SCN4B by a disulfide bond to form voltage-gated sodium channels.

Basic Information of SCN2A
Protein Name Sodium channel protein type 2 subunit alpha
Gene Name SCN2A, NAC2, SCN2A1, SCN2A2
Aliases HBSC II, Sodium channel protein brain II subunit alpha, Sodium channel protein type II subunit alpha, Voltage-gated sodium channel subunit alpha Nav1.2
Organism Homo sapiens (Human)
UniProt ID Q99250
Transmembrane Times 24
Length (aa) 2005
Sequence MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSVPLEDLDPYYINKKTFIVLNKGKAISRFSATPALYILTPFNPIRKLAIKILVHSLFNMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSSFEINITSFFNNSLDGNGTTFNRTVSIFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQSGEEEKNDRVRKSESEDSIRRKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFRGRAKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRHSNVSQASRASRVLPILPMNGKMHSAVDCNGVVSLVGGPSTLTSAGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSIASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHLVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEVEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQVYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECKALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRYYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPDKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFAKLSDFADALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIIIQRAYRRYLLKQKVKKVSSIYKKDKGKECDGTPIKEDTLIDKLNENSTPEKTDMTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK

Function of SCN2A Membrane Protein

SCN2A mediates the voltage-dependent sodium ion permeability of excitable membranes. Through the change of opened or closed conformations responding to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na+ ions may pass in accordance with their electrochemical gradient. Mutations in SCN2A are associated with a variety of diseases, including benign familial neonatal-infantile seizures, generalized epilepsy with febrile seizures, Dravet syndrome, some intractable childhood epilepsies, and acute encephalitis with refractory, repetitive, partial seizures. Although almost all SCN2A mutations are missense, electrophysiological analyses show that different mutations cause diverse effects on NaV1.2 channel.

Roles of voltage-gated Na+ channels in taste cells. Fig.1 Roles of voltage-gated Na+ channels in taste cells. (Vandenbeuch, 2009)

Application of SCN2A Membrane Protein in Literature

  1. Howell K.B., et al. SCN2A encephalopathy: A major cause of epilepsy of infancy with migrating focal seizures. Neurology. 2015, 85(11):958-66. PubMed ID: 26291284

    This article expands the phenotypic spectrum of SCN2A encephalopathy and emphasizes SCN2A as a major gene for epilepsy of infancy with migrating focal seizures.

  2. Tavassoli T., et al. De novo SCN2A splice site mutation in a boy with Autism spectrum disorder. BMC Medical Genetics. 2014, 15:35. PubMed ID: 24650168

    This article suggests a splice site mutation in SCN2A plays a role in autism spectrum disorder, which indicates that SCN2A mutator phenotype might help to reduce heterogeneity seen in autism spectrum disorder.

  3. Nakamura K., et al. Clinical spectrum of SCN2A mutations expanding to Ohtahara syndrome. Neurology. 2013, 81(11):992-8. PubMed ID: 23935176

    This article suggests that 14 novel SCN2A mutations in 15 patients with EOEE have been identified. All mutations show high scores for predicted negative effects on protein function.

  4. Shi X., et al. Clinical spectrum of SCN2A mutations. Brain Development. 2012, 34(7):541-5. PubMed ID: 22029951

    This article reveals that SCN2A mutations are associated with a variety of human epilepsy syndromes, such as BFNIS and BFIS.

  5. Fukasawa T., et al. A case of recurrent encephalopathy with SCN2A missense mutation. Brain Development. 2015, 37(6):631-4. PubMed ID: 25457084

    This article suggests that the SCN2A mutations might predispose children to repetitive encephalopathy with variable clinical and imaging findings.

SCN2A Preparation Options

Membrane protein studies have advanced significantly over the past few years. Based on our versatile Magic™ membrane protein production platform, we could offer a series of membrane protein preparation services for worldwide customers in reconstitution forms as well as multiple active formats. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SCN2A antibody development services.


Creative Biolabs has successfully generated many functional membrane proteins with multiple formats for our global customers. We are happy to accelerate the development of our clients’ programs with our one-stop, custom-oriented service. For more detailed information, please feel free to contact us.

Reference

  1. Vandenbeuch A and Kinnamon S C. (2009). Why do taste cells generate action potentials? Journal of Biology. 8(4): 42.

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