SCN2B_RAT
ID SCN2B_RAT Reviewed; 215 AA.
AC P54900;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Sodium channel subunit beta-2;
DE Flags: Precursor;
GN Name=Scn2b;
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], AND PROTEIN SEQUENCE OF 30-58; 95-134 AND
RP 142-151.
RX PubMed=8521473; DOI=10.1016/0092-8674(95)90121-3;
RA Isom L.L., Ragsdale D.S., de Jongh K.S., Westenbroek R.E., Reber B.F.X.,
RA Scheuer T., Catterall W.A.;
RT "Structure and function of the beta 2 subunit of brain sodium channels, a
RT transmembrane glycoprotein with a CAM motif.";
RL Cell 83:433-442(1995).
RN [2]
RP PROTEIN SEQUENCE OF 30-61; 99-135 AND 191-197, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [3]
RP SUBUNIT, INTERACTION WITH TNR, AND FUNCTION.
RX PubMed=9861042; DOI=10.1073/pnas.95.26.15753;
RA Srinivasan J., Schachner M., Catterall W.A.;
RT "Interaction of voltage-gated sodium channels with the extracellular matrix
RT molecules tenascin-C and tenascin-R.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:15753-15757(1998).
RN [4]
RP SUBUNIT, AND INTERACTION WITH SCN10A.
RX PubMed=15178439; DOI=10.1016/j.bbrc.2004.05.026;
RA Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.;
RT "Role of auxiliary beta1-, beta2-, and beta3-subunits and their interaction
RT with Na(v)1.8 voltage-gated sodium channel.";
RL Biochem. Biophys. Res. Commun. 319:531-540(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND THR-204, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=26894959; DOI=10.7554/elife.10960;
RA Das S., Gilchrist J., Bosmans F., Van Petegem F.;
RT "Binary architecture of the Nav1.2-beta2 signaling complex.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Crucial in the assembly, expression, and functional
CC modulation of the heterotrimeric complex of the sodium channel. The
CC subunit beta-2 causes an increase in the plasma membrane surface area
CC and in its folding into microvilli. Interacts with TNR may play a
CC crucial role in clustering and regulation of activity of sodium
CC channels at nodes of Ranvier. {ECO:0000269|PubMed:9861042}.
CC -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC conducting pore forming alpha-subunit (SCN2A) regulated by one or more
CC beta subunits (SCN1B, SCN2B, SCN3B and SCN4B). SCN1B and SCN3B are non-
CC covalently associated with SCN2A. SCN2B and SCN4B are disulfide-linked
CC to SCN2A (PubMed:26894959). Interacts with SCN10A and TNR.
CC {ECO:0000269|PubMed:15178439, ECO:0000269|PubMed:9861042}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- TISSUE SPECIFICITY: Brain specific.
CC -!- DEVELOPMENTAL STAGE: Detected in the earliest phase of neurogenesis in
CC brain, and expression is greatly increased concomitant with axon
CC extension and synaptogenesis.
CC -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B (TC
CC 8.A.17) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U37026; AAC52967.1; -; mRNA.
DR PIR; A57843; A57843.
DR RefSeq; NP_037009.1; NM_012877.1.
DR AlphaFoldDB; P54900; -.
DR SMR; P54900; -.
DR BioGRID; 247388; 2.
DR STRING; 10116.ENSRNOP00000021819; -.
DR GlyGen; P54900; 3 sites.
DR iPTMnet; P54900; -.
DR PhosphoSitePlus; P54900; -.
DR PaxDb; P54900; -.
DR PRIDE; P54900; -.
DR ABCD; P54900; 1 sequenced antibody.
DR DNASU; 25349; -.
DR Ensembl; ENSRNOT00000106113; ENSRNOP00000078627; ENSRNOG00000063505.
DR GeneID; 25349; -.
DR KEGG; rno:25349; -.
DR UCSC; RGD:3633; rat.
DR CTD; 6327; -.
DR RGD; 3633; Scn2b.
DR eggNOG; ENOG502R29H; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_090350_0_0_1; -.
DR InParanoid; P54900; -.
DR OMA; NCYVTNP; -.
DR OrthoDB; 1380581at2759; -.
DR PhylomeDB; P54900; -.
DR TreeFam; TF331728; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:P54900; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000016221; Expressed in frontal cortex and 14 other tissues.
DR Genevisible; P54900; RN.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; ISO:RGD.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; ISO:RGD.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
DR GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0061337; P:cardiac conduction; ISO:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; ISO:RGD.
DR GO; GO:0010467; P:gene expression; ISO:RGD.
DR GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; IEP:RGD.
DR GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0009408; P:response to heat; ISO:RGD.
DR GO; GO:0046684; P:response to pyrethroid; IDA:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR000920; Myelin_P0-rel.
DR InterPro; IPR029873; SCN2B.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF3; PTHR13869:SF3; 1.
DR Pfam; PF07686; V-set; 1.
DR PRINTS; PR00213; MYELINP0.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Immunoglobulin domain; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Signal; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:8521473"
FT CHAIN 30..215
FT /note="Sodium channel subunit beta-2"
FT /id="PRO_0000014932"
FT TOPO_DOM 30..159
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..215
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..154
FT /note="Ig-like C2-type"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 56
FT /note="Binds SCN2A"
FT /evidence="ECO:0000250|UniProtKB:O60939"
FT SITE 135
FT /note="Binds SCN2A"
FT /evidence="ECO:0000250|UniProtKB:O60939"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 204
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 42
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 50..127
FT /evidence="ECO:0000250|UniProtKB:O60939,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 55
FT /note="Interchain; with alpha subunit"
FT /evidence="ECO:0000269|PubMed:26894959"
FT DISULFID 72..75
FT /evidence="ECO:0000250|UniProtKB:O60939"
FT VARIANT 80
FT /note="F -> V"
SQ SEQUENCE 215 AA; 24145 MW; 23D432EA83C1459D CRC64;
MHRDAWLPRP AFSLTGLSLF FSLVPSGRSM EVTVPTTLSV LNGSDTRLPC TFNSCYTVNH
KQFSLNWTYQ ECSNCSEEMF LQFRMKIINL KLERFGDRVE FSGNPSKYDV SVTLKNVQLE
DEGIYNCYIT NPPDRHRGHG KIYLQVLLEV PPERDSTVAV IVGASVGGFL AVVILVLMVV
KCVRRKKEQK LSTDDLKTEE EGKTDGEGNA EDGAK