SCN4B_RAT
ID SCN4B_RAT Reviewed; 228 AA.
AC Q7M730; Q80Z84;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Sodium channel subunit beta-4;
DE Flags: Precursor;
GN Name=Scn4b;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 134-228, FUNCTION, TISSUE SPECIFICITY,
RP SUBUNIT, INTERACTION WITH SCN2A, DISULFIDE BONDS, AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley;
RX PubMed=12930796; DOI=10.1523/jneurosci.23-20-07577.2003;
RA Yu F.H., Westenbroek R.E., Silos-Santiago I., McCormick K.A., Lawson D.,
RA Ge P., Ferriera H., Lilly J., DiStefano P.S., Catterall W.A., Scheuer T.,
RA Curtis R.;
RT "Sodium channel beta4, a new disulfide-linked auxiliary subunit with
RT similarity to beta2.";
RL J. Neurosci. 23:7577-7585(2003).
RN [3]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-71, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [4]
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: Modulates channel gating kinetics. Causes negative shifts in
CC the voltage dependence of activation of certain alpha sodium channels,
CC but does not affect the voltage dependence of inactivation. Modulates
CC the susceptibility of the sodium channel to inhibition by toxic
CC peptides from spider, scorpion, wasp and sea anemone venom.
CC {ECO:0000269|PubMed:12930796}.
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:12930796, PubMed:26894959).
CC {ECO:0000269|PubMed:12930796, ECO:0000269|PubMed:26894959}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12930796};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:12930796}.
CC -!- TISSUE SPECIFICITY: Expressed at a high level in dorsal root ganglia,
CC at a lower level in brain, spinal cord, skeletal muscle and heart.
CC {ECO:0000269|PubMed:12930796}.
CC -!- PTM: Contains an interchain disulfide bond with SCN2A.
CC -!- PTM: N-glycosylated.
CC -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN4B (TC
CC 8.A.17) family. {ECO:0000305}.
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DR EMBL; AC129680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC129457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC136555; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF544988; AAO62631.1; -; mRNA.
DR EMBL; BK001030; DAA01204.1; -; mRNA.
DR RefSeq; NP_001008880.1; NM_001008880.1.
DR AlphaFoldDB; Q7M730; -.
DR SMR; Q7M730; -.
DR STRING; 10116.ENSRNOP00000033284; -.
DR GlyGen; Q7M730; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q7M730; -.
DR PhosphoSitePlus; Q7M730; -.
DR PaxDb; Q7M730; -.
DR PRIDE; Q7M730; -.
DR ABCD; Q7M730; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000030152; ENSRNOP00000033284; ENSRNOG00000026679.
DR GeneID; 315611; -.
DR KEGG; rno:315611; -.
DR UCSC; RGD:631404; rat.
DR CTD; 6330; -.
DR RGD; 631404; Scn4b.
DR eggNOG; ENOG502QTZ6; Eukaryota.
DR GeneTree; ENSGT01030000234556; -.
DR HOGENOM; CLU_104235_0_0_1; -.
DR InParanoid; Q7M730; -.
DR OMA; EGQYICF; -.
DR OrthoDB; 1219179at2759; -.
DR PhylomeDB; Q7M730; -.
DR TreeFam; TF331728; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:Q7M730; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000026679; Expressed in skeletal muscle tissue and 10 other tissues.
DR Genevisible; Q7M730; RN.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0031226; C:intrinsic component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:UniProtKB.
DR GO; GO:0017080; F:sodium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:RGD.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; ISO:RGD.
DR GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0086016; P:AV node cell action potential; 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:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; 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; ISS:UniProtKB.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO: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; IPR044572; Na_channel_b4.
DR PANTHER; PTHR13869; PTHR13869; 1.
DR PANTHER; PTHR13869:SF14; PTHR13869:SF14; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Ion channel; Ion transport; Membrane; Reference proteome; Signal; Sodium;
KW Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW Transport; Voltage-gated channel.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..228
FT /note="Sodium channel subunit beta-4"
FT /id="PRO_0000014939"
FT TOPO_DOM 31..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..148
FT /note="Ig-like C2-type"
FT REGION 199..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..131
FT /evidence="ECO:0000250|UniProtKB:Q8IWT1,
FT ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 58
FT /note="Interchain; with alpha subunit"
FT /evidence="ECO:0000250|UniProtKB:Q8IWT1,
FT ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000305|PubMed:26894959"
SQ SEQUENCE 228 AA; 25247 MW; 8E5A752281D25DEC CRC64;
MSRAGNRGNT QARWLGIGLL GLFLLPMYLS LEVSVGKATT IYAINGSAIL LPCTFSSCYG
FENLYFRWSY NNSETSRILI DGIVKNDKSD PKVRVKDDDR ITLEGSTKEK MNNISILLSD
LEFSDTGRYT CFVRNPKEKD LNNSATIFLQ VVDKLEEVDN TVTLIILAVV GGVIGLLVCI
LLLKKLITFI LKKTREKKKE CLVSSSGNDN TENGLPGSKA EEKPPTKV
