SCN1B_RAT
ID SCN1B_RAT Reviewed; 218 AA.
AC Q00954; Q505J0;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Sodium channel subunit beta-1;
DE Flags: Precursor;
GN Name=Scn1b;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=1375395; DOI=10.1126/science.1375395;
RA Isom L.L., De Jongh K.S., Patton D.E., Reber B.F.X., Offord J.,
RA Charbonneau H., Walsh K., Goldin A.L., Catterall W.A.;
RT "Primary structure and functional expression of the beta 1 subunit of the
RT rat brain sodium channel.";
RL Science 256:839-842(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=8282123; DOI=10.1016/0014-5793(93)80871-q;
RA Wallner M., Weigl L., Meera P., Lotan I.;
RT "Modulation of the skeletal muscle sodium channel alpha-subunit by the beta
RT 1-subunit.";
RL FEBS Lett. 336:535-539(1993).
RN [4]
RP FUNCTION.
RX PubMed=8021275; DOI=10.1016/s0021-9258(17)32490-0;
RA Patton D.E., Isom L.L., Catterall W.A., Goldin A.L.;
RT "The adult rat brain beta 1 subunit modifies activation and inactivation
RT gating of multiple sodium channel alpha subunits.";
RL J. Biol. Chem. 269:17649-17655(1994).
RN [5]
RP SUBCELLULAR LOCATION, INTERACTION WITH NFASC, DEVELOPMENTAL STAGE, AND
RP TISSUE SPECIFICITY.
RX PubMed=11470829; DOI=10.1083/jcb.200102086;
RA Ratcliffe C.F., Westenbroek R.E., Curtis R., Catterall W.A.;
RT "Sodium channel beta1 and beta3 subunits associate with neurofascin through
RT their extracellular immunoglobulin-like domain.";
RL J. Cell Biol. 154:427-434(2001).
RN [6]
RP FUNCTION, 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 [7]
RP DISULFIDE BOND.
RX PubMed=22425777; DOI=10.1016/j.bbrc.2012.02.163;
RA Barbieri R., Baroni D., Moran O.;
RT "Identification of an intra-molecular disulfide bond in the sodium channel
RT beta1-subunit.";
RL Biochem. Biophys. Res. Commun. 420:364-367(2012).
RN [8]
RP FUNCTION, INTERACTION WITH SCN4A, AND MUTAGENESIS OF 109-THR-ASN-110.
RX PubMed=28012039; DOI=10.1007/s00249-016-1193-3;
RA Sanchez-Solano A., Islas A.A., Scior T., Paiz-Candia B.,
RA Millan-PerezPena L., Salinas-Stefanon E.M.;
RT "Characterization of specific allosteric effects of the Na+ channel beta1
RT subunit on the Nav1.4 isoform.";
RL Eur. Biophys. J. 46:485-494(2017).
CC -!- FUNCTION: Regulatory subunit of multiple voltage-gated sodium channel
CC complexes that play important roles in excitable membranes in brain,
CC heart and skeletal muscle (PubMed:1375395, PubMed:8282123,
CC PubMed:8021275, PubMed:15178439, PubMed:28012039). Enhances the
CC presence of the pore-forming alpha subunit at the cell surface and
CC modulates channel gating characteristics and the rate of channel
CC inactivation (PubMed:1375395, PubMed:8282123, PubMed:8021275,
CC PubMed:15178439, PubMed:28012039). Modulates the activity of a variety
CC of pore-forming alpha subunits, such as SCN1A, SCN2A, SCN3A, SCN4A,
CC SCN5A and SCN10A (PubMed:1375395, PubMed:8282123, PubMed:8021275,
CC PubMed:15178439, PubMed:28012039). {ECO:0000269|PubMed:1375395,
CC ECO:0000269|PubMed:15178439, ECO:0000269|PubMed:28012039,
CC ECO:0000269|PubMed:8021275, ECO:0000269|PubMed:8282123}.
CC -!- SUBUNIT: Component of a voltage-sensitive sodium channel complex that
CC consists of a pore-forming alpha subunit and one or more regulatory
CC beta subunits (PubMed:1375395, PubMed:28012039). Interacts with SCN4A
CC (PubMed:28012039). Interacts with NFASC (PubMed:11470829). Interacts
CC with SCN10A (PubMed:15178439). Interacts with SCN1A. Interacts with
CC SCN3A. Interacts with SCN5A. Interacts with SCN8A (By similarity).
CC {ECO:0000250|UniProtKB:Q07699, ECO:0000269|PubMed:11470829,
CC ECO:0000269|PubMed:1375395, ECO:0000269|PubMed:15178439,
CC ECO:0000269|PubMed:28012039}.
CC -!- INTERACTION:
CC Q00954; P21707: Syt1; NbExp=2; IntAct=EBI-2619363, EBI-458098;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11470829};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07699}.
CC Perikaryon {ECO:0000250|UniProtKB:P97952}. Cell projection
CC {ECO:0000250|UniProtKB:P97952}. Cell projection, axon
CC {ECO:0000269|PubMed:11470829}. Note=Detected at nodes of Ranvier on the
CC sciatic nerve. {ECO:0000269|PubMed:11470829}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:11470829). Expressed in brain, heart, skeletal muscle and
CC spinal cord (PubMed:1375395, PubMed:8282123).
CC {ECO:0000269|PubMed:11470829, ECO:0000269|PubMed:1375395,
CC ECO:0000269|PubMed:8282123}.
CC -!- DEVELOPMENTAL STAGE: In developing nodes of Ranvier, it is localized in
CC the sciatic nerve at postnatal days 3 and 10, during the process of
CC myelination and maturation of the nodes. {ECO:0000269|PubMed:11470829}.
CC -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN1B (TC
CC 8.A.17) family. {ECO:0000305}.
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DR EMBL; M91808; AAA88513.1; -; mRNA.
DR EMBL; BC094523; AAH94523.1; -; mRNA.
DR PIR; A42737; A42737.
DR RefSeq; NP_001257974.1; NM_001271045.1.
DR RefSeq; NP_058984.1; NM_017288.2.
DR AlphaFoldDB; Q00954; -.
DR SMR; Q00954; -.
DR BioGRID; 248306; 2.
DR CORUM; Q00954; -.
DR IntAct; Q00954; 2.
DR STRING; 10116.ENSRNOP00000028653; -.
DR ChEMBL; CHEMBL4524040; -.
DR GlyGen; Q00954; 4 sites, 3 N-linked glycans (1 site).
DR iPTMnet; Q00954; -.
DR PhosphoSitePlus; Q00954; -.
DR PaxDb; Q00954; -.
DR PRIDE; Q00954; -.
DR ABCD; Q00954; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000028653; ENSRNOP00000028653; ENSRNOG00000021102.
DR GeneID; 29686; -.
DR KEGG; rno:29686; -.
DR UCSC; RGD:3631; rat.
DR CTD; 6324; -.
DR RGD; 3631; Scn1b.
DR eggNOG; ENOG502R0UM; Eukaryota.
DR GeneTree; ENSGT00390000018560; -.
DR HOGENOM; CLU_096296_0_0_1; -.
DR InParanoid; Q00954; -.
DR OMA; DRIDWNG; -.
DR OrthoDB; 1345300at2759; -.
DR PhylomeDB; Q00954; -.
DR TreeFam; TF332097; -.
DR Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
DR PRO; PR:Q00954; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000021102; Expressed in skeletal muscle tissue and 20 other tissues.
DR ExpressionAtlas; Q00954; baseline and differential.
DR Genevisible; Q00954; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0014704; C:intercalated disc; ISO:RGD.
DR GO; GO:0033268; C:node of Ranvier; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034706; C:sodium channel complex; ISO:RGD.
DR GO; GO:0030315; C:T-tubule; ISO:RGD.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IDA:UniProtKB.
DR GO; GO:0019871; F:sodium channel inhibitor activity; ISO:RGD.
DR GO; GO:0017080; F:sodium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
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:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; ISO:RGD.
DR GO; GO:0007411; P:axon guidance; 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:0021966; P:corticospinal neuron axon guidance; ISO:RGD.
DR GO; GO:0040011; P:locomotion; ISO:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:RGD.
DR GO; GO:0019227; P:neuronal action potential propagation; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO: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:0002028; P:regulation of sodium ion transport; IDA:RGD.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; IDA:UniProtKB.
DR GO; GO:0046684; P:response to pyrethroid; IDA:RGD.
DR GO; GO:0035725; P:sodium ion transmembrane transport; ISO:RGD.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR027098; Na_channel_b1/b3.
DR InterPro; IPR044568; Na_chnl_b1.
DR PANTHER; PTHR10546; PTHR10546; 1.
DR PANTHER; PTHR10546:SF2; PTHR10546:SF2; 1.
DR Pfam; PF07686; V-set; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Ion channel; Ion transport; Membrane;
KW Reference proteome; Signal; Sodium; Sodium channel; Sodium transport;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT SIGNAL 1..18
FT CHAIN 19..218
FT /note="Sodium channel subunit beta-1"
FT /id="PRO_0000014929"
FT TOPO_DOM 19..160
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..150
FT /note="Ig-like C2-type"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 21..43
FT /evidence="ECO:0000250|UniProtKB:Q07699"
FT DISULFID 40..121
FT /evidence="ECO:0000269|PubMed:22425777"
FT MUTAGEN 109..110
FT /note="TN->AA: Strongly decreased ability to mediate rapid
FT channel inactivation."
FT /evidence="ECO:0000269|PubMed:28012039"
SQ SEQUENCE 218 AA; 24692 MW; 0BA84FC44FF2306B CRC64;
MGTLLALVVG AVLVSSAWGG CVEVDSETEA VYGMTFKILC ISCKRRSETT AETFTEWTFR
QKGTEEFVKI LRYENEVLQL EEDERFEGRV VWNGSRGTKD LQDLSIFITN VTYNHSGDYE
CHVYRLLFFD NYEHNTSVVK KIHLEVVDKA NRDMASIVSE IMMYVLIVVL TIWLVAEMVY
CYKKIAAATE AAAQENASEY LAITSESKEN CTGVQVAE
