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SCN1B_MOUSE
ID   SCN1B_MOUSE             Reviewed;         218 AA.
AC   P97952;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Sodium channel subunit beta-1;
DE   Flags: Precursor;
GN   Name=Scn1b;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=9013777; DOI=10.1016/s0169-328x(96)00123-4;
RA   Grosson C.L.S., Cannon S.C., Corey D.P., Gusella J.F.;
RT   "Sequence of the voltage-gated sodium channel beta1-subunit in wild-type
RT   and in quivering mice.";
RL   Brain Res. Mol. Brain Res. 42:222-226(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9721701; DOI=10.1161/01.res.83.4.441;
RA   Kupershmidt S., Yang T., Roden D.M.;
RT   "Modulation of cardiac Na+ current phenotype by beta1-subunit expression.";
RL   Circ. Res. 83:441-447(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19710327; DOI=10.1523/jneurosci.2475-09.2009;
RA   Patino G.A., Claes L.R., Lopez-Santiago L.F., Slat E.A., Dondeti R.S.,
RA   Chen C., O'Malley H.A., Gray C.B., Miyazaki H., Nukina N., Oyama F.,
RA   De Jonghe P., Isom L.L.;
RT   "A functional null mutation of SCN1B in a patient with Dravet syndrome.";
RL   J. Neurosci. 29:10764-10778(2009).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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. Enhances the presence of the pore-forming
CC       alpha subunit at the cell surface and modulates channel gating
CC       characteristics and the rate of channel inactivation. Modulates the
CC       activity of a variety of pore-forming alpha subunits, such as SCN1A,
CC       SCN2A, SCN3A, SCN4A, SCN5A and SCN10A. {ECO:0000250|UniProtKB:Q00954}.
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. Interacts with SCN4A. Interacts with NFASC. Interacts
CC       with SCN10A (By similarity). Interacts with SCN1A. Interacts with
CC       SCN3A. Interacts with SCN5A. Interacts with SCN8A (By similarity).
CC       {ECO:0000250|UniProtKB:Q00954, ECO:0000250|UniProtKB:Q07699}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19710327};
CC       Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q07699}.
CC       Perikaryon {ECO:0000269|PubMed:19710327}. Cell projection
CC       {ECO:0000269|PubMed:19710327}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q00954}. Note=Detected at nodes of Ranvier on
CC       the sciatic nerve. {ECO:0000269|PubMed:19710327}.
CC   -!- TISSUE SPECIFICITY: Detected in hippocampus CA3 bipolar neurons (at
CC       protein level) (PubMed:19710327). Detected in skeletal muscle
CC       (PubMed:9013777). {ECO:0000269|PubMed:19710327,
CC       ECO:0000269|PubMed:9013777}.
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN1B (TC
CC       8.A.17) family. {ECO:0000305}.
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DR   EMBL; U46681; AAC53006.1; -; mRNA.
DR   EMBL; U85786; AAB49368.1; -; mRNA.
DR   EMBL; BC009652; AAH09652.1; -; mRNA.
DR   EMBL; BC039140; AAH39140.1; -; mRNA.
DR   CCDS; CCDS21126.1; -.
DR   RefSeq; NP_035452.1; NM_011322.3.
DR   AlphaFoldDB; P97952; -.
DR   SMR; P97952; -.
DR   STRING; 10090.ENSMUSP00000096148; -.
DR   BindingDB; P97952; -.
DR   ChEMBL; CHEMBL4630761; -.
DR   ChEMBL; CHEMBL4630764; -.
DR   ChEMBL; CHEMBL4630766; -.
DR   GlyConnect; 2720; 8 N-Linked glycans (2 sites).
DR   GlyGen; P97952; 4 sites, 8 N-linked glycans (2 sites).
DR   iPTMnet; P97952; -.
DR   PhosphoSitePlus; P97952; -.
DR   SwissPalm; P97952; -.
DR   jPOST; P97952; -.
DR   PaxDb; P97952; -.
DR   PeptideAtlas; P97952; -.
DR   PRIDE; P97952; -.
DR   ProteomicsDB; 253411; -.
DR   ABCD; P97952; 1 sequenced antibody.
DR   Antibodypedia; 29258; 220 antibodies from 29 providers.
DR   DNASU; 20266; -.
DR   Ensembl; ENSMUST00000098548; ENSMUSP00000096148; ENSMUSG00000019194.
DR   Ensembl; ENSMUST00000211945; ENSMUSP00000148295; ENSMUSG00000019194.
DR   GeneID; 20266; -.
DR   KEGG; mmu:20266; -.
DR   UCSC; uc009gie.1; mouse.
DR   CTD; 6324; -.
DR   MGI; MGI:98247; Scn1b.
DR   VEuPathDB; HostDB:ENSMUSG00000019194; -.
DR   eggNOG; ENOG502R0UM; Eukaryota.
DR   GeneTree; ENSGT00390000018560; -.
DR   HOGENOM; CLU_096296_0_0_1; -.
DR   InParanoid; P97952; -.
DR   OMA; DRIDWNG; -.
DR   OrthoDB; 1345300at2759; -.
DR   PhylomeDB; P97952; -.
DR   TreeFam; TF332097; -.
DR   Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR   BioGRID-ORCS; 20266; 1 hit in 78 CRISPR screens.
DR   PRO; PR:P97952; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P97952; protein.
DR   Bgee; ENSMUSG00000019194; Expressed in superior frontal gyrus and 161 other tissues.
DR   Genevisible; P97952; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR   GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR   GO; GO:0033268; C:node of Ranvier; IDA:MGI.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0034706; C:sodium channel complex; IPI:MGI.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; ISS:UniProtKB.
DR   GO; GO:0019871; F:sodium channel inhibitor activity; IMP:BHF-UCL.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISS: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:MGI.
DR   GO; GO:0086006; F:voltage-gated sodium channel activity involved in cardiac muscle cell action potential; IMP:BHF-UCL.
DR   GO; GO:0086062; F:voltage-gated sodium channel activity involved in Purkinje myocyte action potential; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IMP:MGI.
DR   GO; GO:0061337; P:cardiac conduction; IMP:BHF-UCL.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR   GO; GO:0060048; P:cardiac muscle contraction; ISO:MGI.
DR   GO; GO:0021966; P:corticospinal neuron axon guidance; IMP:MGI.
DR   GO; GO:0040011; P:locomotion; IMP:MGI.
DR   GO; GO:0051899; P:membrane depolarization; ISO:MGI.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IMP:BHF-UCL.
DR   GO; GO:0086047; P:membrane depolarization during Purkinje myocyte cell action potential; ISO:MGI.
DR   GO; GO:0031175; P:neuron projection development; IGI:MGI.
DR   GO; GO:0019227; P:neuronal action potential propagation; IMP:MGI.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IGI:MGI.
DR   GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; ISO:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:MGI.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0002028; P:regulation of sodium ion transport; ISO:MGI.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IMP:BHF-UCL.
DR   GO; GO:1905150; P:regulation of voltage-gated sodium channel activity; ISO:MGI.
DR   GO; GO:0046684; P:response to pyrethroid; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; IMP:BHF-UCL.
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; Disulfide bond; Glycoprotein;
KW   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                   /evidence="ECO:0000250"
FT   CHAIN           19..218
FT                   /note="Sodium channel subunit beta-1"
FT                   /id="PRO_0000014927"
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:0000250|UniProtKB:Q07699"
SQ   SEQUENCE   218 AA;  24650 MW;  5198F3383B0A8CA5 CRC64;
     MGTLLALVVG AALVSSAWGG CVEVDSDTEA VYGMTFKILC ISCKRRSETT AETFTEWTFR
     QKGTEEFVKI LRYENEVLQL EEDERFEGRV VWNGSRGTKD LQDLSIFITN VTYNHSGDYE
     CHVYRLLFFD NYEHNTSVVK KIHLEVVDKA NRDMASIVSE IMMYVLIVVL TIWLVAEMVY
     CYKKIAAATE AAAQENASEY LAITSESKEN CTGVQVAE
 
 
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