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SCN2B_MOUSE
ID   SCN2B_MOUSE             Reviewed;         215 AA.
AC   Q56A07;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Sodium channel subunit beta-2;
DE   Flags: Precursor;
GN   Name=Scn2b; Synonyms=Gm183;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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   [2]
RP   PROTEIN SEQUENCE OF 99-107, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [3]
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: 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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250|UniProtKB:O60939}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B (TC
CC       8.A.17) family. {ECO:0000305}.
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DR   EMBL; BC092225; AAH92225.1; -; mRNA.
DR   CCDS; CCDS40606.1; -.
DR   RefSeq; NP_001014761.1; NM_001014761.2.
DR   AlphaFoldDB; Q56A07; -.
DR   SMR; Q56A07; -.
DR   STRING; 10090.ENSMUSP00000126826; -.
DR   BindingDB; Q56A07; -.
DR   ChEMBL; CHEMBL4630761; -.
DR   ChEMBL; CHEMBL4630764; -.
DR   ChEMBL; CHEMBL4630766; -.
DR   GlyGen; Q56A07; 3 sites.
DR   iPTMnet; Q56A07; -.
DR   PhosphoSitePlus; Q56A07; -.
DR   MaxQB; Q56A07; -.
DR   PaxDb; Q56A07; -.
DR   PRIDE; Q56A07; -.
DR   ProteomicsDB; 253412; -.
DR   ABCD; Q56A07; 1 sequenced antibody.
DR   Antibodypedia; 2511; 310 antibodies from 33 providers.
DR   DNASU; 72821; -.
DR   Ensembl; ENSMUST00000093855; ENSMUSP00000091377; ENSMUSG00000070304.
DR   Ensembl; ENSMUST00000170998; ENSMUSP00000126826; ENSMUSG00000070304.
DR   GeneID; 72821; -.
DR   KEGG; mmu:72821; -.
DR   UCSC; uc009pfg.1; mouse.
DR   CTD; 6327; -.
DR   MGI; MGI:106921; Scn2b.
DR   VEuPathDB; HostDB:ENSMUSG00000070304; -.
DR   eggNOG; ENOG502R29H; Eukaryota.
DR   GeneTree; ENSGT01030000234556; -.
DR   HOGENOM; CLU_090350_0_0_1; -.
DR   InParanoid; Q56A07; -.
DR   OMA; NCYVTNP; -.
DR   OrthoDB; 1380581at2759; -.
DR   PhylomeDB; Q56A07; -.
DR   TreeFam; TF331728; -.
DR   Reactome; R-MMU-5576892; Phase 0 - rapid depolarisation.
DR   BioGRID-ORCS; 72821; 2 hits in 71 CRISPR screens.
DR   PRO; PR:Q56A07; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; Q56A07; protein.
DR   Bgee; ENSMUSG00000070304; Expressed in cerebellum lobe and 193 other tissues.
DR   ExpressionAtlas; Q56A07; baseline and differential.
DR   Genevisible; Q56A07; MM.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0030315; C:T-tubule; IDA:MGI.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; ISO:MGI.
DR   GO; GO:0017080; F:sodium channel regulator activity; ISO:MGI.
DR   GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IMP:MGI.
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:MGI.
DR   GO; GO:0061337; P:cardiac conduction; IMP:MGI.
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:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:Ensembl.
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:0009408; P:response to heat; IMP:MGI.
DR   GO; GO:0046684; P:response to pyrethroid; ISO:MGI.
DR   GO; GO:0035725; P:sodium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0006814; P:sodium ion transport; IMP:MGI.
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:0000250"
FT   CHAIN           30..215
FT                   /note="Sodium channel subunit beta-2"
FT                   /id="PRO_0000045177"
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          188..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:0000250|UniProtKB:P54900"
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:0000250|UniProtKB:O60939,
FT                   ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        72..75
FT                   /evidence="ECO:0000250|UniProtKB:O60939"
SQ   SEQUENCE   215 AA;  24228 MW;  38C1687665924FD7 CRC64;
     MHRDAWLPRP AFSLTGLSLF FSLVPPGRSM EVTAPTTLSV LNGSDTRLPC TFNSCYTVNH
     KQFSLNWTYQ ECNNCTEEMF LQFRMKIINL KLERFGDRVE FSGNPSKYDV SVTLKNVQLE
     DEGIYNCYIT NPPDRHRGHG KIYLQVLLEV PPERDSTVAV IVGASVGGFL AVVILVLMVV
     KCVRRKKEQK LSTDDLKTEE EGKMDGEGNA EDGTK
 
 
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