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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}.
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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
 
 
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