ID   SCN2B_CANLF             Reviewed;         215 AA.
AC   Q864L3;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Sodium channel subunit beta-2;
DE   Flags: Precursor;
GN   Name=SCN2B;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mishra S., Sabbah H.N., Undrovinas A.I.;
RT   "Cloning of dog cardiomyocyte sodium channel beta-2 subunit cDNA.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
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; Single-pass type I membrane protein.
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN2B (TC
CC       8.A.17) family. {ECO:0000305}.
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DR   EMBL; AY263393; AAP30026.2; -; mRNA.
DR   STRING; 9612.ENSCAFP00000042471; -.
DR   eggNOG; ENOG502R29H; Eukaryota.
DR   InParanoid; Q864L3; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IBA:GO_Central.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IBA:GO_Central.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; IBA:GO_Central.
DR   GO; GO:0086012; P:membrane depolarization during cardiac muscle cell action potential; IBA:GO_Central.
DR   GO; GO:2000649; P:regulation of sodium ion transmembrane transporter activity; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Immunoglobulin domain; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Signal;
KW   Sodium; Sodium channel; Sodium transport; Transmembrane;
KW   Transmembrane helix; Transport; 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_0000014930"
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          190..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   MOD_RES         204
FT                   /note="Phosphothreonine"
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:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        55
FT                   /note="Interchain; with alpha subunit"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        72..75
FT                   /evidence="ECO:0000250|UniProtKB:O60939"
SQ   SEQUENCE   215 AA;  24306 MW;  D5A30A7CCF569F9F CRC64;
     MHRDAWLPRP AFSLTGLSLF FSLVPPGRSM EVTVPATLNV LNGSDARLPC TFNSCYTVNH
     KQFSLNWTYQ ECNNCSEEMF LQFRMKIINL KLERFQDRVE FSGNPSKYDV SVMLRNVQPE
     DEGIYNCYIM NPPDRHRGHG KIHLQVLXEE PPERDSTVAV IVGASVGGFL AVVILVLMVV
     KCVRRKKEQK LSTDDLKTEE EGKTDGEGNP DDGAK