ID   SCN3B_MACFA             Reviewed;         215 AA.
AC   Q8HXJ7;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Sodium channel subunit beta-3;
DE   Flags: Precursor;
GN   Name=SCN3B; ORFNames=QmoA-13657;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Medulla oblongata;
RX   PubMed=11574149; DOI=10.1016/s0378-1119(01)00665-5;
RA   Osada N., Hida M., Kususda J., Tanuma R., Iseki K., Hirata M., Suto Y.,
RA   Hirai M., Terao K., Suzuki Y., Sugano S., Hashimoto K.;
RT   "Assignment of 118 novel cDNAs of cynomolgus monkey brain to human
RT   chromosomes.";
RL   Gene 275:31-37(2001).
CC   -!- FUNCTION: Modulates channel gating kinetics. Causes unique persistent
CC       sodium currents. Inactivates the sodium channel opening more slowly
CC       than the subunit beta-1. Its association with NFASC may target the
CC       sodium channels to the nodes of Ranvier of developing axons and retain
CC       these channels at the nodes in mature myelinated axons (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The voltage-sensitive sodium channel consists of an ion
CC       conducting pore forming alpha-subunit regulated by one or more beta-1,
CC       beta-2, beta-3 and/or beta-4 subunits. Beta-1 and beta-3 are non-
CC       covalently associated with alpha, while beta-2 and beta-4 are
CC       covalently linked by disulfide bonds (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the sodium channel auxiliary subunit SCN3B (TC
CC       8.A.17) family. {ECO:0000305}.
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DR   EMBL; AB097521; BAC41746.1; -; mRNA.
DR   RefSeq; NP_001271569.1; NM_001284640.1.
DR   AlphaFoldDB; Q8HXJ7; -.
DR   SMR; Q8HXJ7; -.
DR   STRING; 9541.XP_005580051.1; -.
DR   Ensembl; ENSMFAT00000022770; ENSMFAP00000004109; ENSMFAG00000001774.
DR   GeneID; 102139038; -.
DR   CTD; 55800; -.
DR   VEuPathDB; HostDB:ENSMFAG00000001774; -.
DR   eggNOG; ENOG502QWH0; Eukaryota.
DR   GeneTree; ENSGT00390000018560; -.
DR   OMA; LIFEYRN; -.
DR   OrthoDB; 1198549at2759; -.
DR   Proteomes; UP000233100; Chromosome 14.
DR   Bgee; ENSMFAG00000001774; Expressed in temporal lobe and 4 other tissues.
DR   GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:InterPro.
DR   GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0017080; F:sodium channel regulator activity; IEA:InterPro.
DR   GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR   GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR027098; Na_channel_b1/b3.
DR   InterPro; IPR027096; Na_channel_b3.
DR   PANTHER; PTHR10546; PTHR10546; 1.
DR   PANTHER; PTHR10546:SF1; PTHR10546:SF1; 1.
DR   Pfam; PF07686; V-set; 1.
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; Reference proteome; Signal; Sodium;
KW   Sodium channel; Sodium transport; Transmembrane; Transmembrane helix;
KW   Transport; Voltage-gated channel.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..215
FT                   /note="Sodium channel subunit beta-3"
FT                   /id="PRO_0000014934"
FT   TOPO_DOM        23..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          24..138
FT                   /note="Ig-like C2-type"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        121
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   DISULFID        45..120
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ   SEQUENCE   215 AA;  24702 MW;  25319D5ED218AACF CRC64;
     MPAFNRLFPL VSLVLIYWAS VCFPVCVEVP SETEAVQGNP MKLRCISCMK REEVEATTVV
     EWFYRPEGGK DFLIYEYRNG HQEVESPFQG RLQWNGSKDL QDVSITVLNV TLNDSGLYTC
     NVSREFEFEA HRPFVKTTRL IPLRVTEEAG EDFTSVVSEI MMYILLVFLT LWLLIEMIYC
     YRKVSKAEEA AQENASDYLA IPSENKENSA VPVEE