SC4AB_DANRE
ID SC4AB_DANRE Reviewed; 1784 AA.
AC Q20JQ7; Q2XVR2;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Sodium channel protein type 4 subunit alpha B;
DE AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.4b;
GN Name=scn4ab; Synonyms=nav1.4b;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=16830092; DOI=10.1007/s00239-005-0287-9;
RA Novak A.E., Jost M.C., Lu Y., Taylor A.D., Zakon H.H., Ribera A.B.;
RT "Gene duplications and evolution of vertebrate voltage-gated sodium
RT channels.";
RL J. Mol. Evol. 63:208-221(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16303569; DOI=10.1016/j.cub.2005.10.068;
RA Venkatesh B., Lu S.Q., Dandona N., See S.L., Brenner S., Soong T.W.;
RT "Genetic basis of tetrodotoxin resistance in pufferfishes.";
RL Curr. Biol. 15:2069-2072(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pore-forming subunit of a voltage-gated sodium channel
CC complex through which Na(+) ions pass in accordance with their
CC electrochemical gradient. Alternates between resting, activated and
CC inactivated states. Required for normal muscle fiber excitability,
CC normal muscle contraction and relaxation cycles.
CC {ECO:0000250|UniProtKB:P35499}.
CC -!- ACTIVITY REGULATION: Channel activity is regulated by ancillary beta
CC subunits. Interaction with a beta subunit is required for rapid channel
CC inactivation and rapid recovery after inactivation, and prevents
CC decrease of channel activity in response to repetitive, high-frequency
CC depolarizations. {ECO:0000250|UniProtKB:P15390}.
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. {ECO:0000250|UniProtKB:P15390}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15390};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}.
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, heart, brain, spinal
CC cord, and eye. {ECO:0000269|PubMed:16830092}.
CC -!- DOMAIN: The sequence contains 4 internal repeats, each with 5
CC hydrophobic segments (S1, S2, S3, S5, S6) and one positively charged
CC segment (S4). Segments S4 are probably the voltage-sensors and are
CC characterized by a series of positively charged amino acids at every
CC third position. {ECO:0000250|UniProtKB:P35499}.
CC -!- PTM: Lacks the cysteine which covalently binds the conotoxin GVIIJ.
CC This cysteine (position 719) is speculated in other sodium channel
CC subunits alpha to be implied in covalent binding with the sodium
CC channel subunit beta-2 or beta-4. {ECO:0000250|UniProtKB:P15389}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC Nav1.4/SCN4A subfamily. {ECO:0000305}.
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DR EMBL; DQ149505; ABA54920.1; -; mRNA.
DR EMBL; DQ221254; ABB29446.2; -; Genomic_DNA.
DR EMBL; BC163558; AAI63558.1; -; mRNA.
DR RefSeq; NP_001038530.1; NM_001045065.1.
DR AlphaFoldDB; Q20JQ7; -.
DR SMR; Q20JQ7; -.
DR STRING; 7955.ENSDARP00000044156; -.
DR PaxDb; Q20JQ7; -.
DR GeneID; 564977; -.
DR KEGG; dre:564977; -.
DR CTD; 564977; -.
DR ZFIN; ZDB-GENE-051201-1; scn4ab.
DR eggNOG; KOG2301; Eukaryota.
DR HOGENOM; CLU_000540_5_0_1; -.
DR InParanoid; Q20JQ7; -.
DR PhylomeDB; Q20JQ7; -.
DR TreeFam; TF323985; -.
DR PRO; PR:Q20JQ7; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; 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; IBA:GO_Central.
DR GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
DR GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.20.120.350; -; 4.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001696; Na_channel_asu.
DR InterPro; IPR044564; Na_chnl_inactivation_gate.
DR InterPro; IPR010526; Na_trans_assoc.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037; PTHR10037; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR PRINTS; PR00170; NACHANNEL.
DR PROSITE; PS50096; IQ; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion channel; Ion transport;
KW Membrane; Reference proteome; Repeat; Sodium; Sodium channel;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..1784
FT /note="Sodium channel protein type 4 subunit alpha B"
FT /id="PRO_0000371318"
FT TOPO_DOM 1..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..149
FT /note="Helical; Name=S1 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 150..156
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 157..177
FT /note="Helical; Name=S2 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 178..191
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 192..209
FT /note="Helical; Name=S3 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 210..215
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 216..232
FT /note="Helical; Name=S4 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 233..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 252..271
FT /note="Helical; Name=S5 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 272..366
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 367..391
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 392..398
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 399..419
FT /note="Helical; Name=S6 of repeat I"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 420..568
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 569..587
FT /note="Helical; Name=S1 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 588..598
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 599..618
FT /note="Helical; Name=S2 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 619..632
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 633..652
FT /note="Helical; Name=S3 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 653..654
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 655..672
FT /note="Helical; Name=S4 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 673..688
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 689..707
FT /note="Helical; Name=S5 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 708..736
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 737..757
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 758..768
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 769..787
FT /note="Helical; Name=S6 of repeat II"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 788..973
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 974..991
FT /note="Helical; Name=S1 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 992..1004
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1005..1023
FT /note="Helical; Name=S2 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1024..1037
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1038..1056
FT /note="Helical; Name=S3 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1057..1064
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1065..1083
FT /note="Helical; Name=S4 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1084..1101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1102..1121
FT /note="Helical; Name=S5 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1122..1173
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1174..1195
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1196..1212
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1213..1234
FT /note="Helical; Name=S6 of repeat III"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1235..1297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1298..1315
FT /note="Helical; Name=S1 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1316..1326
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1327..1345
FT /note="Helical; Name=S2 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1346..1357
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1358..1375
FT /note="Helical; Name=S3 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1376..1388
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1389..1405
FT /note="Helical; Name=S4 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1406..1424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 1425..1442
FT /note="Helical; Name=S5 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1443..1464
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT INTRAMEM 1465..1487
FT /note="Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1488..1516
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1517..1539
FT /note="Helical; Name=S6 of repeat IV"
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT TOPO_DOM 1540..1784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 112..429
FT /note="I"
FT /evidence="ECO:0000305"
FT REPEAT 550..821
FT /note="II"
FT /evidence="ECO:0000305"
FT REPEAT 954..1269
FT /note="III"
FT /evidence="ECO:0000305"
FT REPEAT 1278..1575
FT /note="IV"
FT /evidence="ECO:0000305"
FT DOMAIN 1669..1698
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 29..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 455..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 870..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1255
FT /note="Important for rapid channel inactivation"
FT /evidence="ECO:0000250|UniProtKB:P15390"
FT COMPBIAS 455..469
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 337
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 279..335
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 344..350
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 721..727
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 759..768
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1131..1151
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT DISULFID 1495..1510
FT /evidence="ECO:0000250|UniProtKB:P35499"
FT CONFLICT 1089
FT /note="Missing (in Ref. 2; ABB29446 and 3; AAI63558)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1784 AA; 201663 MW; 63B260ED94E3BBFF CRC64;
MARLLPPTGT DVFRPLTLES LAEIDRRMAE EAAEQERMKE QNVKVAEEDL PKPTSDLEAG
KVLPFIYGDP PPNLLNVPIE ELDPYYKAQK TFIVIDKKNT IYRFNTEPAC YCLSPFNPVR
RAAIRILIHS LFSLVIMLTI LTNCVFMAMS DPPGWSKILE YVFTGIYTFE AMVKVLSRGF
CIGDFTFLRD PWNWLDFMVI SMAYLTEFVD LGNISALRTF RVLRALKTIT VIPGLKTIVG
ALIQSVKKLA DVMILTVFCL SVFALIGLQL FMGNLRQKCV LWPPVGWYSD NLTVLSNYTD
INGNGTANST FDYQKYINSE ENYYYVPGQM DPLVCGNSSD AGLCPEGYIC LKAGRNPNYG
YTSYDNFGWA FLALFRLMTQ DFWENLFQLT LRAAGKTYMI FFVVIIFLGS FYLINLILAV
VAMAYAEQNE ATAAEAKEKE EEYAKIMEQL KKQAEQKNGM VNGSKTSLSS KKKGDNDQMQ
SDYDGIALKP LSKSNGSKGN INYLEVPDSQ IRKPSVVSAV ESALDAQEDI ERPCPPGWYK
FADIFLKWDC CIPWVKFKRI VYLFVMDPFV DLGITLCIVL NTVFMAMEHY PMSVHVEEVL
AIGNLVFTGI FAAEMVLKLI ALDPYYYFQV GWNIFDSIIV TMSLVELMLA DVEGLSVLRS
FRLMRVFKLA KSWPTLNMLI KIIGNSVGAL GNLTLVLAII VFIFAVVGMQ LFGKSYTDSV
CKISSDCELP RWHMADFFHA FLIIFRVLCG EWIETMWDCM EVAGQGMCII VFMMVMVIGN
LVVLNLFLAL LLSSFSGDNL SASDDDGENN LQIAISRITR GIDWIKAFVN KHVRQCLNLK
PKEEGAKVNG EGDAKMNAIM NSSSSMVKVP IANGESDDDD GNGSSEDEDD EGRDINMKKK
NGDESSTCST VDKPPEVEDL VEEEEEDLTS PEDCYTENCI RRCPCLDLDV SQGKGKAWWN
FRKTCFAIVE HSYFETFIIF MILLSSGALA FEDIYIEQRR MIKIILEYAD QVFTYVFVVE
MLLKWVAYGF KVYFTNAWCW LDFLIVDVSL ISLTANILGY SELGAIKSLR TLRALRPLRA
LSRFEGMRVV VVNALVGAIP SIFNVLLVCL IFWLIFSIMG VNLFAGKFYY CFNETSEEVF
DHNVVNNKTD CYELMEFHPE VRWMNGKINF DNVGMGYLAL LQVATFKGWM DIMYSAVDSR
AIESQPVYEA NLYMYIYFVI FIIFGSFFTL NLFIGVIIDN FNQQKAKLGG TDIFMTEEQK
KYYNAMKKLG SKKPQKPIPR PTNCCQGLVF DFVTQQFFDI FIMVMICLNM VTMMVETDDQ
SAEIEEILFY INFAFIILFT GECVLKITAL RYHYFSIGWN IFDFVVVILS ILGIGLADLI
EKYFVSPTLF RVIRLARIGR VLRLIRGAKG IRTLLFALMM SLPALFNIGL LLFLIMFIFS
IFGMSNFAYV KKEVGIDDMM NFETFGNSII CMFMITTSAG WDGLLAPILN SPPDCDPDVD
NPGSTTRGNC GNAAVGIVFF CSYIVMSFLV VVNMYIAIIL ENFNVATEES SDPLCEDDFE
MFYETWEKFD PTASQFIDYN RLSEFCDTLK DPLRIPKPNT LKLITMDIPM VTGDKIHCLD
LLLALTGEVL GGSDQMDGMK ATMEEKFMAN NPSKASYEPI TSTLKRKQEE VAASTIQRAY
RSHILKRCVK QASYMYRDKT GSKKPTGEAP EKVGMIAENM RSLYGDQAVE DDHPVGCSFS
QHGKTQFGAK RPPVKVQSDV VLHSAPFPVP ESSTAADNLR ESIV
