ID A0A452SQZ2_URSAM Unreviewed; 1827 AA.
AC A0A452SQZ2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
GN Name=SCN3A {ECO:0000313|Ensembl:ENSUAMP00000035243.1};
OS Ursus americanus (American black bear) (Euarctos americanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=9643 {ECO:0000313|Ensembl:ENSUAMP00000035243.1, ECO:0000313|Proteomes:UP000291022};
RN [1] {ECO:0000313|Proteomes:UP000291022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Korstanje R., Srivastava A., Sarsani V.K., Sheehan S.M., Seger R.L.,
RA Barter M.E., Lindqvist C., Brody L.C., Mullikin J.C.;
RT "De novo assembly and RNA-Seq shows season-dependent expression and editing
RT in black bear kidneys.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSUAMP00000035243.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Mediates the voltage-dependent sodium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a sodium-selective channel through which Na(+) ions may pass in
CC accordance with their electrochemical gradient.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651,
CC ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
CC {ECO:0000256|RuleBase:RU361132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU361132}.
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DR Ensembl; ENSUAMT00000039231.1; ENSUAMP00000035243.1; ENSUAMG00000026151.1.
DR GeneTree; ENSGT00940000157130; -.
DR Proteomes; UP000291022; Unassembled WGS sequence.
DR GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005248; F:voltage-gated sodium channel activity; IEA:InterPro.
DR CDD; cd13433; Na_channel_gate; 1.
DR Gene3D; 1.10.287.70; -; 4.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR Gene3D; 1.20.5.1190; iswi atpase; 1.
DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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_dom.
DR InterPro; IPR024583; Na_trans_cytopl.
DR InterPro; IPR043203; VGCC_Ca_Na.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR10037:SF237; SODIUM CHANNEL PROTEIN TYPE 3 SUBUNIT ALPHA; 1.
DR PANTHER; PTHR10037; VOLTAGE-GATED CATION CHANNEL CALCIUM AND SODIUM; 1.
DR Pfam; PF00520; Ion_trans; 4.
DR Pfam; PF06512; Na_trans_assoc; 1.
DR Pfam; PF11933; Na_trans_cytopl; 1.
DR PRINTS; PR00170; NACHANNEL.
DR SMART; SM00015; IQ; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 4.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion channel {ECO:0000256|RuleBase:RU361132};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU361132};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361132};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000291022};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|RuleBase:RU361132};
KW Sodium channel {ECO:0000256|ARBA:ARBA00022461,
KW ECO:0000256|RuleBase:RU361132};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361132};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361132};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU361132};
KW Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882,
KW ECO:0000256|RuleBase:RU361132}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1827
FT /note="Sodium channel protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019193716"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 269..296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 630..648
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 660..682
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 694..719
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 739..768
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 830..853
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1067..1086
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1106..1131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1151..1177
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1272..1296
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1354..1372
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1384..1402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1409..1434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1471..1499
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1575..1598
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 1..302
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 427..579
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 629..860
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 867..1061
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1110..1305
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1353..1608
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 362..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1000..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1776..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..334
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 380..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1778..1799
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1800..1827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1827 AA; 206775 MW; C5F5C1AC11E25EDA CRC64;
MLIMCTILTN CVFMTLSNPP DWTKNVEYTF TGIYTFESLI KILARGFCLE DFTFLRDPWN
WLDFSVIVMA YVTEFVDLGN VSALRTFRVL RALKTISVIP GLKTIVGALI QSVKKLSDVM
ILTVFCLSVF ALIGLQLFMG NLRNKCLQWP PSDSAFDTNT TSYFNGTMDS NGIFVNVTMS
TFNWKDYIED DSHFYVLDGQ KDPLLCGNGS DAGQCPEGYI CVKAGRNPNY GYTSFDTFSW
AFLSLFRLMT QDYWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLVNLILA VVAMAYEEQN
QATLEEAEQK EAEFQQMLEQ LKKQQEEAQA VAAASAASRD FSGIGGLGEL LESSSEASKL
SSKSAKEWRN RRKKRRQREH LEGNNKGEGD RFPKSESEDS VKRRSFLFSM DGNRLTSDKK
FYSPHQSLLS IRGSLFSPRR NSKTSIFSFR GRAKDVGSEN DFADDEHSTF EDSESRRDSL
FVPHRHGERR NSNVSQASMS SRMVPGLPAN GKMHSTVDCN GVVSLVGGPS ALTSPTGQLP
PEGTTTETEV RKRRLSSYQI SMEMMEDSSG RQRAMSIASI LTNTMEELEE SRQKCPPCWY
RFANVFLIWD CCDAWLKVKH LVNLIVMDPF VDLAITICIV LNTLFMAMEH YPMTGQFSSV
LTVGNLVFTG IFTAEMVLKI IAMDPYYYFQ EGWNIFDGII VSLSLMELGL ANVEGLSVLR
SFRLLRVFKL AKSWPTLNML IKIIGNSVGA LGNLTLVLAI IVFIFAVVGM QLFGKSYKEC
VCKISSDCQL PRWHMNDFFH SFLIVFRVLC GEWIETMWDC MEVAGQTMCL IVFMLVMVIG
NLVVLNLFLA LLLSSFSSDN LAATDDDNEM NNLQIAVGRM QKGIDYVKNK IRECFRKTFF
RKPKVIEIHE GNKIDSCISN NTGIEISKEL NYLKDGNGTT SGVGTGSSVE KYVIDENDYM
SFINNPSLTV TVPIAVGESD FENLNTEEFS KKSQFAMGSS EGSTVDVAPP REGEQAEIEP
EEDLKPEACF TEGCIKKFPF CQVSIEEGKG KVWWNLRKTC YSIVEHNWFE TFIVFMILLS
SGALAFEDIY IEQRKTIKTM LEYLAVYFQV SLVSLVANAL GYSELGAIKS LRTLRALRPL
RALSRFEGMR VVVNALVGAI PSIMNVLLVC LIFWLIFSIM GVNLFAGKFY HCVNTTTGNM
FEVSEVNNLS DCQALGKQAR WKNVKVNFDN VGAGYLALLQ VATFKGWMDI MYAAVDSRDV
KLQPVYEENL YMYLYFVIFI IFGSFFTLNL FIGVIIDNFN QQKKKISQDI FMTEEQKKYY
NAMKKLGSKK PQKPIPRPAN KFQGMVFDFV TRQVFDISIM ILICLNMVTM MVETDDQSKY
MTLVLSRINL VFIILFTGEF VLKLISLRYY YFTIGWNIFD FVVVILSIVG MFLAELIEKY
FVSPTLFRVI RLARIGRILR LIKGAKGIRT LLFALMMSLP ALFNIGLLLF LVMFIYAIFG
MSNFAYVKKE AGIDDMFNFE TFGNSMICLF QITTSAGWDG LLAPILNSAP PDCDPDTIHP
GSSVKGDCGN PSVGIFFFVS YIIISFLVVV NMYIAVILEN FSVATEESAE PLSEDDFEMF
YEVWEKFDPD ATQFIEFSKL SDFAAALDPP LLIAKPNKVQ LIAMDLPMVS GDRIHCLDIL
FAFTKRVLGE SGEMDALRIQ MEDRFMASNP SKVSYEPITT TLKRKQEEVS AAIIQRNFRC
YLLRQRLKRV SSEYNKEAIK GRIDLPIKED MIIDKLNGNS TPEKTDGSSS TTSPPSYDSV
TKPDKEKFEK DKPEKESKGK EVRENQK
//
