ID A0A452J5Q6_9SAUR Unreviewed; 1941 AA.
AC A0A452J5Q6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Sodium channel protein {ECO:0000256|RuleBase:RU361132};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000035802.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000035802.1}
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR STRING; 38772.ENSGAGP00000035802; -.
DR Ensembl; ENSGAGT00000040531.1; ENSGAGP00000035802.1; ENSGAGG00000025408.1.
DR Proteomes; UP000291020; 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; IPR008051; Na_channel_a1su.
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:SF280; SODIUM CHANNEL PROTEIN TYPE 1 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 PRINTS; PR01664; NACHANNEL1.
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:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 339..366
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 694..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 730..751
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 813..841
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 900..926
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1151..1169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1190..1209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1265..1293
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1391..1415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1474..1492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1504..1522
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1529..1554
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1591..1619
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT TRANSMEM 1695..1718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361132"
FT DOMAIN 78..372
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 500..652
FT /note="Voltage-gated Na+ ion channel cytoplasmic"
FT /evidence="ECO:0000259|Pfam:PF11933"
FT DOMAIN 702..932
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 940..1145
FT /note="Sodium ion transport-associated"
FT /evidence="ECO:0000259|Pfam:PF06512"
FT DOMAIN 1149..1424
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT DOMAIN 1473..1728
FT /note="Ion transport"
FT /evidence="ECO:0000259|Pfam:PF00520"
FT REGION 411..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 363..401
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 451..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1941 AA; 221544 MW; 2135E3BF0CD389B6 CRC64;
MVIKMSRMKR WSSQCLYHQD PTASTTSLES LLQLLNNGLL QQRLSIQNKT IKMMKMAQNQ
IVTWRQESHF HLFMVTYLQE WCPSPWRIWT HITLIKKYTF TGIYTFESLI KIFARGFCLE
DFTFLRDPWN WLDFTVITFA YVTEFVNLGN VSALRTFRVL RALKTISVIP GLKTIVGALI
QSVKKLSDVM ILTVFCLSVF ALIGLQLFMG NLRHKCLQWP PDNFTLETNI TSYFNSTIGE
NGTFVNVTVT PFDWKGYIED ERHFYVLEGQ NDALLCGNGS DAGQCPEGYI CVKAGRNPNY
GYTSFDTFSW AFLSLFRLMT QDYWENLYQL TLRAAGKTYM IFFVLVIFLG SFYLINLILA
VVAMAYEEQN QANMEEAEQK EAEFQQMLEQ LRKQQEVAQA AAVAVATASA GSRDPSAEGG
IGGLSESSSD VSKLSSKSAK ERRNRRKKRK QKEQYGGEEK DEDEFQKSES EGSIRKKTFR
FSIEGNRLTY EKKYSSPHQS LLSIRGSLFS PRRNSKTSLF SFRGRARDIG SENDFADDEH
STFEDNDSRR DSLFVPRRHG ERRNSNISQA SRSSRVLAMF PANGKMHSTV DCNGIVSLVG
GPSVPTSPVG QLLPEGMTTE TETRKRRSSS FHVSMDFLED PAQRDRAMSI ASILTNTMEE
LEESRQKCPP CWYKFANIFL IWDCSPHWLK VKHIVSLVVM DPFVDLAITI CIVLNTLFMA
MEHYPMTDEF NNVLSVGNLV FTGIFAAEMF LKIIAKDPYY YFQEGWNIFD SFIVTLSLVE
LGLANVEGLS VLRSFRLLRV FKLAKSWPTL NMLIKIIGNS VGALGNLTLV LAIIVFIFAV
VGMQLFGKNY KECVCKIASD CVLPRWHMQD FFHSFLIVFR VLCGEWIETM WDCMEVAGQA
MCLTVFMMVM VIGNLVVLNL FLALLLSSFS ADNLAATDDD NEMNNLQIAV ARIEKGIDYV
KRKVREFIQK SLVKKQKALN EIKPLEELNK KDSCISNHLT VEINKDLDYL KDGNGTSGIG
TGSSVEKYII DESDYMSFIN NPSLTVTVPI AVGESDFENL NTEEFSSESD LEESKEKLNL
SSSSEGSTVD IGHPEEEQHE AEPEEAAEPE ACFTESCVRR FKCCQVSLEE GRGKQWWNLR
KTCFKIVEHN WFETFIVFMI LLSSGALAFE DIYIEQRKTI KTMLEYADKV FTYIFILEML
LKWVAYGYQT YFTNAWCWLD FLIVDVSLVS LTANALGYSE LGAIKSLRTL RALRPLRALS
RFEGMRVVVN ALLGAIPSIM NVLLVCLIFW LIFSIMGVNL FAGKFYYCVN TTNDERFDVD
RINNFSQCEE LIKNNETARW KNVKVNFDNV GFGYLSLLQV ATFKGWMDIM YAAIDSRAVL
DQPKYEENLY MYLYFVIFII FGSFFTLNLF IGVIIDNFNQ QKKKFGGQDI FMTEEQKKYY
NAMKKLGSKK PQKPIPRPGN KFQGMVFDFV TKQVFDIGIM ILICLNMVTM MVETDDQSDE
MQTVLQRINL VFVVLFTGEC VLKLISLRYY YFTIGWNIFD FVVVILSIVG MFLAKVIEKY
FVSPTLFRVI RLARIGRILR LIKGAKGIRT LLFALMMSLP ALFNIGLLLF LVMFIYAIFG
MSNFAYVKRE AGIDDMFNFE TFGNSMICLF QITTSAGWDG LLAPILNSGE PDCDPNKPHP
GSSVKGDCGN PSVGIFFFVS YIIISFLVVV NMYIAVILEN FSVATEESAE PLSEDDFEMF
YEVWEKYDPD ATQFMEFAKL SDFAAALDPP LHLPKPNKVQ LIAMDLPMVS GDRIHCLDIL
FAFTKRVLGE SGEMDALRIQ MEDRFMASNP SKASYEPITT TLKRKQEEAS AVIIQRAFRR
YLLKRTVKQA SFAYNKNKIQ GGIGQCIKDE ILIDKLNENS FTEKTDMITS TPVCPPSYDC
VTKLVKEKHV KEDKDVRKKE K
//
