ID A0A6I8TEC3_AEDAE Unreviewed; 1040 AA.
AC A0A6I8TEC3;
DT 12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT 12-AUG-2020, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN Name=5575790 {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL012062-PZ};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000256|ARBA:ARBA00037422}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. {ECO:0000256|ARBA:ARBA00038795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000256|ARBA:ARBA00006934,
CC ECO:0000256|RuleBase:RU362084}.
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DR AlphaFoldDB; A0A6I8TEC3; -.
DR EnsemblMetazoa; AAEL012062-RZ; AAEL012062-PZ; AAEL012062.
DR InParanoid; A0A6I8TEC3; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000008820; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR CDD; cd02608; P-type_ATPase_Na-K_like; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005775; P-type_ATPase_IIC.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR43294:SF13; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065,
KW ECO:0000256|RuleBase:RU362084};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362084};
KW Metal-binding {ECO:0000256|RuleBase:RU362084};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362084};
KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|RuleBase:RU362084};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538,
KW ECO:0000256|RuleBase:RU362084};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362084};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362084}; Transport {ECO:0000256|RuleBase:RU362084}.
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 147..166
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 308..332
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 338..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 870..889
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 931..949
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 969..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1002..1018
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 59..133
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1040 AA; 115296 MW; A42599AE4F3A33D7 CRC64;
MARSIDEETG RTDSYRVATV APLKDDNRTA DGQFKSRRKM PPKKKGDNLD DLKQELDIDY
HKITPEELYQ RLQTHPENGL SHAKAKENLE RDGPNALTPP KQTPEWVKFC KNLFGGFALL
LWIGAILCFI AYSILASTVE EPADDNLYLG IVLTAVVIVT GIFSYYQESK SSKIMESFKN
MVPQFATVLR EGEKLTLRAE DLVIGDVVEV KFGDRLPADI RIIEARNFKV DNSSLTGESE
PQSRGPDFTH ENPLETKNLA FFSTNAVEGT AKGVVISCGD HTVMGRIAGL ASGLDTGETP
IAKEIHHFIH LITGVAVFLG VTFFVIAFIL GYHWLDAVIF LIGIIVANVP EGLLATVTVC
LTLTAKRMAS KNCLVKNLEA VETLGSTSTI CSDKTGTLTQ NRMTVAHMWF DNQIIEADTT
EDQSGVQYDR TSPGFKALSR IATLCNRAEF KGGQEGVPIL KKEVSGDASE AALLKCMELA
LGDVLSIRKR NKKVCEIPFN STNKYQVSIH ETEDPSDPRY LLVMKGAPER ILERCSTIFI
NGKEKLMDEE MKEAFNNAYL ELGGLGERVL GFCDFMLPSD KFPAGFKFNS DEVNFPCESL
RFVGLMSMID PPRAAVPDAV AKCRSAGIKV IMVTGDHPIT AKAIAKSVGI ISEGNETVED
IAQRLNIPVS EVNPREAKAA VVHGSELRDL STDQIDEILR YHTEIVFART SPQQKLIIVE
GCQRMGAIVA VTGDGVNDSP ALKKADIGVA MGIAGSDVSK QAADMILLDD NFASIVTGVE
EGRLIFDNLK KSIAYTLTSN IPEISPFLAF ILCDIPLPLG TVTILCIDLG TDMVPAISLA
YEHAESDIMK RPPRDPFNDK LVNERLISMA YGQIGMIQAA AGFFVYFVIM AENGFLPLHL
FGLRKGWDSK AVNDLTDSYG QEWTYRDRKT LEFTCHTAFF VSIVVVQWAD LIICKTRRNS
IFHQGMRNWA LNFGLVFETI LAAILSYTPG MDKGLRMFPL KFVWWLPALP FSLSIFVYDE
IRRFYLRRNP GGWLEQETYY
//
