ID A0A3P8XPV5_ESOLU Unreviewed; 1029 AA.
AC A0A3P8XPV5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN Name=ATP1A1 {ECO:0000313|Ensembl:ENSELUP00000006540.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000006540.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000006540.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000006540.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|RuleBase:RU362084}.
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DR RefSeq; XP_010878503.1; XM_010880201.3.
DR RefSeq; XP_019910600.1; XM_020055041.1.
DR RefSeq; XP_019910601.1; XM_020055042.1.
DR RefSeq; XP_019910602.1; XM_020055043.1.
DR RefSeq; XP_019910603.1; XM_020055044.1.
DR AlphaFoldDB; A0A3P8XPV5; -.
DR STRING; 8010.ENSELUP00000006540; -.
DR Ensembl; ENSELUT00000008763.2; ENSELUP00000006540.2; ENSELUG00000007421.2.
DR GeneID; 105016395; -.
DR KEGG; els:105016395; -.
DR GeneTree; ENSGT00940000154840; -.
DR InParanoid; A0A3P8XPV5; -.
DR OMA; RNYVLIF; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000265140; LG16.
DR Bgee; ENSELUG00000007421; Expressed in pharyngeal gill and 6 other cell types or tissues.
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:SF8; 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000265140};
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 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 296..320
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 326..349
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 795..818
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 918..939
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 959..976
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 47..121
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1029 AA; 113945 MW; B39182E39E8BD976 CRC64;
MGFGKGKEDY KLAATSDDNG KKKSKKQAKK AKDKMDLEQL KKEVELDDHK LTMEEIHRKY
GTELTRGLSS TRAREIRLRD GPNALTPPPT TPEWVKFCRQ LFGGFCMLLW IGAFLCFIAY
IIQVSSEQEP AGDNLWLGIV LAVVVIITGV FSYYQEAKAS NIMDSFKNLV PQQALVIRDG
EKMNINTEDV VVGDLVEVKG GDRVPADLRI ISANHCKVDN SSLTGESEPQ HRSPDFTHEN
PLETRNIAFF STNCVEGTAR GVVINTGDRT IMGRIATLAM SLEGGKTPIA IEIEHFIHII
TGVAIFLGVT FLILSVILGY GWLESVIFLI GIIVANVPEG LLATVTVCLT LTAKRMAKKN
CLVKNLEAVE TLGSTSTICS DKTGTLTQNR MTVSHMWFDN HIHDADTTEN QTGTSFDKSS
ATWAALAKIA GLCNRAVFLA EQNNIPILKR VVAGDASESA LLKCIELCCG SVKDMREKYS
NIAEIPFNST NKYQLSIHKN NMPGESRHLL VMKGAPERIL DRCSTILIQG KEHPLDEVMM
ESFQNAYEEL GGLGERVLGF CHFQLPDDHF PEGFEFDCEE VNFPTEGLCF VGLISLIDPP
RAAVPDAVNK CRCAGIKVIM VTGDHPITAK AIAKGVGIIS EGNETVEDIA SRLKIPVSEV
NPREAKACVV HGGLLKDMTA EQLDDILKYH TEIVFARTSP QQKLIIVEGC QRQGAIVAVT
GDGVNDSPAL KKADIGVAMG IAGSDVSKQA ADMILLDDNF ASIVTGVEEG RLIFDNLKKS
IAYTLTSKIP EMSPFLLLIL ANIPLALGTV TILCIDLGTD MIPAISLAYE EAENDIMKRQ
PRNAKTDKLV NERLISMAYG QIGMMQATAG FFTYLVIMAE NGFYPLDLLG IRMYWENKYL
NDMEDSYGQQ WTYERRKIVE YTCHTAFFVS IVIVQWADLI ICKTRKNSLA QQGMMSNRVL
VFGLFAETAL AAFLSYCPGM DIALRMYPLK PCWWLCALPY SLLIFVYDEV RKYILRKYPG
GWVDQETYY
//
