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Database: UniProt
Entry: A0A673BAR1_9TELE
LinkDB: A0A673BAR1_9TELE
Original site: A0A673BAR1_9TELE 
ID   A0A673BAR1_9TELE        Unreviewed;       988 AA.
AC   A0A673BAR1;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS   Sphaeramia orbicularis (orbiculate cardinalfish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Kurtiformes; Apogonoidei; Apogonidae; Apogoninae; Sphaeramia.
OX   NCBI_TaxID=375764 {ECO:0000313|Ensembl:ENSSORP00005038369.1, ECO:0000313|Proteomes:UP000472271};
RN   [1] {ECO:0000313|Ensembl:ENSSORP00005038369.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) +
CC         Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC         EC=7.2.2.13; Evidence={ECO:0000256|ARBA:ARBA00035887};
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU362084}.
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DR   Ensembl; ENSSORT00005039361.1; ENSSORP00005038369.1; ENSSORG00005012910.1.
DR   Ensembl; ENSSORT00005047840.1; ENSSORP00005046678.1; ENSSORG00005017944.1.
DR   Proteomes; UP000472271; Unplaced.
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   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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:SF6; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-2; 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; 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:UP000472271};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201};
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        52..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        247..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        277..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        808..829
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        908..925
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        940..956
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          10..72
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          170..189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..188
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   988 AA;  109086 MW;  664F187105797F11 CRC64;
     SAAEKMGRCV VIRFPAQGLT NARAAEVLAR DGPNALTPPP TTPEWVKFCR QLFGGFSILL
     WIGAILCFLA YSIQVATEDE PVNDNLYLGV VLAAVVIITG CFSYFQEAKS SRIMDSFKKM
     VPQQAMVIRE GEKMQINAEL VVQGDLVEIK GGDRIPADLR VISSSGCKVD NSSLTGESEP
     QTRSPEFTHE NPLETRNICF FSTNCVEGTA RGIVIATGDR TVMGRIATLA SELEVRRTPI
     NIEIEHFIHI ITGVAVFLGV SFFILSLILG YTWLEAVIFL IGIIVANVPE GLLATVTVCL
     TLTAKRMAKK NCLVKNLEAV ETLGSTSTIC SDKTGTLTQN RMTVAHMWFD NQIHEADTTE
     DQTGSGFDKS SPTWAALSRV AGLCNRADFK ADQEHIPILM RETAGDASES ALLKCIEVCC
     GSVRDLRGRN PKVAEIPFNS TNKYQLSIHE VEDNPSGHIL VMKGAPERIL DRCSTIMIQG
     QEQALDESWR ESFQNAYMEL GGLGERVLGF CHLNLSSSQF PRGYTFDTDD MNFPTEQLCF
     LGLIAMIDPP RAAVPDAVGK CRSAGIKVIM VTGDHPITAK AIAKGVGIIS EGNETVEDIA
     ERLNIPLSQV NPRDAKACVV HGSDLKDMST EYLDDLLRNH TEIVFARTSP QQKLIIVEGC
     QRQGAIVAVT GDGVNDSPAL KKADIGVAMG ITGSDVSKQA ADMILLDDNF ASIVTGVEEG
     RLIFDNLKKS IAYTLTSNIP EISPFLLFII ASVPLPLGTV TILCIDLGTD MVPAISLAYE
     TAESDIMKRQ PRNPKTDKLV NERLISMAYG QIGMIQALAG FFTYFVILAE NGFLPRTLLG
     VRILWDDREV NDLEDSYGQQ WTYEERKIIE FTCHTAFFTS IVVVQWADLI ICKTRRNSLF
     QQGMKNRILI FGLFVETALA AFLSYCPGMD VALRMYPLKT WWWFCAFPYS LLIFIYDEVR
     KFILRRTPGG KHLLRQTKIK RFKPSLSC
//
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