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Database: UniProt
Entry: W5L3X0_ASTMX
LinkDB: W5L3X0_ASTMX
Original site: W5L3X0_ASTMX 
ID   W5L3X0_ASTMX            Unreviewed;       989 AA.
AC   W5L3X0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS   Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Characidae; Astyanax.
OX   NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000014532.2, ECO:0000313|Proteomes:UP000018467};
RN   [1] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA   Jeffery W., Warren W., Wilson R.K.;
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000018467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX   PubMed=25329095; DOI=10.1038/ncomms6307;
RA   McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA   Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA   Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA   Yoshizawa M., Warren W.C.;
RT   "The cavefish genome reveals candidate genes for eye loss.";
RL   Nat. Commun. 5:5307-5307(2014).
RN   [3] {ECO:0000313|Ensembl:ENSAMXP00000014532.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   AlphaFoldDB; W5L3X0; -.
DR   STRING; 7994.ENSAMXP00000014532; -.
DR   Ensembl; ENSAMXT00000014532.2; ENSAMXP00000014532.2; ENSAMXG00000014095.2.
DR   eggNOG; KOG0203; Eukaryota.
DR   GeneTree; ENSGT00940000159936; -.
DR   HOGENOM; CLU_002360_4_3_1; -.
DR   InParanoid; W5L3X0; -.
DR   Proteomes; UP000018467; Unassembled WGS sequence.
DR   Bgee; ENSAMXG00000014095; Expressed in muscle tissue 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   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; 3.
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; 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; 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:UP000018467};
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        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        286..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        316..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        819..840
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        919..936
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   TRANSMEM        951..968
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362084"
FT   DOMAIN          37..111
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          208..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   989 AA;  109219 MW;  3864DEDDE40E16F0 CRC64;
     SLSQYGRQYS PEAAQNNGKK KKKNKDLDEL KKEVSLDDHK LALEELSVRY GVDLNQGLTI
     QRAAEILARD GPNALTPPPT TPEWVKFCKQ LFGGFSILLW IGAILCFFAY SLQAATEDEP
     ANDNLYLGVV LAAVVIITGC FSYYQEAKSS RIMDSFKNMV PQQALVIREG EKRQINAEGV
     VVGDLVEIKG GDRTPADLRI ISSSGCKVDN SSLTGESEPQ TRSPDFTHEN PLETRNICFF
     STNCVEGTAR GIVIATGDHT VMGRIATLAS GLEVGQTPIN IEIEHFIHII TGVAVFLGVS
     FFILSIILGY TWLEAVVFLI GIIVANVPEG LLATVTVCLT LTAKRMARKN CLVKNLEAVE
     TLGSTSTICS DKTGTLTQNR MTVAHMWFDN QIHEADTTED QSGYGSFDKN SPTWTALSRV
     AGLCNRAVFK PGQEEIPILK RDTAGDASES ALLKCIELSC GSVRALRDNN PKVCEIPFNS
     TNKYQLSIHE IEDSPTGHLL VMKGAPERIL DSYYKSQFLC AAGFCHLSMS ASHFPRGFAF
     DPEEVNFPTS QMCFLGLMSM IDPPRAAVPT LWCNLFAKVI MVTGDHPITA KAIAKGVGII
     SEGNETVEDI AERLNIPLSQ VNPRDAKACV VHGTDLKEMS SEYLDDLLKN HTEIVFARTS
     PQQKLIIVEG CQRQGAIVAV TGDGVNDSPA LKRADIGVAM GISGSDVSKQ AADMILLDDN
     FASIVTGVEE GRLIFDNLKK SIAYTLTSNI PEISPFLLFI IASVPLPLGT VTILCIDLGT
     DMVPAISLAY ESAESDIMKR QPRNPKTDKL VNERLISMAY GQIGMIQALA GFFTYFVILA
     ENGFLPYTLL GLRLQWDDRS NNDLEDSYGQ QWTYEQRKIV EFTCHTSFFA SIVVVQWADL
     IICKTRRNSL FQQGMRNKIL IFGLFAETAL AAFLSYCPGM DIALRMYPLK VYWWFCALPY
     SILIFIYDEV RKLILRRRPG GWVEQETYY
//
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