ID A0A1L8FGU0_XENLA Unreviewed; 1025 AA.
AC A0A1L8FGU0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN Name=atp1a3.S {ECO:0000313|Xenbase:XB-GENE-17342181};
GN Synonyms=LOC108697760 {ECO:0000313|RefSeq:XP_018083596.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|Proteomes:UP000186698, ECO:0000313|RefSeq:XP_018083596.1};
RN [1] {ECO:0000313|RefSeq:XP_018083596.1}
RP IDENTIFICATION.
RC STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018083596.1};
RC TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018083596.1};
RG RefSeq;
RL Submitted (NOV-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}.
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DR RefSeq; XP_018083596.1; XM_018228107.2.
DR AlphaFoldDB; A0A1L8FGU0; -.
DR STRING; 8355.A0A1L8FGU0; -.
DR PaxDb; 8355-A0A1L8FGU0; -.
DR GeneID; 108697760; -.
DR KEGG; xla:108697760; -.
DR CTD; 108697760; -.
DR Xenbase; XB-GENE-17342181; atp1a3.S.
DR OMA; IQREVWF; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000186698; Chromosome 7S.
DR Bgee; 108697760; Expressed in brain and 9 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; 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:SF15; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-3; 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:UP000186698};
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 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 132..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 293..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 323..346
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 851..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 915..934
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 955..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 987..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 44..118
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1025 AA; 112974 MW; 0C2EC74535ADF700 CRC64;
MGYGRSDSYR VATTQDNKDD ESPKKGKGVP KKEMDDLKKE VDMTEHKMSV EEVCRKYNTD
CVQGLTLSKA AEILARDGPN ALTPPPTTPE WIKFCRQLFG GFSILLWIGA ILCFLAYGIQ
KGMEDDPAGD NLYLGIVLAA VVIITGCFSY YQEAKSSKIM ESFKNMVPQQ ALLIREGEKM
QLNAEEVVVG DLVEIKGGDR VPADLRIISS HGCKVDNSSL TGESEPQTRS PDCTHENPLE
TRNIAFFSTN CVEGTARGVV VATGDRTVMG RIATLASGLE VGKTPIAKEI EHFIHLITGV
AVFLGISFFI LSLVLGYSWL EAVIFLIGII VANVPEGLLA TVTVCLTLTA KRMARKNCLV
KNLEAVETLG STSTICSDKT GTLTQNRMTV AHMWFDNQIH EADTTEDQSG ASFDKSSPTW
LALAQIAALC NRAVFKAGND NIPVLKRDVA GDASESALLK CIELSCGSVK AIREKNKKVA
EIPFNSTNKY QLSIHETEDP NDNRYMLVMK GAPERILDVC STILIQGKEQ PLDDELKEAF
QNAYLELGGL GERVLGFCHF YFPEELYPKG FAFDTEDQNF STENMCFVGL MSMIDPPRAA
VPDAVGKCRS AGIKVIMVTG DHPITAKAIA KGVGIISEGN ETVEDIAARL NIPVSQVNPR
DAKACVIHGT NLKDMPTEQI DEILQNHTEI VFARTSPQQK LIIVEGCQRQ GAIVAVTGDG
VNDSPALKKA DIGVAMGIAG SDVSKQAADM ILLDDNFASI VTGVEEGRLI FDNLKKSIAY
TLTSNIPEIT PFLLFIMANI PLPLGTITIL CIDLGTDMVP AISLAYEAAE SDIMKRQPRN
PRTDKLVNER LISMAYGQIG MIQALGGFFA YFVILAENGF LPSHLVGIRL TWDDRTTNDL
EDSYGQQWTY EQRKIVEFTC HTAFFVSIVV VQWADVIICK TRRNSVFQQG MKNKILIFGL
FEETALAAFL SYCPGMDIAL RMYPLKPSWW FCAFPYSFLI FIYDEIRKLI LRRHPGGWVE
KESYY
//
