ID W5M0Y2_LEPOC Unreviewed; 1013 AA.
AC W5M0Y2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000002039.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000002039.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AHAT01038855; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038856; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038859; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038861; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AHAT01038862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; W5M0Y2; -.
DR STRING; 7918.ENSLOCP00000002039; -.
DR Ensembl; ENSLOCT00000002044.1; ENSLOCP00000002039.1; ENSLOCG00000001762.1.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000159936; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; W5M0Y2; -.
DR OMA; ISWEWAL; -.
DR Proteomes; UP000018468; Linkage group LG5.
DR Bgee; ENSLOCG00000001762; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0005391; F:P-type sodium:potassium-exchanging transporter activity; IBA:GO_Central.
DR GO; GO:0030007; P:intracellular potassium ion homeostasis; IBA:GO_Central.
DR GO; GO:0006883; P:intracellular sodium ion homeostasis; IBA:GO_Central.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IBA:GO_Central.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IBA:GO_Central.
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; 2.
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 NCBIfam; TIGR01106; ATPase-IIC_X-K; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
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:UP000018468};
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 291..315
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 321..344
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 840..861
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 903..922
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 943..960
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 975..991
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..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 210..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1013 AA; 111556 MW; 6989CB7DD0C7FA9C CRC64;
MGKERGRDHT PNQNGRDKKK KQKEKDLDEL KKEVSLDDHR ITLDELGRRY GVDLSRGFTT
AQAVEILARD GPNALTPPPT TPEWVKFCRQ LFGGFSILLW IGAILCFLAY SIQAAMEDEP
ANDNLYLGVV LAAVVIITGC FSYYQEAKSS RIMDSFKNMV PQQALVIRDG EKLQINAEEV
VLGDLVEIKG GDRIPADLRI ISSHGCKVDN SSLTGESEPQ TRSPEYTHDN PLETRNIAFF
STNCVEEISF FLYRGAVCVC GGVGGGRGFL RLLNSGLEVG RTPISMEIEH FIHIITGVAV
FLGVSFFALS LILGYSWLEA VIFLIGIIVA NVPEGLLATV TVCLTLTAKR MARKNCLVKN
LEAVETLGST STICSDKTGT LTQNRMTVAH MWFDNQIYEA DTTEDQSGST FDKSSPTWTA
LAHISGLCNR ATFKPGQENV LILKRDTAGD ASESALLKCI ELSLCNNRKQ LTMKQNRNAL
TRTSSPSLLQ LSIHEFQDNP KGHILVMKGA PERILDRCST ILIQGQEVPL DEDMKDAFQN
AYMELGGLGE RVLGFCHYHL SPDKFPRGFR FDTEDVNFPT EDLCFVGLMS MIDPPRAAVP
DAVGKCRSAG IKVRVTTTAS AAAARTRLAE PCLKNPQTVA DSSSPNLRPA AGPSLLTCWA
EGSPNASIDK TWPIESLSGL RVDFLAGSPN PLSMKTPGSA DLSACRRRGS NDSPALKKAD
IGVAMGIAGS DVSKQAADMI LLDDNFASIV TGVEEGRLIF DNLKKSIAYT LTSNIPEITP
FLLFIIANIP LPLGTVTILC IDLGTDMVPA ISLAYEAAES DIMKRQPRNP RTDKLVNERL
ISMAYGQIAL LTQLTLLLTH LRTVEPDGSL FSCAESPGSY WCSGPANLLV TPLSPQTYEQ
RKIVEFTCHT AFFSSIVVVQ WADLIICKTR RNSVFQQGMK NRILIFGLFE ETALAAFLSY
CPGMDIALRM YPLKITWWFC AFPYSLLIFI YDEIRKLILR RNPGGWVEKE TYY
//
