ID G3H7Y5_CRIGR Unreviewed; 1194 AA.
AC G3H7Y5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha-2 {ECO:0000256|ARBA:ARBA00039738};
DE EC=7.2.2.13 {ECO:0000256|ARBA:ARBA00039096};
DE AltName: Full=Sodium pump subunit alpha-2 {ECO:0000256|ARBA:ARBA00041492};
GN ORFNames=I79_006481 {ECO:0000313|EMBL:EGV93401.1};
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029 {ECO:0000313|EMBL:EGV93401.1, ECO:0000313|Proteomes:UP000001075};
RN [1] {ECO:0000313|Proteomes:UP000001075}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX PubMed=21804562; DOI=10.1038/nbt.1932;
RA Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA Famili I., Palsson B.O., Wang J.;
RT "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL Nat. Biotechnol. 29:735-741(2011).
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 -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. Interacts with regulatory subunit FXYD1.
CC {ECO:0000256|ARBA:ARBA00038783}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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}.
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DR EMBL; JH000204; EGV93401.1; -; Genomic_DNA.
DR AlphaFoldDB; G3H7Y5; -.
DR STRING; 10029.G3H7Y5; -.
DR PaxDb; 10029-XP_007637430-1; -.
DR eggNOG; KOG0203; Eukaryota.
DR InParanoid; G3H7Y5; -.
DR Proteomes; UP000001075; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 3.
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; 2.
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; 2.
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};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001075};
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, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023201}.
FT TRANSMEM 115..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1003..1020
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1035..1051
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1090..1108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1123..1142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1163..1181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 61..135
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 20..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1194 AA; 131546 MW; 2DAFA3B9546B1A93 CRC64;
MNYLITPRAA APVSIEYNAE DTCPAGGREY SPAATTSENG GGKKKQKEKE LDELKKEVAM
DDHKLSLDEL GRKYQVDLSK GLTNQRAQDI LARDGPNALT PPPTTPEWVK FCRQLFGGFS
ILLWIGALLC FLAYGILAAM EDEPSNDNLY LGIVLAAVVI VTGCFSYYQE AKSSKIMDSF
KNMVPQQALV IREGEKMQIN AEEVVVGDLV EVKGGDRVPA DLRIISSHGC KVDNSSLTGE
SEPQTRSPEF THENPLETRN ICFFSTNCVE GTARGIVIAT GDRTVMGRIA TLASGLEVGQ
TPIAMEIEHF IQLITGVAVF LGVSFFVLSL ILGYSWLEAV IFLIGIIVAN VPEGLLATVT
VCLTLTAKRM ARKNCLVKNL EAVETLGSTS TICSDKTGTL TQNRMTVAHM WFDNQIHEAD
TTEDQSGATF DKRSPTWTAL SRIAGLCNRA VFKAGQENIS VSKLPLVTST DALSLPSCTP
SPPATVTLNS IFFWQRDTAG DASESALLKC IELSCGSVRK MRDRNPKVAE IPFNSTNKYQ
LSIHEREDSP QSHVLVMKGA PERILDRCST ILVQGKEIPL DKEMQDAFQN AYMELGGLGE
RVLGFCQLNL PSGKFPRGFK FDTDELNFPT EKLCFVGLMS MIDPPRAAVP DAVGKCRSAG
IKVIMVTGDH PITAKAIAKG VGIISEGNET VEDIAARLNI PVSQVNPREA KACVVHGSDL
KDMTSEQLDE ILRDHTEIVF ARTSPQQKLI IVEGCQRQGA IVAVTGDGVN DSPALKKADI
GIAMGISGSD VSKQAADMIL LDDNFASIVT GVEEGRLIFD NLKKSIAYTL TSNIPEITPF
LLFIIANIPL PLGTVTILCI DLGTDMVPAI SLAYEAAESD IMKRQPRNSQ TDKLVNERLI
SMAYGQIGMI QALGGFFTYF VILAENGFLP SRLLGIRLDW DDRTTNDLED SYGQEWTYEQ
RKVVEFTCHT AFFASIVVVQ WADLIICKTR RNSVFQQGMK NKILIFGLLE ETALAAFLSY
CPGMGVALRM YPLKVTWWFC AFPYSLLIFI YDEVRKLILR RYPGGRLIFD NLKKSIAYTL
TSNIPEITPF LLFIILSIPL PLGTITILCI DLGTDMTYEQ RKVVEYTCHT SFFISIVIVQ
WADLIICKTR RNSLFKQGMK NKILLFGLFE ETILAAILSY TPGMDVALRM YPLK
//