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Database: UniProt
Entry: G3H7Y5_CRIGR
LinkDB: G3H7Y5_CRIGR
Original site: G3H7Y5_CRIGR 
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
//
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