ID K0GEY3_ONCFA Unreviewed; 994 AA.
AC K0GEY3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
DE Flags: Fragment;
OS Oncopeltus fasciatus (Large milkweed bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Pentatomomorpha; Lygaeoidea; Lygaeidae; Lygaeinae; Oncopeltus.
OX NCBI_TaxID=7536 {ECO:0000313|EMBL:AFU25687.1};
RN [1] {ECO:0000313|EMBL:AFU25687.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23019645; DOI=10.1126/science.1226630;
RA Zhen Y., Aardema M.L., Medina E.M., Schumer M., Andolfatto P.;
RT "Parallel molecular evolution in an herbivore community.";
RL Science 337:1634-1637(2012).
CC -!- FUNCTION: This is the catalytic component of the active enzyme, which
CC catalyzes the hydrolysis of ATP coupled with the exchange of sodium and
CC potassium ions across the plasma membrane. This action creates the
CC electrochemical gradient of sodium and potassium ions, providing the
CC energy for active transport of various nutrients.
CC {ECO:0000256|ARBA:ARBA00037422}.
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. {ECO:0000256|ARBA:ARBA00038795}.
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}.
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DR EMBL; JQ771518; AFU25687.1; -; mRNA.
DR AlphaFoldDB; K0GEY3; -.
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 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:SF13; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 2: Evidence at transcript level;
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 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 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 262..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 293..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 820..843
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 884..903
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 923..944
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 956..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 13..87
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFU25687.1"
SQ SEQUENCE 994 AA; 110117 MW; F6D62716C12BF0F6 CRC64;
GDLDDLKQEL DIDHHKISVE ELYQRFSTHP DSGLTHAKAK ENLERDGPNA LTPPKTTPEW
VKFCKQLFGG FALLLWVGAI LCFIAYSIQA TTVEEPSDDH LYLGIVLATV VIITGIFSYY
QESKSSRIME SFKNMVPQFA TVVRQGEKLT IRAEDIVLGD VVEVKFGDRI PADIRIIEAR
GFKVDNSSLT GESEPQSRGV ENTHENPLET KNLAFFSTNA VEGTAKGVVI SCGDNTVMGR
IAGLASGLDT GETPIAKEIH HFIHIITGVA IFLGITFFII AFLLGYYWLD AVIFLIGIIV
ANVPEGLLAT VTVCLTLTAK RMAAKNCLVK NLEAVETLGS TSTICSDKTG TLTQNRMTVA
HMWFDNQIIE ADTTEDQSGV QYDRTSPGFK ALARIATLCN RAEFKGGQEG VPILKKEVNG
DASEAALLKC MELALGDVLS IRRRNRKVCE IPFNSTNKYQ VSIHETEDPN DPRHLMVMKG
APERILDRCS TIFIGGKEKL LDEEMKEAFN NAYLELGGLG ERVLGFCDLM LPSDKFPLGF
KFDCDDPNFP LSGLRFVGLM SMIDPPRAAV PDAVAKCRSA GIKVIMVTGD HPITAKAIAK
SVGIISEGNE TVEDIAQRLN IPVSEVNPRE AKAAVVHGTD LRDTSPEQLD EILRYHTEIV
FARTSPQQKL IIVEGCQRMG AIVAVTGDGV NDSPALKKAD IGVAMGISGS DVSKQAADMI
LLDDNFASIV TGVEEGRLIF DNLKKSIAYT LTSNIPEISP FLAFMILDIP LPLGSVTILC
IDLGTDMMPA ISLAYEAPES DIMKRQPRDP YRDKLVNKRL ISMAYGQIGM IQAAAGFFVY
FVIMAENGFL PMKLFGLRKS WDSKAVNDLL DSYGQEWTYQ DRKALEYTCH TAFFVSIVVV
QWADLIICKT RRNSIFHQGM RNWPLNFGLV FETALAALLS YTPGMDKGLR MYPLKFVWWL
PALPFMITIF IYDEVRRFYL RRNPGGWLEQ ETYY
//
