ID A0A0V0V0V9_9BILA Unreviewed; 1058 AA.
AC A0A0V0V0V9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
DE Flags: Fragment;
GN ORFNames=T09_12028 {ECO:0000313|EMBL:KRX56877.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX56877.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX56877.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX56877.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX56877.1}.
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DR EMBL; JYDN01000113; KRX56877.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0V0V9; -.
DR Proteomes; UP000054681; Unassembled WGS sequence.
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; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000054681};
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 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 339..363
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 369..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 884..907
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 948..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 987..1008
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1020..1036
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 89..163
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 47..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX56877.1"
SQ SEQUENCE 1058 AA; 116556 MW; BB6B86DE4AD9B565 CRC64;
LLEMDYGRTE SYRVATQVIL PVAQQDVNVG KEPNLVNLDR MAKDGDAKPV EAVNAHQSSA
QQQPKMEKSR GRGRKPHTLE NLKKEVEMDE HHIPLSELYR RLGTDPELGL TDEQAREILI
RDGPNALTPP KKVPEWVKFA RNLFGGFAML LWIGAILCFI AYGVELATSD AVITDNVYLG
TVLAVVVIVT GCFQYYQEAK SSKIMESFKD MVPHYALVVR GGQKKNVRTE ELVIGDIVEM
RGGDRVPADI RIIAAQSFKV DNSSLTGESE PQSRSAECTN VENPLETKNL AFFSTNAVEG
TARGIVVNIG DHTLMGRIAH LASGLETGQT PIAQEITRFI HLITGVAVFL GVTFFIIAFI
LGYQWLDAVI FLIGIIVANV PEGLLATVTV CLTLTAKRMA SKNCLVKNLE AVETLGSTST
ICSDKTGTLT QNRMTVAHMW YDDNIVEADT SEHQSNKATF ASSSTFDALT HIAALCNKAE
FKPGQEDVPI VKRECTGDAS ESALLKCMEI TVGDVAGWRK RFKKVSIHEY SGDPEHAYLL
VMKGAPERIF ERCSTIACRG QDYEIDAEWT NKFQQSYLQL GGLGERVLGF CDMLLPVSKF
PHGFEFSGDD QNFPLDGLRF VGLISMIDPP RAAVPDAVSK CRSAGIKVIM VTGDHPITAQ
AIARSVGIIS EGSETVEDIA LRLGIAKKDV DPSQARAIVV HGSDLKDMNS DQLDIILANH
PEIVFARTSP QQKLIIVEGC QRQGAIVAVT GDGVNDSPAL KKADIGVAMG ISGSDVSKQA
ADMILLDDNF ASIVTGVEEG RLIFDNLKKS IAYTLTSNIP EISPFLLFIL ADIPLPLGTV
TILCIDLGTD LWPAISLAYE EAESDIMKRK PRDPKRDKLV NERLISLAYG MIGMIQAAAG
FFAYFVIMGE NGFLPNRLLG LREQWDSKAV NDLEDSYGQQ WTHANRKVLE YTCHTAFFVS
IVIVQWADLI ISKTRRNSLV QQGMSNWTLN AGLIFETALA AFLCYCPGLD KGLRMYGLRF
AWWFPALPFS ILIFVYDEAR KAIIRRNPDG WVSKETYY
//
