ID T2B507_MONAL Unreviewed; 1093 AA.
AC T2B507;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS Monopterus albus (Swamp eel).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Synbranchiformes; Synbranchidae; Monopterus.
OX NCBI_TaxID=43700 {ECO:0000313|EMBL:AGV06214.1};
RN [1] {ECO:0000313|EMBL:AGV06214.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24391932;
RA Chen X.L., Wee N.L., Hiong K.C., Ong J.L., Chng Y.R., Ching B., Wong W.P.,
RA Chew S.F., Ip Y.K.;
RT "Properties and expression of Na+/K+-ATPase alpha-subunit isoforms in the
RT brain of the swamp eel, Monopterus albus, which has unusually high brain
RT ammonia tolerance.";
RL PLoS ONE 8:e84298-e84298(2013).
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; KC620450; AGV06214.1; -; mRNA.
DR AlphaFoldDB; T2B507; -.
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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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:SF21; 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 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 83..105
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 117..136
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 278..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 308..331
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 777..800
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 899..918
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 939..956
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 971..987
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1069..1091
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 29..103
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 120252 MW; B8B37EFD34529AFA CRC64;
MGDKDGQSPK KKKGATKNMD DLKKEVPITE HKMSVEEVCR KFQTDIVQGL TNAKAVEILQ
RDGPNALTPP PTTPEWVKFC RQLFGGFSIL LWIGAILCFL AYAIQAATEE DPAGDNLYLG
IVLTAVVVIT GCFSYFQEAK SSKIMESFKN MVPQQALVIR EGEKVQLNAE EVVAGDLIEV
KGGDRIPADI RVVSAHGCKV DNSSLTGESE PQSRSPDCTH DNPLETRNVA FFSTNCVEGT
ARGIVICTGD RTVMGRIATL TSGLEQAKPP IAKEIEHFIH IITGVAVFLG ITFFVLALIL
GYSWLEAVIF LIGIIVANVP EGLLATVTVC LTLTAKRMAK KNCLVKNLEA VETLGSTSTI
CSDKTGTLTQ NRMTVAHMWF DNQIHEADTT EDQSGASFDK SSVTWLSLAR VAALCNRAQF
KAGQDSVAIL KRDVAGDASE SALLKCIELS CGSVRMMREK NKKVAEIPFN STNKYQLSVH
ETEDPNDNRY LLVMKGAPER ILDRCSTILL QGKEQPMDEE MKEAFQNAYM ELGGLGERVL
GFCHLLLPED QYPKGFAFDT DDVNFQTDNL CFVGLMSMID PPRAAVPDAV GKCRSAGIKV
IMVTGDHPIT AKAIAKGVGI ISEGNETVED IAARLNIPVS QVNPRDAKAC VIHGTDLKDL
SQDQMDDILK NHTEIVFART SPQQKLIIVE GCQRQGAIVA VTGDGVNDSP ALKKADIGVA
MGISGSDVSK QAADMILLDD NFASIVTGVE EGRLIFDNLK KSIAYTLTSN IPEITPFLLF
IIINIPLPLG TITILCIDLG TDMVPAISLA YETAESDIMK RQPRNPFRDK LVNERLISIA
YGQIGMIPGT GRLLRLLCNL GCGFLPSRLV GIRLDWDERT MNDLEDSYGQ QWTYEQRKIV
EFTCHTAFFV SIVVVQWADV IICKTRRNSV FQQGMKNKIL IFGLFEETAL AAFLSYCPGM
DVALRMYPLK PSWWFCAFPY SFLIFVYDEV RKLILRRNPG GWVEKETTID PVSIFAQTLT
FSTYFSSISP SLARHISRCP ASSKTKTALK QFSSQLPQRL KTAKAPLPLY TLTHPSFLLI
TILFACVLSL LCT
//
