ID T2B3R7_MONAL Unreviewed; 1025 AA.
AC T2B3R7;
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:AGV06212.1};
RN [1] {ECO:0000313|EMBL:AGV06212.1}
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, sarcolemma
CC {ECO:0000256|ARBA:ARBA00004415}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004415}. Cell membrane
CC {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein
CC {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; KC620448; AGV06212.1; -; mRNA.
DR AlphaFoldDB; T2B3R7; -.
DR BRENDA; 7.2.2.13; 10161.
DR GO; GO:0042383; C:sarcolemma; 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:SF9; SODIUM_POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA-1; 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; 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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362084};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
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}; Sodium {ECO:0000256|ARBA:ARBA00023053};
KW Sodium transport {ECO:0000256|ARBA:ARBA00023201};
KW Sodium/potassium transport {ECO:0000256|ARBA:ARBA00022607};
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 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 292..316
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 322..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 851..874
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 915..934
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 955..972
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 987..1003
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 43..117
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1025 AA; 112589 MW; 1E81F2550A631CFC CRC64;
MGRGEGREQY ELAATSEQGG KKKGKGKKKE KDMDELKKEV DMDDHKLTLD ELNRKYGTDL
TNGLTSTKAA EILARDGPNA LTPPPTTPEW VKFCKQMFGG FSMLLWTGAI LCFLAYGIQA
ALDEEPANDN LYLGVVLSAV VIITGCFSYY QEAKSSKIMD SFKNLVPQQA LVIRDGEKKS
INAEDVVVGD LVEVKGGDRI PADLRIISAH GCKVDNSSLT GESEPQTRTP DFSNENPLET
RNIAFFSTNC VEGTARGIVI STGDRTVMGR IATLASGLEV GRTPISIEIE HFIHIITGVA
VFLGVSFFIL SLILGYSWLE AVIFLIGIIV ANVPEGLLAT LTVCLTLTAK RMAKKNCLVK
NLEAVETLGS TSTICSDKTG TLTQNRMTVA HMWFDNQIHE ADTTENQSGT SFDRSSATWA
ALARIAGLCN RAVFLAEQSN IPILKRDVAG DASESALLKC IELCCGSVQG MREKNPKIAE
IPFNSTNKYQ LSIHKNSAPE GETKHLLVMK GAPERILDRC STIMMQGKEQ PLDDEMKDAF
QNAYLELGGL GERVLGFCHF NLPDDQFSED FAFDTDEVNF PTEKLCFIGL MSMIDPPRAA
VPDAVGKCRS AGIKVIMVTG DHPITAKAIA KGVGIISEGN ETVEDIAARL NIPINEVNPR
DAKACVVHGG DLKDLTSEQL DDILKHHTEI VFARTSPQQK LIIVEGCQRQ GAIVAVTGDG
VNDSPALKKA DIGVAMGIAG SDVSKQAADM ILLDDNFASI VTGVEEGRLI FDNLKKSIAY
TLTSNIPEIT PFLLFIIANI PLPLGTVTIL CIDLGTDMVP AISLAYEAAE SDIMKRQPRN
PKTDKLVNER LISIAYGQIG MIQALAGFFT YFVILAENGF LPSTLLGIRV SWDSKHVNDL
EDSYGQQWTY EQRKIVEFTC HTAFFVSIVI VQWADLIICK TRRNSVFQQG MKNKILIFGL
FEETALAAFL SYCPGMDVAL RMYPLKPNWW FCAFPYSLLI FIYDEIRKLI LRRSPGGWVE
RETYY
//
