ID X2CMC9_9GOBI Unreviewed; 1024 AA.
AC X2CMC9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
OS Periophthalmodon schlosseri (giant mudskipper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmodon.
OX NCBI_TaxID=1365757 {ECO:0000313|EMBL:AGR87393.1};
RN [1] {ECO:0000313|EMBL:AGR87393.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AGR87393.1};
RA Hiong K.C., Ip Y.K., Chew S.F.;
RT "Molecular characterization and mRNA expression of two Na+/K+-ATPase alpha-
RT subunit isoforms in the gills of the giant mudskipper, Periophthalmodon
RT schlosseri, on exposure to salinity and/or ammonia stress.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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; KF410828; AGR87393.1; -; mRNA.
DR AlphaFoldDB; X2CMC9; -.
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:SF8; 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 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 97..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 850..873
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 914..933
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 954..971
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 986..1002
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..35
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 11..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 112462 MW; CFCD26A6A3B358EF CRC64;
MGLGRGKDEY QLAATSEKEK GKKAKKAKEK KDMDDLKKEV DLDDHKLTLD ELHRKYGTDL
TRGLSSSRAK EILARDGPNA LTPPPTTPEW VKFCKQLFGG FSMLLWIGAI LCFLAYGIQA
ASEDEPANDN LYLGVVLSAV VIITGCFSYY QEAKSSKIMD SFKNLVPQQA LVVRDGEKKN
INAEEVVVGD LVEVKGGDRI PADLRIISAH GCKVDNSSLT GESEPQTRTP DFSNENPLET
RNIAFFSTNC VEGTARGVVI NTGDRTVMGR IATLASSLEG GKTPIAIEIE HFIHIITGVA
VFLGVSFFIL SLILGYGWLE AVIFLIGIIV ANVPEGLLAT VTVCLTLTAK RMAKKNCLVK
NLEAVETLGS TSTICSDKTG TLTQNRMTVA HMWFDNQIYE ADTTENQSGT SFDRSSATWG
ALSRVAGLCN RAVFLADQSN VPILKRDVAG DASEAALLKC IELCCGSVAG MREKYPKVAE
IPFNSTNKYQ LSIHKNSTVG ETKHLLVMKG APERILDRCS SILLHGKEQP LDDEMKDAFQ
NAYVELGGLG ERVLGFCHFS LPDDQFPDGF AFDTEEVNFP TENLCFVGLM AMIDPPRAAV
PDAVGKCRSA GIKVIMVTGD HPITAKAIAK GVGIISEGNE TVEDIAARLN VPVSEVNPRD
AKACVVHGGE LKDMTTEQLA DILKHHTEIV FARTSPQQKL IIVEGCQRQG AIVAVTGDGV
NDSPALKKAD IGVAMGIAGS DVSKQAADMI LLDDNFASIV TGVEEGRLIF DNLKKSIAYT
LTSNIPEISP FLLFIIANIP LPLGTVTILC IDLGTDMVPA ISLAYEAAES DIMKRQPRNP
KTDKLVNERL ISIAYGQIGM MQATAGFFTY FVILAENGFL PMDLLGIRVF WDDKYVNDLE
DSYGQQWTYE RRKIVEFTCH TAFFTSIVIV QWADLIICKT RRNSILQQGM KNRILIFGLF
EETALAAFLS YCPGMDVALR MYPLKPSWWF CAFPYSLLIF LYDEARRYIL RRNPGGWVEQ
ETYY
//
