ID A0A226E289_FOLCA Unreviewed; 1078 AA.
AC A0A226E289;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN ORFNames=Fcan01_12967 {ECO:0000313|EMBL:OXA51683.1};
OS Folsomia candida (Springtail).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC Entomobryomorpha; Isotomoidea; Isotomidae; Proisotominae; Folsomia.
OX NCBI_TaxID=158441 {ECO:0000313|EMBL:OXA51683.1, ECO:0000313|Proteomes:UP000198287};
RN [1] {ECO:0000313|EMBL:OXA51683.1, ECO:0000313|Proteomes:UP000198287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VU population {ECO:0000313|EMBL:OXA51683.1,
RC ECO:0000313|Proteomes:UP000198287};
RC TISSUE=Whole body {ECO:0000313|EMBL:OXA51683.1};
RA Faddeeva A., Derks M.F., Anvar Y., Smit S., Van Straalen N., Roelofs D.;
RT "The genome of Folsomia candida.";
RL Submitted (DEC-2015) 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}.
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:OXA51683.1}.
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DR EMBL; LNIX01000007; OXA51683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A226E289; -.
DR STRING; 158441.A0A226E289; -.
DR Proteomes; UP000198287; 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 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:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; 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 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:UP000198287};
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 147..176
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 380..405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 830..850
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 856..878
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 903..926
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 973..990
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1002..1027
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 1039..1056
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 101..175
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1078 AA; 119890 MW; 18A5498E70EFE673 CRC64;
MAQNYVNRRR QSTIVIENQD RILIPERKIS RVSFTGSDAP SRKTSTVSYK SNVDEKGTIN
PSFTSDEQSQ DQISLREVHV GHSPDIRRKS VTYIKKELEI DYHAVELGTL CNRYNSHVQL
GLTDAQAHKN RELYGKNILT PPKKTPLWIT FLHTLVGGFQ LLLWTAAILS FIAYVAQMVQ
IGDAPPDNLY LGIALSVLVL VLGLFTFYQE FSSGKVMDSF SRLVPTMATV TRDHKILLIP
ASELVVGDVV HIKLGDSIPA DIRILECQGL KVDNSSLTGE SEPQPRSPLC TDDNPMETQN
LAFFSTNALE GTGKGLVVAV GDGTFIGRIA GLTTGMNKID TPMSREVAYF VKVISFVAII
FGISFFAISL TMGYQILDAA IFLVGIIVAN VPEGLLVTFT VILALTAKRM AKKNCVVRQL
HAVETLGSCS VICSDKTGTL TQNKMTMSHI WVNNQVLDVS LGENGTLPDL EDLAGFRDLS
RAAALCSRAT FLAGQEELSI PQRLVSGDAS ESAILRFVEM SLGKVEAFRD NYPKLFEIPF
NSTNKYQLSI HKHDMTRCLV VMKGAPERVI NLCSKIRIGD KVHKMEDWKE VCIQTVDNLG
SLGERVIGFC EGELPESEYP VGYKFSAEDL TFLEGNLVLV GLGSMIDPPR PGVPNAVELC
RKAGIKVVMV TGDLPSTARA IARKVGIITP ENLTREEIAK SRNINKDDID PATCNAAVIS
GTELQELTTQ ELDWVLANHS EIVFARVSPQ QKLIIVEGFQ RLGKIVAVTG DGVNDSPALR
KADIGIAMGI SGSDVSKQAA DMILLDDNFS SIVTGVEEGR LIFENLKKCI RYLLCANTAN
LLPFLLYITL QIPLPLGTIQ MLAITLGTDI LPTISLSYEK PEGEIMIRQP RNPEKDKLVT
QQLISYAYGV IGVIEAFAGF FTYVVIMEQN GFLVKDLIDI RKQWVSSFIN DLSDSYGQEW
THQQRKELEW TCWTAYFCTI VLCQWSNLLI SKVRKDPLHR KLFDNWIVLV AIVGETAIAC
CLTYTPGLNH SLSYMPIKFV WWLTAVPFMF AIIFCDEIRR LLLRLRPNWS WYQNEFFY
//
