ID G3TVH2_LOXAF Unreviewed; 861 AA.
AC G3TVH2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Potassium-transporting ATPase alpha chain 1 {ECO:0000256|ARBA:ARBA00022094};
DE EC=7.2.2.19 {ECO:0000256|ARBA:ARBA00012803};
DE AltName: Full=Gastric H(+)/K(+) ATPase subunit alpha {ECO:0000256|ARBA:ARBA00029571};
DE AltName: Full=Proton pump {ECO:0000256|ARBA:ARBA00031813};
GN Name=ATP4A {ECO:0000313|Ensembl:ENSLAFP00000019580.1};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000019580.1, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000019580.1, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019580.1,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000019580.1}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000019580.1};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR STRING; 9785.ENSLAFP00000019580; -.
DR Ensembl; ENSLAFT00000030397.1; ENSLAFP00000019580.1; ENSLAFG00000031203.1.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000160297; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; G3TVH2; -.
DR OMA; PVQKDCD; -.
DR TreeFam; TF312838; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008900; F:P-type potassium:proton transporter activity; IEA:Ensembl.
DR GO; GO:0045851; P:pH reduction; IEA:Ensembl.
DR GO; GO:0010155; P:regulation of proton transport; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
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; 2.
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; 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; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF10; POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 1; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Potassium {ECO:0000256|ARBA:ARBA00022958};
KW Potassium transport {ECO:0000256|ARBA:ARBA00022538};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..647
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 792..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..85
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 861 AA; 95143 MW; 51C388437F6AC59B CRC64;
LENMKKEMEI NDHQLSVAEL EQKYQTSATK GLSASLAAEL LLRDGPNALR PPRGTPEYVK
FARQLAGGLQ CLMWVAAAIC LIAFAIQASE GDLTTDDNLY LALALIAVVM VTGCFGYYQE
FKSTNIIASF KNLVPQQATV IRDGDKCQIN ADQLVVGDLV EMKGGDRVPA DIRILAAQGC
KVDNSSLTGE SEPQTRSPEC THESPLETRN IAFFSTMCLE GTAQGLVVNT GDRTIIGRIA
SLASGVENEK TPIAIEIEHF VDIIAGLAIL FGATFFVVAM CIGYTFLRAM VFFMAIVVAY
VPEGLLATVT VRWGAEEGGR ELRGXPTLNT DLPTYSPPDF PRPDLTCDPA IFSQRLPQLT
PFKTASCLTF PILVLTPDLP QFLSPLCFLL GFCQLYLSEK DYPPGYAFDV EDMNFPTSSL
CFAGLVSMID PPRATVPDAV LKCRTAGIRV IMVTGDHPIT AKAIASSVGI ISEGSETVED
IAARLRVPVD QVNHKDARAC VISGMQLKDM DPSELVEALR THPEMVFART SPQQKLVIVE
SCQRLGAIVA VTGDGVNDSP ALKKADIGVA MGIAGSDAAK NAADMILLDD NFASIVTGVE
QGRLIFDNLK KSIAYTLTKN IPELTPYLIY ITVSVPLPLG CITILFIELC TDIFPSVSLA
YEKAESDIMH LRPRNPKRDR LVNEPLAAYS YFQIGAIQSF AGFTDYFTAM AQEGWFPLLC
VGLRPQWEDH HLQDLQDSYG QEWTFGQRLY QQYTCYTVFF ISIEVCQIAD VLIRKTRRLS
AFQQGFFRNR ILVIAIVFQV CIGCFLCYCP GMPNIFNFMP IRYQWWLVPL PYGILIFVYD
ELRKLGVRCC PGSWWDQELY Y
//