ID A0A670K4K1_PODMU Unreviewed; 989 AA.
AC A0A670K4K1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit alpha {ECO:0000256|RuleBase:RU362084};
GN Name=ATP12A {ECO:0000313|Ensembl:ENSPMRP00000032453.1};
OS Podarcis muralis (Wall lizard) (Lacerta muralis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Laterata;
OC Lacertibaenia; Lacertidae; Podarcis.
OX NCBI_TaxID=64176 {ECO:0000313|Ensembl:ENSPMRP00000032453.1, ECO:0000313|Proteomes:UP000472272};
RN [1] {ECO:0000313|Ensembl:ENSPMRP00000032453.1, ECO:0000313|Proteomes:UP000472272}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=30819892; DOI=10.1073/pnas.1820320116;
RA Andrade P., Pinho C., Perez I de Lanuza G., Afonso S., Brejcha J.,
RA Rubin C.J., Wallerman O., Pereira P., Sabatino S.J., Bellati A.,
RA Pellitteri-Rosa D., Bosakova Z., Bunikis I., Carretero M.A., Feiner N.,
RA Marsik P., Pauperio F., Salvi D., Soler L., While G.M., Uller T., Font E.,
RA Andersson L., Carneiro M.;
RT "Regulatory changes in pterin and carotenoid genes underlie balanced color
RT polymorphisms in the wall lizard.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:5633-5642(2019).
RN [2] {ECO:0000313|Ensembl:ENSPMRP00000032453.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362084};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR AlphaFoldDB; A0A670K4K1; -.
DR Ensembl; ENSPMRT00000034412.1; ENSPMRP00000032453.1; ENSPMRG00000017987.1.
DR GeneTree; ENSGT00940000159259; -.
DR Proteomes; UP000472272; Chromosome 15.
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:0008900; F:P-type potassium:proton transporter activity; IEA:UniProtKB-EC.
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:SF1; POTASSIUM-TRANSPORTING ATPASE ALPHA CHAIN 2; 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:UP000472272};
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 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 256..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 286..311
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 755..775
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 814..835
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 881..900
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 920..939
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT TRANSMEM 951..967
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362084"
FT DOMAIN 2..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 989 AA; 109875 MW; 4587C1C412514D12 CRC64;
CSLKKQSFIE ELEDKYGTSI TKGLPSSRAA EVLARDGPNA LTPPKSTPEI IKFLKQMVGG
FSILLWIGAI LCWIAFGIQH FADNILLETS FHHSALPRSG PCTGGCPHWM FAYYQEAKST
NIMASFGKMI PQRALVLRDA EKKDISAEEL VVGDIVEIKG GDRIPADIRI ITSQGCKVDN
SSLTGESEPQ SRSCEYTHEN PLETKNIAFY STTCLEGTAT GMVINTGDNT IIGRIASLAS
GVGNEKTPIA IEIEHFVHIV AAVAISIGVV FFIISVSMKY TVMKAIIFLI GIIVANVPEG
LLATVTVTLS LTAKRMAKKN CLVKNLEAVE TLGSTSVICS DKTGTLTQNR MTVAHLWFDN
EIFSADTSEN QTTQTFDQTS GTWTALSRIV ALCNRAEFRP GQDSEPIMKR IVVGDASETA
LLKFSEVVMG NIMDIRKRNR KVTEIPFNST NKFQLSIHET EDPNDKRFLL VMKGAPERIL
EKCSTIMING KEEPLDAERK EAFQTAYMAL GGMGERVLGF CHLYLPEEEF PDTYPFDTDS
MNFPTSNLCF VGLLSMIDPP RSTVPDAVIK CRSAGIKVIM VTGDHPITAK AIAKSVGIIS
ANSETVEDIA QRLKIPVEQV NRSDARAAVV NGMELKDMTS EQLDDILRNH SEIVFARTSP
QQKLIIVEGC QRQDAVVAVT GDGVNDSPAL KKADIGIAMG IAGSDAAKNA ADMVLLDDNF
ASIVTGVEEG RLIFDNLKKT IAYTLTKNIA ELCPFLIYIM ASIPLPIGTI TILFIDLGTD
IIPSVSLAYE KAESDIMKRK PRHKKKDRLV NQELVTYSYL QIGLLQTIGA FLTYFTVYAQ
QGWLPHTLLH IRTSWEDPFI NDLEDSYGQE WTFDQRQILE YHGYTAFFVS ITIEQVADLI
IRKTRRNSIF QQGLFRNKVI WVGIFSQIGI AAILCYGLGS VYALNFAPLR FQYWFVAVPF
AILIWVYDEF RKLFIRRYPG SWWDKNMYY
//
