AT12A_RHIMB
ID AT12A_RHIMB Reviewed; 1042 AA.
AC Q92036;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Potassium-transporting ATPase alpha chain 2;
DE EC=7.2.2.19;
DE AltName: Full=Non-gastric H(+)/K(+) ATPase subunit alpha;
DE AltName: Full=Proton pump;
GN Name=ATP12A;
OS Rhinella marina (Cane toad) (Bufo marinus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Hyloidea; Bufonidae; Rhinella.
OX NCBI_TaxID=8386;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Urinary bladder urothelium;
RX PubMed=8253841; DOI=10.1083/jcb.123.6.1421;
RA Jaisser F., Horisberger J.-D., Geering K., Rossier B.C.;
RT "Mechanisms of urinary K+ and H+ excretion: primary structure and
RT functional expression of a novel H,K-ATPase.";
RL J. Cell Biol. 123:1421-1429(1993).
CC -!- FUNCTION: Catalyzes the hydrolysis of ATP coupled with the exchange of
CC H(+) and K(+) ions across the plasma membrane. Responsible for
CC potassium absorption in various tissues.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+)(in) + H2O + K(+)(out) = ADP + 2 H(+)(out) +
CC K(+)(in) + phosphate; Xref=Rhea:RHEA:22044, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.19;
CC -!- SUBUNIT: Composed of two subunits: alpha (catalytic) and beta.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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 EMBL; Z25809; CAA81058.1; -; mRNA.
DR PIR; I50099; I50099.
DR AlphaFoldDB; Q92036; -.
DR SMR; Q92036; -.
DR PRIDE; Q92036; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR030318; Atp12a.
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 PANTHER; PTHR43294:SF1; PTHR43294:SF1; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR SUPFAM; SSF81653; SSF81653; 1.
DR SUPFAM; SSF81660; SSF81660; 1.
DR SUPFAM; SSF81665; SSF81665; 1.
DR TIGRFAMs; TIGR01106; ATPase-IIC_X-K; 1.
DR TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Hydrogen ion transport; Ion transport; Magnesium; Membrane;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Potassium;
KW Potassium transport; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..1042
FT /note="Potassium-transporting ATPase alpha chain 2"
FT /id="PRO_0000046264"
FT TOPO_DOM 1..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..149
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..306
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..338
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 357..790
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 791..810
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 811..820
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..861
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 862..884
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 885..936
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 937..956
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 957..970
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 971..989
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 990..1004
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1005..1025
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1026..1042
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 735
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 739
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 961
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1042 AA; 115349 MW; 92AED15486957B94 CRC64;
MGTEANSDVY STAINGINEI GYPDKEKEED LGLEVQKKKE KKQKKKKGKN VDDLKQELDL
EDHKLSIEEL EAKYETSLQG LTSARAAEIL ARDGPNTLTP PKGTPEIIKF LKQMIGGFSL
LLWAGAILCW IAYGILYAQD HNTSRDNLYL GIVLAVVVIL TGCFAYFQEA KSTNIMASFN
QMIPQQAVVT RNGQKLEIPA KDLVVGDLVD VKGGDRIPAD LRIIFAQGCK VDNSSLTGES
EAQPRSSEFT HENPLETKNI AFYSTTCLEG TARGFVINTG DQTIIGRIAS LASGVGNEKT
PIAVEIEHFV HIVAGVAVSV GVLFFIIAIC MGYSALNSII FLIGIIVANV PEGLLATVTV
TLSLTAKRMA KKNCLVKNLE AVETLGSTSI ICSDKTGTLT QNRMTVAHLW FDDHIHIADT
SEDQSHHSFE QTPETWNALC KIVSLCNRAE FKAGQDDVPI MKKVAVGDAS ETALLKFSEV
ITGNVMNIRS QNRKVCEIPF NSTNKFQLSI HETDDPQDQR LLLVMKGAPE RILEKCSTIM
IGGKELPLDE SMKDSFQTAY MELGGLGERV LGFCHLYLPE EEYPSSYAFD IESMNFPTSN
LCFVGLLSMI DPPRSTVPDA VTKCRSAGIK VIMVTGDHPI TAKAIARSVG IISAGSETVD
DIAKRLNIPV EQVNKREAKA AVVNGGELKD MSSEELDDIL TNHAEIVFAR TSPQQKLIIV
EGCQRQNYVV AVTGDGVNDS PALKKADIGI AMGIAGSDAA KNAADMILLD DNFASIVTGV
EEGRLIFDNI KKSIGYTLTK NVAELCPFLI YIIADIPLPI GTITILFIDL GTDIIPSVSF
AYEKAERDIM NRKPRRKNVD RLVNQQLALY AYLQIGIIQS VGAFLNYFTV MAEQGFLPHT
LVGIRIDWEK INNQDLEDSY GQEWTFSQRQ FLEWTGYTAF FVSIVVEQLA DLIIRKTRRN
SVFQQGLFRN KFLLMGLASQ VIIAAFLSYC PEMPYALKFT PLRAQYWFVA APYALLIFVY
DEIRKLFIRR YPGSWWDKNM YY
