AT12A_CAVPO
ID AT12A_CAVPO Reviewed; 1033 AA.
AC Q64392;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
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; Synonyms=ATP1AL1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley;
RA Watanabe T., Sato M., Kaneko K., Suzuki T., Yoshida T., Suzuki Y.;
RT "Isolation and characterization of cDNA encoding the putative guinea pig
RT distal colon H+, K+ -ATPase alpha subunit.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=9872395; DOI=10.1016/s0014-5793(98)01483-5;
RA Pestov N.B., Romanova L.G., Korneenko T.V., Egorov M.V., Kostina M.B.,
RA Sverdlov V.E., Askari A., Shakhparonov M.I., Modyanov N.N.;
RT "Ouabain-sensitive H,K-ATPase: tissue-specific expression of the mammalian
RT genes encoding the catalytic alpha subunit.";
RL FEBS Lett. 440:320-324(1998).
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 -!- TISSUE SPECIFICITY: Found in skin, kidney and distal colon.
CC {ECO:0000269|PubMed:9872395}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIC subfamily. {ECO:0000305}.
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DR EMBL; D21854; BAA04880.1; -; mRNA.
DR RefSeq; NP_001166387.1; NM_001172916.1.
DR AlphaFoldDB; Q64392; -.
DR SMR; Q64392; -.
DR STRING; 10141.ENSCPOP00000003081; -.
DR PRIDE; Q64392; -.
DR Ensembl; ENSCPOT00000003451; ENSCPOP00000003081; ENSCPOG00000003407.
DR GeneID; 100135482; -.
DR KEGG; cpoc:100135482; -.
DR CTD; 479; -.
DR eggNOG; KOG0203; Eukaryota.
DR GeneTree; ENSGT00940000159259; -.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; Q64392; -.
DR OMA; NNVMGCV; -.
DR OrthoDB; 388324at2759; -.
DR TreeFam; TF312838; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000003407; Expressed in zone of skin and 3 other tissues.
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; Reference proteome; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1033
FT /note="Potassium-transporting ATPase alpha chain 2"
FT /id="PRO_0000046259"
FT TOPO_DOM 1..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118..140
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 162..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..317
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..329
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..347
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..781
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 782..801
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 802..811
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 833..852
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 853..875
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 876..927
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 928..947
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 948..961
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 962..980
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 981..995
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 996..1016
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1017..1033
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT ACT_SITE 385
FT /note="4-aspartylphosphate intermediate"
FT /evidence="ECO:0000250"
FT BINDING 726
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 730
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MOD_RES 952
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1033 AA; 114557 MW; C4EEE72D83C1F40C CRC64;
MRRKTLEIYS VELDGTKDTK QLGQEEGKKC NELDLKKSSQ KEELKKELDL DDHKLTSEEL
EQKYGTNIIR GLSSTRAAEL LARDGPNALS PPKQTPEIIK FLKQMIGGFS ILLWVGAILC
WIAYGIQYAS NQSGSLDNVY LGVVLALVVI LTGIFAYYQE AKSTNIMSSF SKMIPQEALV
TRDAEKKVIP AEQLVVGDIV EIKGGDQIPA DIRLLFSQGC KVDNSSLTGE SEPQPRSAEF
THENPLETKN IAFYSTTCLE GTATGMVINT GDRTIIGRIA SLASGVGNEK TPIATEIEHF
VHIVAGVAVS IGILFFIIAV SLKYRVLDSI IFLIGIIVAN VPEGLLATVT VTLSLTAKRM
AKKNCLVKNL EAVETLGSTS VICSDKTGTL TQNRMTVAHL WFDSQIFTAD TSESQSNQAF
DQSSGTWASL SKIIALCNRA EFRPGQENVP IMKRVVVGDA SETALLKFSE VILGDVMEIR
KRNRKVAEIP FNSTNKFQLS IHETEDPGDP RFLMVMKGAP ERILEKCSTI MINGQEQPLD
KNNANAFHTA YMELGGMGER VLGFCHLYLP AHEFPENYSF DVDTMNFPTS NLCFVGLLSM
IDPPRSTVPD AVAKCRSAGI KVIMVTGDHP ITAKAIAKSV GIISANSETV EDIAKRCNIA
VEQVNKQDAR AAVVTGMELK DMTPEQLDEI LANYPEIVFA RTSPQQKLII VEGCQRQNAV
VAVTGDGVND SPALKKADIG IAMGIAGSDA AKNAADMVLL DDNFASIVTG VEEGRLIFDN
LKKTIAYTLT KNIAELCPFL VYIIVGLPLP IGTITILFID LGTDIIPSIA LAYEKVESDI
MNRKPRHKKK DRLVNHQLAI YSYLHIGLMQ ALGAFLVYFT VYAQQGFWPT SLIQLRVKWE
QDYVNDLEDS YGQQWTRYQR KYLEWTGYTA FFVGIMVQQI ADLIIRKTRR NSIFQQGLFR
NKVIWVGITS QIIVALILSC GLGSITALNF TMLRVQYWFV AVPHAILIWV YDEVRKLFLR
LYPGSWWDKN MYY
